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The study of biological sciences at St. Mary's University includes a broad-based curriculum and extensive scientific training designed to prepare well-rounded health care professionals. Students develop written and oral communication skills, critical thinking and analytical skills, and an understanding and respect for ethical and moral concerns. Because our students display competence, dedication and compassion, they are readily accepted into graduate programs, the health professions, biomedical research and teaching fields.
The program in biological sciences is built upon a rigorous study of biology and includes courses in chemistry, physics and mathematics that satisfy professional school entrance requirements.
Advanced biology electives include anatomy, general physiology, microbiology, genetics, embryology, endocrinology, cell biology, neurophysiology, comparative physiology, recombinant DNA technology, advanced nutrition and metabolism, immunology, medical microbiology and molecular biology. The final year includes a two-semester biochemistry course. Many biology majors also choose to minor in chemistry.
210-431-4321
traabe@stmarytx.edu
The program in biological sciences is built upon a rigorous study of biology and includes courses in chemistry, physics and mathematics that satisfy professional school entrance requirements.
Advanced biology electives include anatomy, general physiology, microbiology, genetics, embryology, endocrinology, cell biology, neurophysiology, comparative physiology, recombinant DNA technology, advanced nutrition and metabolism, immunology, medical microbiology and molecular biology. The final year includes a two-semester biochemistry course. Many biology majors also choose to minor in chemistry.
Contact Us
Timothy Raabe, Ph.D.210-431-4321
traabe@stmarytx.edu
Program Highlights
Students in the biological sciences program have been accepted into numerous internship and summer programs at universities around the country, including Columbia University, Cornell University, Harvard University, Loyola University, Massachusetts Institute of Technology, Southwest Research Institute, Texas A&M University and the University of Michigan.Students can apply for admission to cooperative partnership programs with The University of Texas Health Science Center at San Antonio in the following fields of study: clinical laboratory sciences, respiratory care, physical therapy, occupational therapy, nursing, medicine, dentistry and physician assistant.
Research Laboratories
The Department of Biological Sciences is housed in the Moody Life Sciences Building, which includes faculty offices, lecture and seminar facilities, research labs, a recently renovated animal facility, a stock room, a large laboratory for introductory classes, four laboratories for advanced courses and a computer laboratory.The department is well supplied with modern equipment essential for studies in cell and molecular biology, microbiology, immunology and biochemistry.
Two of the advanced labs and the computer lab were constructed in 1996 as part of a suite of labs and support facilities using funding from the Howard Hughes Medical Institute. Much of the department's instrumentation and equipment has been purchased in the last few years, using University resources as well as funding from the National Science Foundation and the Howard Hughes Medical Institute.
Available instrumentation and equipment includes: U.V. trans-illuminators and digital- and photo-documentation systems; DNA amplification and sequencing apparatus; Micro-centrifuges; Heated water baths; A DNA hybridization oven; A Class II bio-safety hood; A variety of vertical and horizontal gel electrophoresis systems; An autoclave; A computer operated micro-titer plate reader; Bioresearch grade water purification systems; Two high speed refrigerated centrifuges and assorted rotors; Walk-in refrigerated and heated environmental chambers; Shaking water baths; A refrigerated water bath; -70 and -20 freezers; Tissue culture and bacteriological incubators; Liquid scintillation and gamma counters; Several U.V. scanning spectrophotometers, Digital analytical balances; Electrophoresis equipment and power supplies; epi-fluorescence and visible light microscopes; A video microscopy workstation.
Students in our advanced courses use recently purchased Nikon Alphaphot2 microscopes. In addition, the computer lab used by faculty and students houses 13 Macintosh PowerPC computers. These computers are used for research and course work, and they all have Internet access.
Student Organizations
There are currently four registered student organizations within the department of Biological Sciences. These organizations serve multiple purposes within and outside of the department: they allow students to associate with others who are pursuing similar career goals; they help keep students informed of programs, opportunities, and events within their major and career path; they allow students to meet and network with professionals in career fields which they are interested; and they provide service to the St. Mary s and San Antonio community in the Marianist tradition.MARC U*STAR
The Minority Access to Research Careers (MARC) Undergraduate Student Training in Academic Research (U*STAR) is sponsored by the National Institute of General Medical Sciences (NIGMS). MARC U*STAR provides underrepresented students majoring in biology, biochemistry, chemistry, physics or engineering science opportunities to complete research training and work alongside faculty mentors in the biomedical sciences. Undergraduate students participating in the MARC U*STAR program are provided with academic and research support to prepare them for Ph.D. programs in the biomedical sciences.Facilitated Admissions for South Texas Scholars (FASTS) Program
FASTS is a joint program between the University of Texas School of Medicine at San Antonio and St. Mary's University.Click for more info
Objectives
- Allow students with academic excellence and a demonstrated interest in medicine to receive early acceptance to the University of Texas School of Medicine at San Antonio (UTSOMSA).
- Provide students with a rigorous academic preparation for medical school.
- Provide students with academic enrichment and clinical experiences provided through the Summer Premedical Academy at the School of Medicine, as well as MCAT preparation.
Eligibility and Program Details
- Academically outstanding first year students who plan to study medicine and currently attend St. Mary's University will be eligible for this program.
- In the spring of their freshman year, students will be encouraged to apply for acceptance into the FASTS program.
- Following completion of the application, a committee of St. Mary's faculty, the St. Mary's Premedical Advisor, and the St. Mary's FASTS Coordinator, as well as UTSOMSA faculty/staff will select students for an interview.
- Interviews will be conducted at UTSOMSA during the spring to determine if the applicant possesses the academic abilities and personal qualities that predict success as a medical student and physician.
- The decision to accept a student into FASTS will be made solely by the Admissions Committee of the School of Medicine.
- The student must be a United States Citizen or a permanent resident and a Texas resident.
- Application deadline will be February 1 every year.
- In addition to academic enrichment and clinical experiences at UTSOMSA, students will be offered tutoring and academic counseling at St. Mary's during the school year.
Acceptance Requirements
- Successful completion of the program requires the participant to complete a Bachelor s Degree at St. Mary s University with an overall GPA and a science GPA of at least 3.25. AP coursework will NOT be considered fulfillment of science requirements.
- In the spring of their junior year, qualified participants who meet the premedical coursework requirements will take the MCAT and those who obtain a ratio of science GPA/MCAT scores of 3.25/28, 3.5/26 or 3.75/24 or better will be eligible for acceptance to medical school following an interview by the admissions committee. In addition, participants cannot have a score less than a 7 on any sub-section of the MCAT.
- Participants must satisfy all requirements of the Texas Medical and Dental Schools Application Service (TMDSAS) application process including a letter of recommendation from the Pre-Professional Health Advisory Committee at St. Mary s, have record of ethical behavior while a pre-medical student, and demonstrate a continuing commitment to study medicine.
- While the coursework typically is completed within a four-year period, an exceptional student may request to apply after three years to the Associate Dean for Admission at the School of Medicine.
FASTS Forms
Joint Admission Medical Program (JAMP)
The Joint Admission Medical Program (JAMP) is a special program created by the Texas Legislature to support and encourage highly qualified, economically disadvantaged students pursuing a medical education. Dr. Tim Raabe is the JAMP Faculty Director at St. Mary's University.JAMP "Pathways Into Medicine" Pre-Medical Summer Camp
In 2010, the St. Mary's University Department of Biological Sciences received funding to hold its first pre-medical summer camp. The "Pathways Into Medicine" summer camp is funded by JAMP and has two goals: (1) Recruit and educate potential JAMP students about the JAMP program and the opportunities it provides, and (2) Present students with a unique, hands-on experience with healthcare professionals in a medical school environment.
Learn more
Camp Summary
For five nights, campers stay in residence hall facilities at St. Mary s University and spend their days at the University of Texas Health Science Center at San Antonio (UTHSCSA) School of Medicine.Each day, camp begins with breakfast after which students are transported from St. Mary s to UTHSCSA where they participate in a myriad of activities alongside medical and healthcare professionals.
Some of the activities include:
- Presentations on topics such as the JAMP program, medical school admission, plastic surgery, ethics in medicine, psychiatry, emergency medicine, pediatrics and more
- Hands-on laboratory activities including exploring the human brain, learning the art of suturing and practicing dissections
- Guided tours of University Hospital, UTHSCSA Medical School , and the Gamma Knife Center
- Panel discussion with current JAMP medical students
- Handling and examining plastinated human body parts provided through the Willed Body Program at UTHSCSA
- Special access to the Johnson Center for Surgical Innovation where students participate in hands-on training sessions for various surgical procedures
- Personal discussion with LifeFlight medics along with a tour of the LifeFlight helicopter and landing pad
Camp closes with a special ceremony which parents are invited to attend. Students are presented with a certificate of completion at the closing ceremony, and parents enjoy a slideshow giving them a peek into the week's activities .
Current Faculty Research
Professors never stop learning. In addition to teaching, advising, grading papers and serving on committees, the Biological Sciences faculty are looking for answers to tough questions in their field. Here's a sampling of what they're currently learning.Veronica Contreras-Shannon, Ph.D.
"The Molecular Mechanisms of Antipsychotic-Induced Metabolic Syndrome"Read about it
My teaching and research interests focus on the molecular mechanisms of disease. For the past several years, I have been involved in research investigating the role of specific genes and their protein products, as well as inflammation, in cardiovascular disease, muscle regeneration and cancer. My current work in understanding the mechanism of metabolic side effects associated with atypical antipsychotics with undergraduate students is an appropriate confluence of my doctoral training in metabolic enzymes and mitochondrial function, and my postdoctoral training in the pathobiology of disease.
The underlying biological cause of the associated side-effects of atypical antipsychotics is unknown. It is interesting to note that there is a growing consensus in the obesity field that understanding the mechanisms responsible for the adverse metabolic effects of atypical antipsychotics may shed an important light on the origin of metabolic disease and obesity in the general population. In my research, we use cultured mammalian cells and a yeast model system to test three interrelated hypotheses for why these drugs cause metabolic side effects: 1) these drugs negatively affect the proper functioning of mitochondria and/or the endoplasmic reticulum (ER), 2) these drugs cause increased oxidative stress in cells and tissues, and 3) these drugs promote inflammation.
In addition to clarifying the mechanism of antipsychotic-induced side effects, my goal is to actively involve undergraduates in cutting-edge biomedical research as a means to improve biology training and increase the number of underrepresented students in the sciences.
Current research students:
Herenia Armenta-Espitia, sophomore chemistry major (pre-MARC)
Dina Attia, junior biology major (Biaggini)
Janet Chen, senior biology major (Honor's Thesis)
Andrew Gonzales, junior biology major (Biaggini)
Uche Ozoemena, junior biochemistry major (Biaggini)
Recent publications: (St. Mary's student names are underlined)
Contreras-Shannon V, Heart D, Navaira E, Paredes M, Catano G, Maffi S and Walss-Bass C. Clozapine-induced mitochondria alterations and inflammation in brain and insulin-responsive cells. Submitted to the journal PLOS ONE.
Shireman PK, Contreras-Shannon V, Ochoa O, Karia BP, Michalek JE, McManus LM. MCP-1 deficiency causes altered inflammation with impaired skeletal muscle regeneration. J Leukoc Biol 2007 Mar;81(3):775-785.
Contreras-Shannon V, Ochoa O, Reyes-Reyna SM, Sun D, Michalek JE, Kuziel WA, McManus LM, Shireman PK. Fat accumulation with altered inflammation and regeneration in skeletal muscle of CCR2-/- mice following ischemic injury. Am J Physiol Cell Physiol 2007 Feb;292(2):c953-c967.
Shireman PK, Contreras-Shannon V, Reyes-Reyna SM, Robinson SC, McManus LM. MCP-1 parallels inflammatory and regenerative responses in ischemic muscle. J Surg Res 2006 Jul;134(1):145-157.
Contreras-Shannon V, Lin AP, McCammon MT, McAlister-Henn L.. Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+-specific isocitrate dehydrogenases. J Biol Chem 2005 Feb;280(6):4469-4475.
The underlying biological cause of the associated side-effects of atypical antipsychotics is unknown. It is interesting to note that there is a growing consensus in the obesity field that understanding the mechanisms responsible for the adverse metabolic effects of atypical antipsychotics may shed an important light on the origin of metabolic disease and obesity in the general population. In my research, we use cultured mammalian cells and a yeast model system to test three interrelated hypotheses for why these drugs cause metabolic side effects: 1) these drugs negatively affect the proper functioning of mitochondria and/or the endoplasmic reticulum (ER), 2) these drugs cause increased oxidative stress in cells and tissues, and 3) these drugs promote inflammation.
In addition to clarifying the mechanism of antipsychotic-induced side effects, my goal is to actively involve undergraduates in cutting-edge biomedical research as a means to improve biology training and increase the number of underrepresented students in the sciences.
Current research students:
Herenia Armenta-Espitia, sophomore chemistry major (pre-MARC)
Dina Attia, junior biology major (Biaggini)
Janet Chen, senior biology major (Honor's Thesis)
Andrew Gonzales, junior biology major (Biaggini)
Uche Ozoemena, junior biochemistry major (Biaggini)
Recent publications: (St. Mary's student names are underlined)
Contreras-Shannon V, Heart D, Navaira E, Paredes M, Catano G, Maffi S and Walss-Bass C. Clozapine-induced mitochondria alterations and inflammation in brain and insulin-responsive cells. Submitted to the journal PLOS ONE.
Shireman PK, Contreras-Shannon V, Ochoa O, Karia BP, Michalek JE, McManus LM. MCP-1 deficiency causes altered inflammation with impaired skeletal muscle regeneration. J Leukoc Biol 2007 Mar;81(3):775-785.
Contreras-Shannon V, Ochoa O, Reyes-Reyna SM, Sun D, Michalek JE, Kuziel WA, McManus LM, Shireman PK. Fat accumulation with altered inflammation and regeneration in skeletal muscle of CCR2-/- mice following ischemic injury. Am J Physiol Cell Physiol 2007 Feb;292(2):c953-c967.
Shireman PK, Contreras-Shannon V, Reyes-Reyna SM, Robinson SC, McManus LM. MCP-1 parallels inflammatory and regenerative responses in ischemic muscle. J Surg Res 2006 Jul;134(1):145-157.
Contreras-Shannon V, Lin AP, McCammon MT, McAlister-Henn L.. Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+-specific isocitrate dehydrogenases. J Biol Chem 2005 Feb;280(6):4469-4475.
S. Colette Daubner, Ph.D.
"Structural basis for regulation of enzymes of neurotransmitter synthesis"Read about it
My group studies the aromatic amino acid hydroxylases. Phenylalanine hydroxylase (PheH) and tyrosine hydroxylase (TyrH). are structurally and functionally related, and genetic analysis reveals that TyrH evolved from PheH about 750 million years ago. They do similar chemistry, using iron and reduced biopterin to incorporate an atom of oxygen into the aromatic ring of an amino acid. PheH is a liver enzyme, and regulates levels of phenylalanine degradation, and hereditary deficiencies of PheH cause phenylketonuria, a disease resulting in mental retardation; TyrH is a nervous system enzyme and regulates levels of the catecholamine neurotransmitters dopamine, epinephrine, and norepinephrine.
We study the chemical and structural differences between the two enzymes that give them their unique substrate specificities. We have identified several amino acids that were critical to the evolution of TyrH; as TyrH regulates neurotransmitter synthesis, this evolutionary step was key for the formation of nervous systems in organisms with catecholaminergic neural tracts. We also study the regulation of PheH and TyrH. They are both regulated by phosphorylation at the end of cellular signal tranduction pathways. We study the conformational changes that result upon phosphorylation. PheH is also regulated by allosteric activation with phenylalanine, and TyrH is regulated by feedback inhibition by the catecholamines; we study the biochemical and biophysical bases for these processes. We use a number of techniques in our lab, including stopped-flow spectrophotometry, fluorimetry, enzyme kinetics, and protein chemistry; we perform site-directed mutagenesis of our enzymes using DNA techniques.
Fig. 1. Similarities and differences between phenylalanine hydroxylase (left) and tyrosine hydroxylase (right). The peptide backbones of the two enzymes, known from x-ray crystallography, are represented as ribbon structures. Their similarity is obvious. Their active sites are portrayed with several amino acids, drawn as stick figures, bound to the active site iron. The large spheres at upper left of each protein accentuate a flexible loop that is very different between the two enzymes. These loops affect catalysis and substrate specificity.
Fig. 2. Both tyrosine and phenyalanine hydroxylase are activated by phosphorylation. This figure presents a model for the conformational change that causes the activation. Each enzyme consists of two domains, one regulatory (R), and one catalytic (C). When a serine residue in the R domain becomes phosphorylated through the action of a protein kinase, the R domain moves with respect to the C domain and allows substrates freer access to the active sites.
Current research students:
Audrey Avila, senior biology major (UTHSCSA R25 neuroscience program student)
Andrew Hansen, senior biochemistry major (MARC)
Jessica Villacorta, junior biochemistry major (MARC)
Ewa Nowara, sophomore biophysics major
Recent publications: (students' names are underlined)
Tormos, Jose R., Taylor, Alex, Daubner, S. Colette, Hart, P. John, and Fitzpatrick, Paul F. (2010), Identification of a Hypothetical Protein from Podospora anserina as a Nitroalkane Oxidase Biochemistry 49, 5035-41.
Daubner, S. Colette, Le, Tiffany, and Wang, Shanzhi (2010), The R Domain of Tyrosine Hydroxylase and Regulation of Dopamine Synthesis. Arch. Biochem. Biophys. 508, 1-12.
Li J, Ilangovan U., Daubner, S. Colette, Hinck Andrew P., Fitzpatrick Paul F. (2011), Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. Arch. Biochem. Biophys. 505, 250-5.
Wang, Shanzhi, Lasagna, Mauricio, Daubner, S. Colette, Reinhart, Gregory, and Fitzpatrick, Paul F. (2011), Effect of Phosphorylation of Tyrosine Hydroxylase on the Dynamics of the Regulatory Domain, Biochemistry 50, 2364-70.
Avila, Audrey M., Bailey, Johnathan, Barrera, Dimitrios, Bermudez, Jacklyn Y., Fitzpatrick, Paul F., Giles, David, Khan, Crystal A., Oxley, Susan, Shaheen, Noel, Vasquez, Jessica, Thompson, Janie, and Daubner, S Colette. Evolution of Tyrosine Hydroxylase: Substitutions at Position 425 Delineate Active Site Requirements for Tyrosine versus Phenylalanine Hydroxylation, manuscript in preparation.
We study the chemical and structural differences between the two enzymes that give them their unique substrate specificities. We have identified several amino acids that were critical to the evolution of TyrH; as TyrH regulates neurotransmitter synthesis, this evolutionary step was key for the formation of nervous systems in organisms with catecholaminergic neural tracts. We also study the regulation of PheH and TyrH. They are both regulated by phosphorylation at the end of cellular signal tranduction pathways. We study the conformational changes that result upon phosphorylation. PheH is also regulated by allosteric activation with phenylalanine, and TyrH is regulated by feedback inhibition by the catecholamines; we study the biochemical and biophysical bases for these processes. We use a number of techniques in our lab, including stopped-flow spectrophotometry, fluorimetry, enzyme kinetics, and protein chemistry; we perform site-directed mutagenesis of our enzymes using DNA techniques.
Fig. 1. Similarities and differences between phenylalanine hydroxylase (left) and tyrosine hydroxylase (right). The peptide backbones of the two enzymes, known from x-ray crystallography, are represented as ribbon structures. Their similarity is obvious. Their active sites are portrayed with several amino acids, drawn as stick figures, bound to the active site iron. The large spheres at upper left of each protein accentuate a flexible loop that is very different between the two enzymes. These loops affect catalysis and substrate specificity.
Fig. 2. Both tyrosine and phenyalanine hydroxylase are activated by phosphorylation. This figure presents a model for the conformational change that causes the activation. Each enzyme consists of two domains, one regulatory (R), and one catalytic (C). When a serine residue in the R domain becomes phosphorylated through the action of a protein kinase, the R domain moves with respect to the C domain and allows substrates freer access to the active sites.
Current research students:
Audrey Avila, senior biology major (UTHSCSA R25 neuroscience program student)
Andrew Hansen, senior biochemistry major (MARC)
Jessica Villacorta, junior biochemistry major (MARC)
Ewa Nowara, sophomore biophysics major
Recent publications: (students' names are underlined)
Tormos, Jose R., Taylor, Alex, Daubner, S. Colette, Hart, P. John, and Fitzpatrick, Paul F. (2010), Identification of a Hypothetical Protein from Podospora anserina as a Nitroalkane Oxidase Biochemistry 49, 5035-41.
Daubner, S. Colette, Le, Tiffany, and Wang, Shanzhi (2010), The R Domain of Tyrosine Hydroxylase and Regulation of Dopamine Synthesis. Arch. Biochem. Biophys. 508, 1-12.
Li J, Ilangovan U., Daubner, S. Colette, Hinck Andrew P., Fitzpatrick Paul F. (2011), Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. Arch. Biochem. Biophys. 505, 250-5.
Wang, Shanzhi, Lasagna, Mauricio, Daubner, S. Colette, Reinhart, Gregory, and Fitzpatrick, Paul F. (2011), Effect of Phosphorylation of Tyrosine Hydroxylase on the Dynamics of the Regulatory Domain, Biochemistry 50, 2364-70.
Avila, Audrey M., Bailey, Johnathan, Barrera, Dimitrios, Bermudez, Jacklyn Y., Fitzpatrick, Paul F., Giles, David, Khan, Crystal A., Oxley, Susan, Shaheen, Noel, Vasquez, Jessica, Thompson, Janie, and Daubner, S Colette. Evolution of Tyrosine Hydroxylase: Substitutions at Position 425 Delineate Active Site Requirements for Tyrosine versus Phenylalanine Hydroxylation, manuscript in preparation.
Ahmad Galaleldeen, Ph.D.
"Understanding Pathogenesis through Structural Biology"Read about it
Project 1:
Chlamydia is a genus of gram negative intracellular pathogens that cause various health problems in humans. C. trachomatis infection of the urinogenital tract is the most common sexually transmitted bacterial disease in the world, while ocular infections cause trachoma, potentially leading to blindness. C. pneumoniae is a common cause of pneumonia and often associated with atherosclerosis and coronary artery disease. The nature of Chlamydia as an intracellular pathogen and its presence in cellular inclusions presents a challenge for researchers. The lack of tools for genetic manipulation of Chlamydia has hindered this research and little is known about the molecular mechanism(s) through which Chlamydia interacts with the host cell and manipulates its cell signaling and immune response. Structural biology is an emerging tool that can be used to overcome the difficulties of genetic manipulation and allow us to determine the functions of chlamydial proteins. We are interested in identifying, characterizing and determining the 3D structure of various effector proteins secreted by Chlamydia in the host cell.
Project 2:
Superoxide dismutases (SODs) are a family of metallo-enzymes that protect cells from oxidative damage caused by reactive oxygen species (ROS). ROS are produced as a direct result of aerobic respiration and photosynthesis and if not detoxified, can exert damaging effects via oxidation of DNA, proteins and lipids. Four distinct classes of SOD have been identified based on the identity of the redox-active metal ions bound as cofactors at the active site, which include nickel, iron, manganese, and copper/zinc. We are interested in characterizing SODs from different species and understanding the activation, i.e. metallation and disulfide bond formation, process of these enzymes.
Figure 1: Wild type hSOD1 structure (pdb code 1HL5) showing the Greek key Beta-barrel in grey, the zinc loop (loop IV, residues 50-83) in pink, and the electrostatic loop (loop VII, residues 121-142) in yellow. The zinc and copper ions are shown as orange and blue spheres respectively. Sulfur atoms forming the intrasubunit disulfide bond between residues 57 and 146 are shown as green spheres.
Figure 2: The zinc and copper binding sites in hSOD1 superimposed on a sigmaA-weighted electron density with coefficients 2mFo-DFc contoured at 1.2 sigma.
Current research students:
Adrian Mehrtash, sophomore biology major (funded by NIH grant)
Dimitrios Barrera, senior biophysics major (MARC)
Recent publications:
Lin, A. P., Demeler, B., Minard, K. I., Anderson S. L., Schirf, V., Galaleldeen, A., and McAlister-Henn, L. (2011) Biochemistry. 50, 230-239. "Construction and Analyses of Tetrameric Forms of Yeast NAD(+) Specific Isocitrate Dehydrogenase."
Chen, D., Lei, L., Lu, C., Galaleldeen, A., Hart, P. J., and Zhong, G. (2010) J. Bacteriol. 192, 6017-24. "Characterization of Pgp3, a Chlamydia trachomatis Plasmid-encoded Immunodominant Antigen."
Galaleldeen, A., Strange, R., Whitson, L. J., Antonyuk, S., Taylor, A. B., Hasnain, S. S., and Hart, P. J. (2009) Arch. Biochem. Biophys. 492, 40-47. "Structural and Biophysical Properties of Metal-Free Pathogenic SOD1 Mutants A4V and G93A."
Galaleldeen, A., and Hart, P. J. "Human Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis" in: Protein Reviews, Protein Misfolding, Aggregation and Conformational Diseases. (Zouhair Atassi Ed.) (2007) pp. 327-344, Springer, New York.
Chlamydia is a genus of gram negative intracellular pathogens that cause various health problems in humans. C. trachomatis infection of the urinogenital tract is the most common sexually transmitted bacterial disease in the world, while ocular infections cause trachoma, potentially leading to blindness. C. pneumoniae is a common cause of pneumonia and often associated with atherosclerosis and coronary artery disease. The nature of Chlamydia as an intracellular pathogen and its presence in cellular inclusions presents a challenge for researchers. The lack of tools for genetic manipulation of Chlamydia has hindered this research and little is known about the molecular mechanism(s) through which Chlamydia interacts with the host cell and manipulates its cell signaling and immune response. Structural biology is an emerging tool that can be used to overcome the difficulties of genetic manipulation and allow us to determine the functions of chlamydial proteins. We are interested in identifying, characterizing and determining the 3D structure of various effector proteins secreted by Chlamydia in the host cell.
Project 2:
Superoxide dismutases (SODs) are a family of metallo-enzymes that protect cells from oxidative damage caused by reactive oxygen species (ROS). ROS are produced as a direct result of aerobic respiration and photosynthesis and if not detoxified, can exert damaging effects via oxidation of DNA, proteins and lipids. Four distinct classes of SOD have been identified based on the identity of the redox-active metal ions bound as cofactors at the active site, which include nickel, iron, manganese, and copper/zinc. We are interested in characterizing SODs from different species and understanding the activation, i.e. metallation and disulfide bond formation, process of these enzymes.
Figure 1: Wild type hSOD1 structure (pdb code 1HL5) showing the Greek key Beta-barrel in grey, the zinc loop (loop IV, residues 50-83) in pink, and the electrostatic loop (loop VII, residues 121-142) in yellow. The zinc and copper ions are shown as orange and blue spheres respectively. Sulfur atoms forming the intrasubunit disulfide bond between residues 57 and 146 are shown as green spheres.
Figure 2: The zinc and copper binding sites in hSOD1 superimposed on a sigmaA-weighted electron density with coefficients 2mFo-DFc contoured at 1.2 sigma.
Current research students:
Adrian Mehrtash, sophomore biology major (funded by NIH grant)
Dimitrios Barrera, senior biophysics major (MARC)
Recent publications:
Lin, A. P., Demeler, B., Minard, K. I., Anderson S. L., Schirf, V., Galaleldeen, A., and McAlister-Henn, L. (2011) Biochemistry. 50, 230-239. "Construction and Analyses of Tetrameric Forms of Yeast NAD(+) Specific Isocitrate Dehydrogenase."
Chen, D., Lei, L., Lu, C., Galaleldeen, A., Hart, P. J., and Zhong, G. (2010) J. Bacteriol. 192, 6017-24. "Characterization of Pgp3, a Chlamydia trachomatis Plasmid-encoded Immunodominant Antigen."
Galaleldeen, A., Strange, R., Whitson, L. J., Antonyuk, S., Taylor, A. B., Hasnain, S. S., and Hart, P. J. (2009) Arch. Biochem. Biophys. 492, 40-47. "Structural and Biophysical Properties of Metal-Free Pathogenic SOD1 Mutants A4V and G93A."
Galaleldeen, A., and Hart, P. J. "Human Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis" in: Protein Reviews, Protein Misfolding, Aggregation and Conformational Diseases. (Zouhair Atassi Ed.) (2007) pp. 327-344, Springer, New York.
Christine E. Gray, Ph.D.
"Cytoplasmic incompatibility in Drosophila and CTCF-dependent insulators in insects"Read about it
I am a geneticist with an interest in gene expression and how it varies with genomic environment. I currently am engaged in two projects. The first of these projects is investigating a potential mechanism to explain a phenomenon known as cytoplasmic incompatibility (CI). CI results in arrested cell division immediately after fertilization and occurs as a direct consequence of infection with a bacterium (Wolbachia). The end result is infertility. The phenomenon is directional. It only occurs when Wolbachia-infected males mate with uninfected females. Understanding just how Wolbachia causes CI in insects may allow other researchers to utilize Wolbachia in efforts to control populations of important insect disease vectors. This project is being done in the fruit fly, Drosophila melanogaster.
The second project involves assessing several CTCF-binding sites from the malaria mosquito vector, Anopheles gambiae, for insulator activity in cell culture. CTCF is a well-characterized DNA binding protein that has been shown to be a potent insulator for gene expression in vertebrate systems. Insulators act as a type of "bookend" for genes and keep regulatory sequences that promote or repress gene expression from interacting with neighboring genes and affecting their expression simply because they are close by. A CTCF-like protein has been identified in fruit flies and in two species of mosquitoes that vector human pathogens. Identification of specific DNA sequences with CTCF-dependent insulator activity would be advantageous in protecting the expression of transgenes which reduce mosquito fertility and/or block expression of key genes required for pathogen replication or transmission.
Current research students:
Tiffany Brown, senior biology major (Biaggini)
Audiel Espitia, senior biology major (SURF)
John Fedorick, senior biology major
Sierra Tamez, senior biology major (Biaggini)
Melissa Valdes, junior biochemistry major (MARC)
Recent publication:
Gray, C.E. and Coates, C.J. (2005) Cloning and characterization of cDNAs encoding putative CTCFs in the mosquitoes, Aedes aegypti and Anopheles gambiae. BMC Molecular Biology 6:16.
Figure 1. Assessing Wolbachia infection status in experimental and control Drosophila lines. The 16S rDNA gene from Wolbachia (936 bp) and the 12S rDNA gene from Drosophila mitochondria (400 bp) were amplified by PCR with gene-specific primers. Samples in lanes 2-4 and lane 6 are infected, while the sample in lane 5 is uninfected. Lane 7 is a control with no input DNA. Lane 8 is a control with no Taq DNA polymerase.
Current research students:
Tiffany Brown, senior biology major (Biaggini)
Audiel Espitia, senior biology major (SURF)
John Fedorick, senior biology major
Sierra Tamez, senior biology major (Biaggini)
Melissa Valdes, junior biochemistry major (MARC)
Recent publication:
Gray, C.E. and Coates, C.J. (2005) Cloning and characterization of cDNAs encoding putative CTCFs in the mosquitoes, Aedes aegypti and Anopheles gambiae. BMC Molecular Biology 6:16.
Thomas E. (Ted) Macrini, Ph.D.
"Comparative Anatomy of Mammalian Skulls" and"Knee Osteoarthritis in a Baboon Model"
Read about it
My research in comparative anatomy focuses on internal structures of mammalian skulls, particularly the nasal cavity, braincase, and inner ear. I use X-ray computed tomography (CT) to non-destructively visual these structures in fossil and extant mammal skulls with the purpose of describing skeletal anatomy related to sensory structures, and to utilize these data to reconstruct phylogenetic relationships among mammals. I've worked on a variety of mammalian groups including monotremes, marsupials, primates, chiropterans (bats), sirenians (manatees), proboscideans (elephants), and a number of completely extinct taxa such as notoungulates, an enigmatic group from South America. I work with colleagues from The University of Texas at Austin and the American Museum of Natural History (New York), among other institutions, and I have ongoing projects involving St. Mary's University (StMU) students.
My other research program examines knee osteoarthritis (OA), a debilitating joint disease in humans, using baboons (Papio hamadryas ssp.) from the Texas Biomedical Research Institute (TBRI) colony in San Antonio. These baboons, like humans, naturally develop OA. This research is conducted in collaboration with Dr. Lorena M. Havill (TBRI, Department of Genetics) among others, and is aimed at uncovering the etiology of early stage OA and understanding the genetic and other factors contributing to disease risk. Ongoing projects involving StMU students include gross anatomical studies of OA in the articular cartilage of the knee joint, and analyses of histological and radiographic evidence of OA in baboons.
Current research students:
Gerardo Astorga, sophomore biology major
Christina Karmann, senior biology major
Celeste Passement, sophomore biology major
Evelia Salinas, sophomore biophysics major (pre-MARC)
Tony Vega, senior biophysics major (MARC)
Recent publications:
Macrini, T. E., J. J. Flynn, D. A. Croft, and A. R. Wyss. 2010. Inner ear of a notoungulate placental mammal: anatomical description and examination of potentially phylogenetically informative characters. Journal of Anatomy 216:600-610.
Rowe, T., T. E. Macrini, and Z.-X. Luo. 2011. Fossil evidence on origin of the mammalian brain. Science 332:955-957.
Macrini, T. E. 2012. Comparative morphology of the internal nasal skeleton of adult marsupials based on X-ray computed tomography. Bulletin of the American Museum of Natural History 365:1-91.
Beatty, B. L., T. Vitkovski, O. Lambert, and T. E. Macrini. 2012. Osteological associations with unique tooth development in manatees (Trichechidae, Sirenia): a detailed look at modern Trichechus and a review of the fossil record. Anatomical Record 295:1504-1512.
Giannini, N. P., T. E. Macrini, J. R. Wible, T. Rowe, and N. B. Simmons. 2012. The internal nasal skeleton of the bat Pteropus lylei K. Andersen, 1908 (Chiroptera: Pteropodidae). Annals of Carnegie Museum (in press).
The above image shows a digital 3-D reconstruction of the semitransparent skull of Hadrocodium wui, a tiny early Jurassic age mammal that weighed just two grams. The cranial endocast, indicating the braincase cavity, is shown in red. The imagery was generated from CT images of the skull and formed the basis of Rowe et al. (2011). Scale: the skull is 13 mm long.
Current research students:
Gerardo Astorga, sophomore biology major
Christina Karmann, senior biology major
Celeste Passement, sophomore biology major
Evelia Salinas, sophomore biophysics major (pre-MARC)
Tony Vega, senior biophysics major (MARC)
Recent publications:
Macrini, T. E., J. J. Flynn, D. A. Croft, and A. R. Wyss. 2010. Inner ear of a notoungulate placental mammal: anatomical description and examination of potentially phylogenetically informative characters. Journal of Anatomy 216:600-610.
Rowe, T., T. E. Macrini, and Z.-X. Luo. 2011. Fossil evidence on origin of the mammalian brain. Science 332:955-957.
Macrini, T. E. 2012. Comparative morphology of the internal nasal skeleton of adult marsupials based on X-ray computed tomography. Bulletin of the American Museum of Natural History 365:1-91.
Beatty, B. L., T. Vitkovski, O. Lambert, and T. E. Macrini. 2012. Osteological associations with unique tooth development in manatees (Trichechidae, Sirenia): a detailed look at modern Trichechus and a review of the fossil record. Anatomical Record 295:1504-1512.
Giannini, N. P., T. E. Macrini, J. R. Wible, T. Rowe, and N. B. Simmons. 2012. The internal nasal skeleton of the bat Pteropus lylei K. Andersen, 1908 (Chiroptera: Pteropodidae). Annals of Carnegie Museum (in press).
Marshall D. McCue, Ph.D.
"Comparative Physiology and Physiological Ecology"Read about it
Animals naturally face many environmental challenges including dehydration, malnutrition or food limitation, extreme temperatures, low oxygen availability, and parasitism. I am generally interested in exploring the physiological and biochemical mechanisms that allow animals to survive - and sometimes thrive - amidst these challenges. I employ a variety of model organisms including fish, reptiles, mammals, birds, and insects in my quest to better understand 'how animals work.'
My most recent research involves using stable isotope labeled metabolic tracers to investigate the physiological 'decisions' that dictate how, when, and where in the body animals allocate the different types of nutrients in the foods they eat and how, when, and were in the body they breakdown and burn different types of nutrients when food resources are scarce.
Current research students:
James Amaya, junior biology major (Biaggini)
Alice Yang, junior biology major (Biaggini)
Agnelio Cardentey, senior biophysics major (funded by Faculty Development Grant)
Roberto de los Santos, junior biology major (SURF)
Recent publications:
McCue, M. D. (2012). "Horizons in starvation research." Chapter 24 in: Comparative Physiology of Fasting, Starvation, and Food Limitation. M. D. McCue, Editor. New York, Springer-Verlag: 409-420.
Munoz-Garcia, A., S. Aamidor, M. D. McCue, S. R. McWilliams and B. Pinshow (2012). "Allocation of endogenous and dietary protein in the reconstitution of the gastrointestinal tract in migratory blackcaps at stopover sites." Journal of Experimental Biology 215: 1069-1075.
Khalilieh, A., M. D. McCue and B. Pinshow (2012). "Physiological responses to food deprivation in the house sparrow, a species not adapted to prolonged fasting." American Journal of Physiology. in press.
McCue, M. D., A. Smith, R. McKinney, B. Rewald, B. Pinshow and S. R. McWilliams (2011). "A mass balance approach to identify and compare differential routing of 13C-labeled carbohydrates, lipids, and proteins in vivo." Physiological and Biochemical Zoology 84(5): 506-513.
McCue, M. D. (2011). "Tracking the oxidative and non-oxidative fates of isotopically labeled nutrients in animals." BioScience 61(3): 217-230.
My most recent research involves using stable isotope labeled metabolic tracers to investigate the physiological 'decisions' that dictate how, when, and where in the body animals allocate the different types of nutrients in the foods they eat and how, when, and were in the body they breakdown and burn different types of nutrients when food resources are scarce.
Current research students:
James Amaya, junior biology major (Biaggini)
Alice Yang, junior biology major (Biaggini)
Agnelio Cardentey, senior biophysics major (funded by Faculty Development Grant)
Roberto de los Santos, junior biology major (SURF)
Recent publications:
McCue, M. D. (2012). "Horizons in starvation research." Chapter 24 in: Comparative Physiology of Fasting, Starvation, and Food Limitation. M. D. McCue, Editor. New York, Springer-Verlag: 409-420.
Munoz-Garcia, A., S. Aamidor, M. D. McCue, S. R. McWilliams and B. Pinshow (2012). "Allocation of endogenous and dietary protein in the reconstitution of the gastrointestinal tract in migratory blackcaps at stopover sites." Journal of Experimental Biology 215: 1069-1075.
Khalilieh, A., M. D. McCue and B. Pinshow (2012). "Physiological responses to food deprivation in the house sparrow, a species not adapted to prolonged fasting." American Journal of Physiology. in press.
McCue, M. D., A. Smith, R. McKinney, B. Rewald, B. Pinshow and S. R. McWilliams (2011). "A mass balance approach to identify and compare differential routing of 13C-labeled carbohydrates, lipids, and proteins in vivo." Physiological and Biochemical Zoology 84(5): 506-513.
McCue, M. D. (2011). "Tracking the oxidative and non-oxidative fates of isotopically labeled nutrients in animals." BioScience 61(3): 217-230.
Current Student Research
When you have direct access to great minds in biology, why not absorb all the knowledge and experience you can? Our Biological Sciences students have teamed up with faculty mentors and are looking for answers to tough questions in their field of interest. Here's a sampling of what they're currently learning.
James Amaya
Biaggini scholarMajor: Biology (Senior)
Faculty Research Mentor: Marshall D. McCue, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: Research
What I'm researching
Quantitative analysis of the metabolism of macromolecules containing carbon isotopes in fasting quail to identify stages of metabolism.
Cassandra Antell
MARC Program traineeMajor: Biophysics (Junior)
Faculty Research Mentor: Richard Cardenas, Ph.D.
Hometown: El Paso, TX
Career Aspirations: Ultimately I want to go into education. I am extremely interested in pursuing biomedical research and possibly working with various imaging modalities used in the medical field or smart prosthetics.
What I'm researching
Electroactive polymers are certain types of polymers that react to electrical stimulation by stretching, bending, or contracting. Electroactive polymers, or EAPs, are categorized by their activation mechanism as being either ionic or electronic. Ionic EAPs activate as a result of interactions involving the mobility or diffusion of ions. Electronic EAPs are triggered by electric fields. Both forms of activation prove to have advantages and disadvantages alike. Electronic EAPs can operate for longer periods of time under normal conditions and exhibit rapid response. However, they require high voltages to do so. Ionic EAPs on the other hand require low voltages and can provide a greater bending displacement, but also provide a slow response and often require the use of an electrolyte. Many electronic EAPs such as ferroelectric polymers are composed of a partially crystalline component such as quartz or tourmaline and can be operated within wide ranges of temperature. Various forms of elastomers such as fibrous electrostrictive papers or grafts and silicon based electro-viscoelastic elastomers are often used in conjunction with other electronic EAP materials or as their own structure to provide different ranges of electric field induced strain. Ionic EAPs come in a variety of forms such as ionic polymer gels, ionometric polymer-metal composites that use two manufactured base polymers (Nafion and Flemion), conductive polymers that use electrodes and an electrolyte, and carbon nanotubes, which also use electrolytes. Because of their abilities to induce significantly high magnitudes of strain at higher response speeds and greater resilience than seen before in other types of polymers, electroactive polymers have proved to be viable candidates in the field of biomimetics. Applications include mimicking life-like systems such as artificial muscles, catheter steering elements, miniature manipulators, arms, and grippers, and even micro-robots and devices. We will be creating both types of EAPs and doing a characterization study on their responses to a variety of stimuli. We intend to create a mixture type of EAP that will exhibit the good properties of electronic and ionic EAPs in one composite material.
Dina Attia
Biaggini scholarMajor: Biology (Junior)
Faculty Research Mentor: Veronica Contreras-Shannon, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: To become a physician
What I'm researching
As a Biaggini scholar working alongside Dr. Contreras-Shannon, I will be conducting research that involves a drug that is used to treat patients with schizophrenia. Although the drug does treat the disease, unfortunately, it also causes loss of mitochondrial function in the cell. In effect, this results in decreased energy output, a lower metabolism, and weight gain. We are hoping to test the effect of antioxidants on these cells affected with the drug to determine whether the antioxidants will restore mitochondrial function. We will be working with three different cell lines, and will observe the difference in ATP production from the control tissue cultures and experimental cultures over the course of the research.
Dimitrios N. Barrera
MARC Program traineeMajor: Biophysics and Mathematics (Senior)
Faculty Research Mentor: Ahmad Galaleldeen, Ph.D.
Hometown: Bad Cannstatt, Germany
Career Aspirations: Ph.D., followed by a scientific research career in academia
What I'm researching
Chlamydiae are obligate, intracellular Gram-negative bacteria that are known to cause various health problems in humans. Chlamydia trachomatis causes the sexually transmitted disease Chlamydia by infecting the epithelial cells of the genital tract. C. trachomatis also causes trachoma that leads to blindness by infecting the conjunctiva. Chlamydophila psittaci, a closely related species, is responsible for psittacosis, which is also known as parrot fever. Chlamydophila pneumoniae is responsible for an infection of the upper respiratory tract that also causes atypical pneumonia, with evidence linking it to the development of atherosclerosis and coronary artery disease. The infectious cycle of Chlamydiae is characterized by a unique biphasic life cycle. Infection begins when small extracellular elementary bodies (EBs) attach themselves to the epithelium of susceptible host cells. These metabolically inactive bacterial forms, upon entry into the cell reside exclusively in a vesicle termed inclusion. Inside the inclusion EBs differentiate into larger non-infectious metabolically active reticulate bodies (RBs) that divide using binary fission. Within 48 hrs RBs transforms back to EBs that get released from the inclusion to infect other cells. Chlamydiae interact with the host cells and manipulate their cell signaling and immune response by secreting effector proteins. The most characterized of these proteins is the Chlamydial Protease/Proteasome-like Activity Factor (CPAF) which plays a role in degrading various proteins inside the host cells. Other factors secreted during Chlamydophila pneumoniae infection are products of a cluster of six homologous genes encoding the effector proteins cpn0794-cpn0799. It has been observed that cpn0796 and cpn0797 are secreted into the host cell and localized in the cytoplasm. We are interested in studying the structures and roles of cpn0794-cpn0799 during infection.
Agnelio Cardentey
Student researcherMajor: Biophysics (Senior)
Faculty Research Mentor: Marshall D. McCue, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: I hope to become a physician specializing in radiology or radiation oncology.
What I'm researching
13C-Breath testing is currently used in research to study protein, lipid, and carbohydrate metabolism. Stable isotope tracers (i.e. 13C) are introduced into the body, and researchers quantify the amount of tracer that is converted into CO2 and exhaled in the breath. Because it provides a safe alternative to radioactive tracers, this technique is used by clinics to diagnose a variety of metabolic disorders in children and pregnant women. Our research will address concerns made by clinicians and researchers regarding the differences in the oxidative fates of different types of 13C-labeled metabolic tracers used in 13CO2 breath testing. We will examine the oxidative fates of free amino acids versus proteins and free fatty acids versus lipids. The results of our experiments will be utilized to better characterize how tracers are metabolized dependent on how they are introduced into the body. This information will be used to re-evaluate how breath testing is conducted in research and clinical settings in order to improve diagnostic accuracy, efficiency, and reliability.
Janet Chen
Honors studentMajor: Biology (Senior)
Faculty Research Mentor: Veronica Contreras-Shannon, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: Become a physician
What I'm researching
My research project examines the effects of the atypical antipsychotic drug clozapine using a yeast model system to better understand how this drug may cause adverse side effects like weight gain and insulin resistance. Specifically, I examine how the drug affects the production of reactive oxygen species (ROS) and cell viability during growth on different types of carbon sources. This semester, three different antioxidants (N-acetylcysteine, vitamin C, and vitamin E) are being tested on the effectiveness of reducing clozapine-induced ROS in yeast cells and whether these antioxidants can restore ATP production in the presence of clozapine. Both ROS production and defects in ATP production are related to mitochondrial dysfunction, which may be the basis for the negative side effects associated with clozapine.
Andrew Gonzalez
Biaggini scholarMajor: Biology (Junior)
Faculty Research Mentor: Veronica Contreras-Shannon, Ph.D.
Hometown: Corpus Christi, TX
Career Aspirations: Physician
What I'm researching
I would like to research about the mechanisms of different pathogens and their effects on different physiological functions. More specifically, the research topics at hand I am excited in delving into are the faulty mechanisms of the endoplasmic reticulum and the consequences of faulty protein folding. I hope to possibly expand my knowledge about pathophysiology and carry the experience with me onto medical school, as I am open to a possibly career in pathology.
Andrew Hansen
MARC Program traineeMajor: Biochemistry (Senior)
Faculty Research Mentor: S. Colette Daubner, Ph.D.
Hometown: Austin, TX
Career Aspirations: Computational neuroscience
What I'm researching
I have been working with Dr. Daubner with the aid of a grant received by the AHA to determine the mechanism involved in the regulation of tyrosine hydroxylase (TyrH), an enzyme present in catecholaminergic neurons. TyrH's regulation/kinetics is relevant in the field of health sciences due to implications for health problems such as hypertension and diseases of the dopaminergic systems within the brain. This regulation is known to occur by both phosphorylation and dopamine feedback inhibition. We are analyzing specifically how this occurs within the regulatory domain of TyrH and structural changes correlative to its regulation. These changes at present must be studied via chemical interactions and UV-Vis spectroscopy. We are using substrate assays, inhibition assays, and dopamine-on/off experiments to study the differences in behavior of TyrH mutants via spectroscopy. The study of these designed mutants will yield results as to whether or not our hypothesized mechanism of regulation is accurate.
Uche Ozoemena
Biaggini scholarMajor: Biochemistry (Sophomore)
Faculty Research Mentor: Veronica Contreras-Shannon, Ph.D.
Hometown: Nigeria
Career Aspirations: Cardiologist
What I'm researching
Our research project is geared towards understanding the root mechanisms through which anti-psychotic drugs cause their side effects (such as changes in the patient's metabolic levels). We will be working with muscle, fat, and liver cells, because these cell groups are known to be responsible for changes in metabolic rates. For our analysis, we will be treating these cells with clozapine, a commonly used anti-psychotic drug.
Melissa Valdes
MARC Program traineeMajor: Biochemistry (Junior)
Faculty Research Mentor: Christine E. Gray, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: Physician scientist
What I'm researching
Insulators are DNA elements that protect a gene from the surrounding genome through enhancer-blocking and barrier activity and are thought to set up chromatin domain boundaries. When positioned between a promoter and an enhancer, insulators can block enhancer-promoter interactions. Insulators also act as barriers to protect against chromosomal position-effects by positioning themselves around genes. Reporter gene assays provide quantitative results to define an insulator's function. The ability of CCCTC-binding factor (CTCF) to act as an insulator has been identified in Drosophila melanogaster (fruit fly). CTCF homologs have also been found in mosquitoes through Dr. Christine Gray's previous research. I will be working with Dr. Gray throughout the academic year to analyze the enhancer-blocking functionality of CTCF in mosquitoes.
Anthony Vega
MARC Program traineeMajor: Biophysics (Senior)
Faculty Research Mentor: Thomas E. (Ted) Macrini, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: Professor and principal investigator of a lab
What I'm researching
I am examining how well the brain fills the braincase in an extant (living) model mammal, Monodelphis domestica, the gray short-tailed opossum. Analyses of fossil vertebrates rely on estimation of brain volume using endocranial (braincase) volume because soft-tissue structures such as the brain often are not preserved. Even brain volume studies of extant mammals can be plagued by measurement errors when the brain is manually dissected and measured. My study involves digital segmentation (individualization) of brain tissue from in vivo and postmortem MRI scans of heads of M. domestica to measure brain volumes, and segmentation of CT imagery from the same individuals to measure endocranial volumes. This study will provide some ground-truth to brain evolution studies that are based on fossil mammals, by establishing how well the brain fills the braincase in a single species of extant mammal.
Jessica Villacorta
MARC Program traineeMajor: Biochemistry (Junior)
Faculty Research Mentor: S. Colette Daubner, Ph.D.
Hometown: Houston, TX
Career Aspirations: Clinical research or industry
What I'm researching
Parkinson's disease is a degenerative disorder of the central nervous system that leads to tremors and difficulty with movement and coordination. Parkinson's disease occurs when the nerve cells that make dopamine are destroyed. Dopamine is a catecholamine neurotransmitter that nerve cells use to send messages. However, little is known as to how nerve cells lose their ability to create dopamine. In our lab we are working with tyrosine hydroxylase, an enzyme required for the synthesis of DOPA which is further converted to dopamine. Our research focuses on the active site of tyrosine hydroxylase and how it binds to DOPA. We hypothesize that acidic amino acids located on the active site are responsible for anchoring down DOPA on the regulatory domain. Results from this work will help generate new therapeutic treatments for Parkinson's disease.
Alice Yang
Biaggini scholarMajor: Biology (Senior)
Faculty Research Mentor: Marshall D. McCue, Ph.D.
Hometown: San Antonio, TX
Career Aspirations: MD
What I'm researching
For the study my team is working on, we will be measuring rates of oxidation of endogenous carbohydrates, lipids, and proteins during prolonged periods of starvation in mice and quail. Using the Carbon-13 tracer, we will be able to quantify an estimate of a timeline of events that occur metabolically during starvation. Mice and quail will be raised on the isotope tracer until it is well incorporated into their system. Food will be withheld while taking measurements of exhaled CO2. The amount of C-13 tracer exhaled will determine what (protein, lipid, carbohydrate) is being oxidized. The ultimate goal of the project is to develop clinical diagnostic methods using the C-13 tracer instead of traditional radioactive molecules.
Departmental Research and Scholarship Opportunities
Research and scholarship opportunities for biology majors are available for deserving students who demonstrate academic achievement and financial need. Listed below are some of scholar programs available, each with their respective eligibility criteria.Biaggini Research Program
Biaggini Research Program
The Biaggini Research Program in the Department of Biological Sciences was established through an endowment created in honor of Benjamin F. Biaggini - Distinguished Alumnus of St. Mary s University and former CEO of Southern Pacific. Funds are utilized to provide scholarships to junior or senior level biology majors who are named Biaggini Research Scholars. As part of the requirements for receiving these scholarships, Biaggini Scholars are required to actively participate in an ongoing research project with Biaggini Research Fellows or another faculty member in the department. Travel funds are also provided for these students to attend a national meeting or conference to present their research findings.The overall goal of the program is to enhance the ability of faculty members in our department to engage in research projects as a means for professional development in the form of publication(s) and/or additional external funding to continue their research endeavors.
Additionally, funds from this endowment were utilized to establish the Biaggini Endowed Chair in Biological Sciences and to create a research program that provides funding for two faculty members (Biaggini Research Fellows) in the department that are actively involved a research project associated with some aspect of human health and/or disease. The Research Fellow budget includes released time to engage in the research, funds for purchasing supplies, and funds for travel to present findings from their research projects.
Eligibility and Rules
To be considered for the Biaggini Research program, a student:
- must be nominated by a biology professor.
- must be a junior or senior biology major.
- must have a GPA of at least 3.0 overall and major.
- must complete the application by the deadline.
Biaggini Fellows
2012-2013 Biaggini Fellows:
Marshall D. McCue, Ph.D.Assistant Professor of Biological Sciences
Developing a method to directly quantify substrate oxidation and physiological shifts during acute nutritional stress
This project will allow us to test a recently-developed approach to investigate the progression of biological changes in health during fasting and malnutrition. The experimental approach uses special chemical tracers to understand what happens within the tissues of the body. Weight loss is an obvious outcome of fasting, but little is known about how the body burns different types of nutrients when food is not available. We will conduct nutritional experiments using laboratory animals, but the ultimate aim is to develop a technique that can be used to study human nutrition.
Veronica Contreras-Shannon, Ph.D.
Associate Professor of Biological Sciences
The Role of Endoplasmic Reticulum Dysfunction and the MCP-1/CCR2 Pathway in Clozapine-Induced Metabolic Side Effects
While being very effective for the treatment of schizophrenia, atypical antipsychotics have been found to cause severe side effects capable of affecting an individual's metabolism and the body's ability to fight infection. With regard to the former, this includes changes to a person's weight, glucose levels and fat composition which may ultimately lead to diabetes, obesity, and high cholesterol all of which are associated with increased risk for cardiovascular disease. The underlying biological cause of the associated side-effects of atypical antipsychotics is unknown. It is interesting to note that there is a growing consensus in the obesity field that understanding the mechanisms responsible for the adverse metabolic effects of atypical antipsychotics may shed an important light on the origin of metabolic disease itself. There are three interrelated hypotheses for why these drugs cause metabolic side effects: 1) these drugs negatively affect the proper functioning of mitochondria and/or the endoplasmic reticulum (ER), 2) these drugs cause increased oxidative stress in cells and tissues, and 3) these drugs promote inflammation. Because mitochondria are the "powerhouses" of the cell responsible for producing energy, when mitochondrial function is altered, so is the way energy is used and produced by the cell. The ER is responsible for the proper folding and secretion of proteins required for normal cellular functions. Under circumstances of stress, the ER may initiate the unfolded protein response (UPR) which can lead to changes in gene expression or in extreme cases, cell death. Oxidative stress refers to a state in which cells are susceptible to damage caused by reactive chemicals capable of damaging cell components (proteins, DNA, cell membranes and organelles such as mitochondria or ER) or initiating cell death. Under normal circumstances, mitochondria produce these reactive species but the cell has protective mechanisms to keep these reactive chemicals from "stressing" the cell. Inflammation is an innate mechanism that protects the body's tissues and cells from insults caused by trauma and a variety of pathogens, such as chemicals and microorganisms. An inflammatory response causes a number of cells and molecules to elicit a protective response, a response that both utilizes and produces a number of reactive chemical species also capable of causing oxidative stress. ER dysfunction and UPR can elicit or result from inflammation, oxidative stress, and/or mitochondria dysfunction. In addition, inflammation, oxidative stress, and mitochondrial dysfunction can each give rise to the other. In the proposed project, several different cell lines representing the "whole body" will be treated with clozapine, a representative atypical antipsychotic, and examined for alterations in ER function and the UPR. Much of the current work on atypical antipsychotics focuses on the target cells for treatment, neurons and the brain. The proposed work will study cell types known to be responsible for metabolic changes, namely fat, muscle and liver cells. Completion of these studies will produce data that will form the basis for student projects, manuscripts and abstracts for presentation.
S.A.L.E. Scholar Program
San Antonio Livestock Exposition (S.A.L.E.) Scholar Program
Biology majors are selected for the S.A.L.E. Scholar Program based on their high school grades and test scores. The S.A.L.E. Scholar Program is made possible through the generosity of the San Antonio Livestock Exposition (S.A.L.E.) and thousands of volunteers. Each academic year, a cohort of 10 freshman students is selected for this program. Each student will receive $10,000 toward the cost of tuition over four years of studies.Eligibility and Rules
Eligibility and Rules:
- Selected students must formally accept the scholarship by filling out the required forms. Once those forms are completed, $1,250 will be applied to the student s account each semester.
- Students must achieve a minimum GPA of 3.0 each semester and overall to receive the scholarship.
- Students must attend a scholarship reception each year with representatives from S.A.L.E. and are strongly encouraged to volunteer at S.A.L.E.-related events.
Faculty & Staff
Reynaldo C. Balli III
Stockroom Manager, BiologyOffice: Biological Sciences, Box 11
Phone: (210) 431-4303
rballi@stmarytx.edu
S. Colette Daubner, Ph.D.
Associate Professor of Biological SciencesOffice: Garni 110
Phone: (210) 431-4358
sdaubner@stmarytx.edu
Full Bio Details
B.S., University of Wisconsin-Milwaukee
Ph.D., University of Michigan
S. Colette Daubner, Ph.D., received her B.S. in Zoology from the University of Wisconsin-Milwaukee, where she worked in the Chemistry Department and a genetics lab in the Zoology Department. She received her Ph.D. in Biological Chemistry from the University of Michigan purifying and studying the enzyme methylenetetrahydrofolate reductase (MTHFR), an important enzyme in one-carbon transfers. MTHFR was later found to play a role in cardiovascular disease, strokes, and neural tube defects. Her post-doctoral work at the Pennsylvania State University centered on the enzymes of purine de novo biosynthesis, which also utilize derivatives of folate, and are also important in fast-growing cells such as cancers and embryonic tissues.
As a research scientist in the Department of Biochemistry and Biophysics at Texas A&M in College Station Daubner worked on the enzymes tyrosine hydroxylase (TyrH), phenylalanine hydroxylase, and tryptophan hydroxylase. This family of rate-limiting enzymes uses the cofactor biopterin and bound iron to hydroxylate aromatic amino acids. Her work brings together enzymological techniques, protein modification, cloning and mutagenesis of the proteins, fluorimetry and other biophysical techniques.
Ahmad Galaleldeen, Ph.D.
Assistant Professor of Biological SciencesOffice: Garni 108B
Phone: 210-436-3502
agalaleldeen@stmarytx.edu
Full Bio Details
B.S., University of Alexandria-Egypt, 1992
M.S., Texas A&M University-Kingsville (TAMUK), 2001
Ph.D., University of Texas Health Science Center at San Antonio (UTHSCSA), 2009
Ahmad Galaleldeen, Ph.D., earned his bachelor's, master's and Ph.D. in Biochemistry. During his Ph.D. and postdoctoral tenure at UTHSCSA, he was trained as a biochemist and a structural biologist. Following his bachelor's, he held a chemistry and biology teaching position in Egypt for 6 years before moving to the US. While pursuing his master's, he also held an algebra and chemistry teaching position at the Presbyterian Pan American School in Kingsville. Galaleldeen teaches General Biology BL 1401, BL 1402 and Cell and Molecular Methods (BL 2233) at St. Mary's.
Galaleldeen joined the laboratory of Dr. John Hart at UTHSCSA in 2003 and focused his research on the familial form of amyotrophic lateral sclerosis (ALS) also known as Lou Gehrig's disease. ALS is the most common adult motor neuron disease, characterized by the progressive destruction of both upper and lower motor neurons. The disorder typically manifests as muscle weakness in the extremities that progresses throughout the body, resulting in paralysis and death generally within five years post-diagnosis. Approximately 20% of the familial cases are linked to mutations in the copper-zinc superoxide dismutase (SOD1) gene. Galaleldeen determined the crystal structure of several pathogenic SOD1 mutants including A4V, the most common ALS mutation in North America, in its metal free form.
During his postdoctoral training in the Hart lab, Galaleldeen collaborated with Dr. Guangming Zhong on a project to understand Chlamydial pathogenesis. Chlamydia trachomatis is an intracellular gram negative bacterial pathogen with many different strains that infect and cause disease in humans and animals. C. trachomatis infection of the urinogenital tract is the most common sexually transmitted disease in the world. C. trachomatis can also infect the eye, causing trachoma that can lead to blindness. Galaleldeen characterized and determined the structure of pgp3, an immuno-dominant antigen that is heavily secreted by C. trachomatis into the cytoplasm of the host cells in the first 24 hours post-infection.
Christine E. Gray, Ph.D.
Associate Professor of Biological SciencesOffice: Moody Life Sciences Center 304
Phone: (210) 436-4306
cgray@stmarytx.edu
Full Bio Details
B.S., DePaul University, 1986
Ph.D., Texas A&M University, 2005
Christine E. Gray, Ph.D., earned her bachelor's with majors in Biological Sciences and Secondary Education, and then taught high school courses in Biology, Chemistry, Anatomy and Physiology, and Topics in Laboratory Science for eleven years at two Chicago area high schools. Gray completed a Ph.D. in the Interdisciplinary Genetics program at Texas A&M University. Gray now teaches General Biology for Majors I and II, Developmental Biology, Evolutionary Biology and Genetic Principles at St. Mary's.
Much of her research involved the identification and initial characterization of a CTCF-like protein in both Aedes aegypti (the primary vector of both yellow fever and dengue fever) and Anopheles gambiae (the principal vector of falciparum malaria). CTCF is a well-known insulator binding protein in vertebrates and its mosquito homologue may provide a useful means to increase the efficiency of the process used to make transgenic mosquitoes. Transgenic mosquitoes are made for two key reasons: to learn more about key mosquito genes involved in the natural transmission of pathogens and to potentially create mosquito strains that are unable to transmit pathogens such as viruses, filarial worms and protozoans.
Gray is also working with several undergraduates on a project to investigate the mechanism for a phenomenon known as cytoplasmic incompatibility (CI) in fruit flies (Drosophila). CI results when specific bacteria (Wolbachia) infect the tissues of insects. These bacteria are then passed very efficiently from mother to offspring, while uninfected females who mate with infected males are essentially sterile. It is hoped that greater understanding of this natural phenomenon might enable others to utilize Wolbachia as part of a strategy to reduce the ability of insect vectors of disease to transmit pathogens.
Holly Harrison
Biological SciencePre-Health Professions Advisor
Office: Moody Life Sciences Center 307
Phone: (210) 436-3241
hharrison@stmarytx.edu
Full Bio Details
Holly earned a Bachelor’s degree in Psychology with a minor in Spanish and a Master of Education degree in Counselor Education at Texas Tech University. She has passed the National Counselor Exam.
At an internship at Texas Tech University, Holly focused on interpreting career assessments such as the Strong Interest Inventory, FOCUS, Myers-Briggs Type Indicator, and StrengthsQuest for students of any major at all stages of career development.
As the Pre-Health Professions advisor she works primarily with freshmen biology majors-keeping students informed of the many career opportunities available within biological sciences; keeping students on track as they pursue their career goals; working together with Career Services and the Service Learning Center to support and coordinate activities related to the Pre-Health Profession programs; and communicating with medical and other health professions schools regarding our students’ application and acceptance to professional programs.
Thomas E. (Ted) Macrini, Ph.D.
Assistant Professor of Biological SciencesOffice: Moody Life Sciences Center 302
Phone: (210) 431-4304
tmacrini@stmarytx.edu
Full Bio Details
B.A., Washington University in St. Louis, 1997
M.S., The University of Texas at Austin, 2000
Ph.D., The University of Texas at Austin, 2006
Thomas E. Macrini, Ph.D., received his bachelor's in biology, and his master's and doctorate in geological sciences with an emphasis in vertebrate paleontology. He completed two postdoctoral fellowships at the American Museum of Natural History in New York, NY. Macrini teaches General Biology I and II, Forensic Osteology, Comparative Anatomy, and Foundations of Reflections: Nature.
Macrini's research focuses on the comparative cranial anatomy of fossil and extant mammals, particularly the internal cranial cavities and associated structures. His studies involve the endocranial and nasal cavities and the bony labyrinth of the ear. Macrini utilizes high-resolution X-ray computed tomography (HRXCT) to non-destructively study the internal cranial osteology of fossil and extant mammalian skulls to document the anatomy of internal cranial cavities, search for new phylogenetic characters, and trace the evolution of sensory structures in the fossil record.
He also is collaborating with Dr. Lorena M. Havill of the Department of Genetics at the Texas Biomedical Research Institute on projects aimed at developing baboons (Papio hamadryas ssp.) as a non-human primate model for studying the genetics, etiology, and prevention of osteoarthritis (OA) in humans. Macrini is currently looking for undergraduate students interested in vertebrate anatomy and systematics for research collaborations.
Selected Publications
Macrini, T. E. 2009. Description of a digital cranial endocast of Bathygenys reevesi (Merycoidodontidae; Oreodonta) and implications for apomorphy-based diagnosis of isolated, natural endocasts. Journal of Vertebrate Paleontology 29:1199-1211.Macrini, T. E., J. J. Flynn, D. A. Croft, and A. R. Wyss. 2010. Inner ear of a notoungulate placental mammal: anatomical description and examination of potentially phylogenetically informative characters. Journal of Anatomy 216:600-610.
Rowe, T., T. E. Macrini, and Z.-X. Luo. 2011. Fossil evidence on origin of the mammalian brain. Science 332:955-957.
Macrini, T. E. 2012. Comparative morphology of the internal nasal skeleton of adult marsupials based on X-ray computed tomography. Bulletin of the American Museum of Natural History 365:1-91.
Lucien C. Manchester, Ph.D.
Professor of Biological SciencesOffice: Moody Life Sciences Center 211
Phone: (210) 431-4320
lmanchester@stmarytx.edu
Full Bio Details
B.A., University of the Virgin Islands
M.A., University of Nebraska (Omaha)
Ph.D., University of Nebraska Medical School, 1983
Born on the Island of St. Kitts in the Caribbean, Lucien C. Manchester, Ph.D. attended the University of the Virgin Islands and received an associate degree and B.A. with honors in biology. He received a pre-doctoral scholarship from the U.S. Department of Public Health to study "Ciguatoxicity and Its Relationship to Colon Carcinogenesis" at the Eppley Cancer Institute, University of Nebraska Medical Center, working under the mentorship of Drs. Phillipe, Shubik, and Melvin Greenblatt. Manchester received post-doctoral training at The University of Texas Medical Branch at Galveston, Texas and The University of Texas Health Science Center in San Antonio, Texas in the Department of Cellular and Structural biology.
One of his primary research focuses is to define the cellular mechanism by which pinealocytes and other melatonin producing cells synthesize and release melatonin. Other research is aimed at investigating biologic importance in photoperiodicity, antioxidantine stress and anti-aging; mechanisms of action of melatonin on the hypothalamo-hypophysical axis particularly in relationship to its anti-gonadal function; and the physical parameters by which light and magnetic fields affect pineal physiology. Awards and recognitions include:
- Distinguished Faculty Award for Excellence in Teaching, 1991
- Marie Hall Research Fellowship U.T.M.B. Galveston, Texas, June-August, 1991
- Trio Achievement Award, Upward Bound, 1992
- Faculty Development Award, Fall, 1994
- Certificate of Appreciation from The University of Texas School of Medicine at Houston: Nomination by entering students to the Doctor of Medicine degree program
- Who's Who in Teaching, 1994 and 1995
Marshall McCue, Ph.D.
Assistant Professor of Biological SciencesOffice: Moody Life Sciences Center 213
Phone: (210) 431-8005
mmccue1@stmarytx.edu
Full Bio Details
B.S., University of Florida, 2001
M.S., University of California Irvine, 2003
Ph.D., University of Arkansas, 2008
McCue is comparative physiologist who seeks to understand how animals have become adapted to cope with the unique challenges presented by their respective environments.
As a graduate student McCue was granted a 3 year fellowship by the National Science Foundation to cover bioenergetic costs and benefits associated with venom production by pit-vipers. As a doctoral student he was granted a four-year fellowship allowing him to research the physiological and biochemical strategies that allow some vertebrates to survive years of starvation. After earning his doctorate, McCue spent two years in Israel supported by the Blaustein Institutes for Desert Research and the Ministry of Education where he mentored undergraduate and graduate students and conducted research to develop novel approaches for using stable isotopes to investigate how animals store and/or breakdown the nutrients in the foods they ingest.
McCue is an active member of the American Physiological Society and the Society for Comparative and Integrative Biology. He teaches general physiology, comparative physiology, and general biology, and is developing a program that will allow St. Mary's students to participate in supervised research in comparative physiology.
Selected Recent Publications
McCue, M.D. 2011. Tracking the oxidative and nonoxidative fates of isotopically labeled nutrients in animals. BioScience. 61(3): 217-230.McCue, M.D., A. Smith, R. McKinney, B. Rewald, B. Pinshow, S.R. McWilliams. 2011. A mass balance approach to identify and compare differential rounting of 13C-labeled carbohydrates, lipids, and proteins in vivo. Physiological and Biochemical Zoology. Physiological and Biochemical Zoology. In press.
McCue, M.D., S.R. McWilliams, B. Pinshow. 2011. Ontogeny and nutritional status influence oxidative kinetics of exogenous nutrients and whole-animal bioenergetics in zebra finches, Taeniopygia guttata. Physiological and Biochemical Zoology. 84(1): 32-42.
McCue, M.D. 2010. Starvation physiology: reviewing the different strategies animals use to survive a common challenge. Comparative Biochemistry and Physiology, 156A: 1-18.
McCue, M.D. 2010. Hyperoxia reduces the costs of digestion in snakes: Investigating the energetic consequences of the paleoatmosphere. Open Access Animal Physiology. 2: 69-79.
McCue, M.D., O. Sivan, S.R. McWilliams, B. Pinshow. 2010. Breath testing reveals the oxidative kinetics of 13C-labeled dietary carbohydrates, amino acids, and fatty acids in house sparrows, Passer domesticus. Journal of Experimental Biology. 213: 782-789.
Gary B. Ogden, Ph.D.
Professor of Biological SciencesOffice: Moody Life Sciences Center 212
Phone: (210) 431-4305
gogden@stmarytx.edu
Full Bio Details
Ph.D., University of Kansas, 1983
Gary B. Ogden earned his doctorate for his studies on the composition of Simian Virus 40 chromatin. His subsequent postdoctoral work at Tufts Medical School uncovered possible roles for DNA-adenine methylation in the segregation of the E. coli chromosome and the timing of new rounds of DNA replication. In 1987, after joining the research staff in the Laboratory of Parasitic Diseases at the National Institutes of Health (NIH), he began to study molecular aspects of microbial pathogenesis, using the protozoan parasite Trypanosoma cruzi as a model. In 1989 he left the NIH to join the research faculty at Yale University's School of Medicine, where he cloned T. cruzi virulence molecules. Since joining St. Mary's in 1991, he has been able to fulfill his long-standing goal of teaching and mentoring undergraduate students, and has continued to study molecular aspects of microbial pathogenesis. Moreover, as an adjunct faculty member in the Department of Microbiology at the University of Texas Health Science Center at San Antonio, he has established collaborative research efforts concerning the development of a genetic vaccine against the protozoan parasite Leishmania.
Ogden's research concerns the study of gene regulation and cell differentiation in Trypanosoma cruzi and Leishmania. He believes that the classical MAP kinase pathway (see figure), which links extracellular differentiation and growth signals to gene expression, is conserved across the evolutionary gap separating mammalian cells from these protozoa. His interests include the identification of parasite genes used in cell signaling and transcriptional activation. He also has ongoing collaborative studies, funded by the Veterans Administration, developing a genetic vaccine against leishmaniasis, and he is also developing molecular methods to detect and identify Leishmania sp. and trypanosomes.
Timothy Raabe, Ph.D.
Chair and Professor of Biological SciencesOffice: Moody Life Sciences Center 306
Phone: (210) 431-4321
traabe@stmarytx.edu
Full Bio Details
B.S., Texas State University (formerly Southwest Texas University), 1989
M.S., Texas State University, 1991
Ph.D., University of Texas at Austin, 1995
Timothy Raabe, Ph.D., joined the laboratory of Dr. George H. DeVries at Loyola and began work on multiple sclerosis (MS). MS is a disease of unknown origin which attacks the myelin (insulation) surrounding the axons of neurons in the central nervous system (brain and spinal cord). The loss of myelin (or demyelination) in the CNS can produce a number of symptoms such as disturbed vision or loss of coordination. The cells responsible for producing myelin in the CNS are termed oligodendrocytes. The oligodendrocytes are not mitotically active in adults so once they are destroyed in MS remyelination is not successful.
His research at Loyola involved using growth factors (molecules that influence oligodendrocyte development) to determine the feasibility of using certain growth factors as possible therapeutic agents. Raabe's work focused on a family of growth factors termed neuregulins. The neuregulins are very important for the development of not only oligodendrocytes, but also Schwann cells which are responsible for myelination in the peripheral nervous system. His research focuses on the ability of both oligodendrocytes and Schwann cells to produce their own neuregulins which may enable these cells to regulate their own survival, differentiation, or proliferation.
Dr. Raabe is also the first Benjamin F. Biaggini Endowed Chair of Biological Sciences at St. Mary’s University.
Veronica Contreras-Shannon, Ph.D.
Associate Professor of Biological SciencesOffice: Moody Life Sciences Center 301
Phone: (210) 431-4324
vcontrerasshann2@stmarytx.edu
Full Bio Details
B.A., University of California at Santa Cruz, 1995
Ph.D., University of Texas Health Science Center at San Antonio, 2003
Veronica Contreras-Shannon, Ph.D., earned her bachelor's in Biology after which she participated in research at Los Alamos National Lab in Los Alamos, New Mexico. Later, she earned her doctorate from the Department of Biochemistry in the Graduate School of Biomedical Sciences. After completing her doctoral work in 2003, she completed two postdoctoral fellowships.
While a graduate student at UTHSCSA, her research elucidated the role of three differentially compartmentalized isozymes of NADP+-dependent isocitrate dehydrogenase in yeast. These studies led to an understanding that these multiple isozymes participate in the shuttle of NADPH reducing equivalents among various cellular compartments and provided strong evidence for isozyme involvement at the intersection of both carbon and nitrogen metabolism.
Her postdoctoral training addressed the molecular mechanisms associated with disease states. During Contreras-Shannon's first fellowship, she examined how the regeneration of damaged muscle was influenced by inflammatory cells following injury. During her second fellowship, she studied the functional role of proteins encoded by genes that were found to be amplified in prostate cancer. She is trained in the Pathobiology of Occlusive Vascular Disease, Immunology, Muscle Regeneration, Genetics and Cancer Biology.
Contreras-Shannon teaches General Biology for Majors, Mechanisms of Disease, Molecular Biology and Endocrinology.
Rosemarie Wahl, Ph.D.
Professor of Biological SciencesOffice: Moody Life Sciences Center 303
Phone: (210) 431-8064
rwahl@stmarytx.edu
Full Bio Details
B.S., Massachusetts Institute of Technology
M.S., University of Chicago
Ph.D., University of Chicago, 1967
Dr. Rosemarie Wahl was born in Chicago and graduated from the Girls Latin School of Chicago. She earned the B.S, degree in Quantitative Biology from MIT, the M.S. in Biochemistry and Ph.D. in Microbiology from the University of Chicago. She has been on the faculty of the University of Illinois at Chicago Circle, Texas Christian University, the University of Texas at Austin, and St. Mary’s University.
Dr. Wahl served as Chair of the Department of Biological Sciences, St. Mary’s University, for 25 years (1979-2004), as well as Chief Advisor for the Health Professions and Chair of the Premedical/Predental Advisory Committee. During her tenure, seven full-time faculty members were recruited and retained, 13 new courses were added to the biology curriculum, external funds totaling $8 million were brought to the university through faculty grant proposals, the application process to medical and dental school was redesigned, the departmental curriculum was tailored to three career goals: teaching and research, the health professions and industry, and approximately 500 St. Mary’s University students were accepted to medical school and 150 to dental school.
Dr. Wahl pioneered in research on DNA. Her research contributions are in the molecular structure of bacterial viruses, the chemical basis of genetic mutation and the mechanism of DNA replication.
Dr. Wahl’s memberships include the American Society of Microbiology, Texas Genetics Society, Sigma Xi Honor Society, and the Texas Association of Advisors for the Health Professions (serving on the executive committee). She is presently a Vice-President of her class of MIT Alumni/ae.
Dr. Wahl has received the Distinguished Faculty Award from St. Mary’s University School of Science, Engineering and Technology. Her biography is included in the Marquis publications: Who’s Who in America, Who’s Who among American Women, Who’s Who in Education and Who’s Who in Medicine and Health Care.
Dr. Wahl currently teaches Genetics and Molecular Biology lecture/laboratory courses for science majors and Food and Nutrition I and II for non-science majors.
