Sponsored by the Dr. Scholl Foundation, this award goes to a graduate student who has performed outstanding research as demonstrated by the submission/publication of a first author manuscript in a peer-reviewed journal.
My recent publication highlighted the role of AMP-activated protein kinase (AMPK) in mouse egg activation. This research, published on the March, 2013 issue of the Biology of Reproduction, sheds light on the multifunctional role of the energy sensor, AMPK, in meiosis. Our lab has previously demonstrated the role of AMPK in meiotic resumption and later completion of the oocyte maturation (meiosis I). As a continuation of the previous work, this recent publication described the role of AMPK beyond oocyte maturation. Normally, meiosis II (egg activation process) is initiated after the sperm fertilization in the mammalian oocyte, and keeping the oocyte from entering meiosis II in the absence of sperm fertilization, is crucial for normal embryonic development. I demonstrated that activation of AMPK prevents chemically induced and spontaneous oocyte activation by regulating MAPK signaling. We were also able to show that AMPK promotes anaphase onset by regulating spindle assembly checkpoint activity. These findings are important since it links the energy sensor with gametogenesis. More importantly, the data support the multifunctional role of AMPK in the entire sequence of events, involving oocyte maturation and subsequent activation.
This award recognizes exceptional
academic achievement by a graduate student in the Ph.D. program. This award will
be based on grade point average (GPA), research activity and scholarly
The focus of my research is to study Urea amidolyase, a promising target for treatment of systemic candidiasis and other infectious diseases. Urea amidolyase harbors two enzyme activities, urea carboxylase and allophanate hydrolase. Its overall activity requires the coordination of four domains, which offers a good model to study the catalytic mechanism of multi-domain enzymes. I am studying the structure and function of urea amidolyase, both by researching the mechanism of individual domains and by investigating the coordination among domains.
First, the mechanism of catalysis and substrate specificity of allophanate hydrolase was investigated using x-ray crystallography and enzyme kinetics. In addition to that, a yeast genetic screen was used to reveal key functional residues in the allophanate hydrolase domain of urea amidolyase. The domain coordination between allophanate hydrolase and urea carboxylase were studied using co-purification and substrate channeling assays. Currently, I am working to solve the overall structure of urea amidolyase. These efforts will further elucidate the mechanism of specificity and coordination for different domains in multi-functional enzymes.
An annual scholarship from the Dr. Catherine Grotelueschen Scholarship Fund for Biology is awarded to provide financial assistance toward the summer research of a graduate student.
The big picture purpose of Cassie Nelson's dissertation work is to better understand the mechanisms of skeletal muscle fatigue. This is clinically relevant in situations such as respiratory or cardiac failure, where the mechanical machinery of the muscle no longer can functionally perform. A better understanding of what is happening in a single muscle cell can shed light on possible therapies for these diseases in the future.
This summer, Cassie Nelson plans to assess the effects of acidosis and myosin light chain phosphorylation on the efficiency of single muscle fibers using the ATPase assay. This assay essentially measures the rate of ATP hydrolysis or how fast ATP is being used and is an indication of the muscle's efficiency. Cassie will do these experiments during isometric and shortening muscle contractions.
Cassie is is also a recipient of Marquette University's Arthur J Schmitt Fellowship for 2013. This fellowship carries a ten-month stipend and is awarded to doctoral candidates who show exceptional leadership ability and strong scholarship. She helps mentor and guide the undergraduates in her lab with their research and independent thinking skills. She is also a part of the Preparing Future Faculty program at Marquette and hopes to take what she learns from this program into a future career as a faculty member. She teaches an 8th grade faith formation class at St Mary Parish in Hales Corners, WI. Cassie's husband is the head cross country coach at Marquette, and she occasionally works with and helps coach his athletes.
Four travel awards are awarded annually on a competitive basis to graduate students who present their work as first author at a scientific conference.
Mentor: Stephen Downs
2012 Society for the Study of Reproduction Annual Meeting, Penn State University, State College, PA
“Fatty Acid Oxidation and Hormone-Induced Meiotic Resumption in Mouse Oocytes”
Mentor: Martin St. Maurice
23rd Enzyme Mechanism Conference,
Coronado Bay, CA
113th General Meeting-
Annual Society for Microbiology,
Experimental Biology 2013 Boston, MA
Competitive scholarships are available for graduate students who attend off-campus courses or specialized symposia, such as those at Woods Hole or Cold Spring Harbor Biological Stations.
Josh Garlich will be attending the FinMIT International Summer School in Vaasky, Finland, on June 1-8. The topic Josh will be studying is "Mitochondria and Organelle Communication." The summer school includes an intensive lecture series given by international research leaders on topics such as; mitochondrial dynamics and turnover, peroxisome biogenesis, organelles and neurodegeneration, mitochondrial lipid metabolism and signaling, E/R mitochondria interactions, intracellular transport, endosomes, lysosomes and autophagosomes.
Prince will be attending an intensive six and a half week course on Microbial Diversity at the Marine Biological Laboratory in Woods Hole, MA. This course will teach microbiological techniques for working with a broad range of microbes, and approaches for recognizing the metabolic, phylogenetic, and genomic diversity of bacteria.