Better Futures for Iowans Program - 2015-2016 Grant Awards

Through the FUTURE in Biomedicine℠ program, the University of Iowa Carver College of Medicine is committed to:

• Fostering closer research collaborations between its faculty and those of primarily undergraduate institutions throughout the state of Iowa.
• Mentoring talented undergraduates who will be our next generation of physicians and biomedical scientists.
• Promoting opportunities to translate biomedical discoveries and methods into educational materials used in Iowa's college classrooms.
• Making its research facilities available to a statewide network of scientist-educators.

Consistent with these commitments, the goal of the Better Futures for Iowans program is to make state-of-the-art core research facilities at the University of Iowa available to academic classes and research projects conducted primarily by undergraduates at 2-year and 4-year institutions in Iowa.

Faculty throughout the state are eligible to apply for small grants to support laboratory-intensive projects involving undergraduate students in "hands-on" inquiry.  Students take responsibility for the preparation of samples and analysis of data obtained.  All participants are invited to present a poster about their work at the FUTURE in Biomedicine℠ Research Symposium.  This activity, which was initiated with support from the Office of the Provost in 2013, extends University resources to Iowans and addresses an important goal of the University Strategic Plan - to provide better futures for Iowans.

2015-2016 Grant Recipients

Drake University - Heidi Sleister, PhD and Jerry Honts, PhD

"We have recently discovered that two Tetrahymena cytoskeletal proteins (Epc1 and Fen1) that we are studying form an unusual type of phase-separated liquid droplets. A number of publications this year have described the role of protein droplets formed by association of protein and RNA, such as P-bodies involved in mRNA storage and turnover. In at least one other case, cytoskeletal proteins have been found to form similar structures. Students working with Dr. Sleister have just completed construction of bacterial expression plasmids for GFP-tagged versions of Fen1. This fall we obtained our first images of liquid droplets formed by GFP-tagged versions of the Epc1 protein, which although similar to others reported in the literature, also appear to have novel structural features. We are also working to construct versions of the mRNAs encoding these proteins with engineered fluorescent RNA aptamers for visualization studies, to see if as in other systems, messenger RNA molecules associate with these liquid droplet structures. We propose to use the Central Microscopy Facility's new confocal microscope to image the 3D structures of these unusual structures, which are revolutionizing our understanding of organization of the cytoplasm of cells."

Heidi Sleister, PhD and Jerry Honts, PhD
BFFI Awardees

Drake University - Adina Kilpatrick, PhD

"Many protist cells use an ATP-independent form of contractile motility, which results from the calcium-triggered contraction of filaments containing novel structural and/or calcium-binding proteins. Several such proteins were previously identified during proteomic analysis of contractile fibers isolated from the membrane-associated cytoskeleton of the ciliated protozoan Tetrahymena thermophila, including the putative calcium-binding protein Tcb2 and the filament-forming structural protein Epc1. The goal of this project is to investigate the structure and dynamics of the two-domain protein Tcb2. The full-length protein and its N-terminal domain are not amenable to high-resolution structure determination, as they tend to aggregate in the presence of calcium and/or upon concentration. However, the C-terminal domain (Tcb2-C) is highly soluble at both low and high calcium concentrations. Solution NMR HSQC spectra of 15N-labeled Tcb2-C indicate that the protein is well folded in the presence and absence of calcium, and undergoes a dramatic conformational change upon calcium addition. We expressed and purified 15N, 13C-labeled Tcb2-C, and assigned the chemical shifts of the main chain and aliphatic and aromatic side chains of the protein at both low and calcium concentrations. NMR structure determination of calcium-free and calcium-bound Tcb2-C is currently underway. For this grant, we propose to acquire additional NMR experiments to quantify the calcium-binding properties of the domain and investigate its conformational dynamics. These studies will establish a structural basis for elucidating the function of Tcb2."

Adina Kilpatrick, PhD
BFFI Awardee

Grand View University - Michael LaGier, PhD

"Funds are requested to support an undergraduate project to characterize a putative catalase and superoxide dismutase from the bacterium Deinococcus maricopensis. D. maricopensis has potential as a bioremediation agent due to its resistance to environmental stressors including oxidative damage. The genome of the bacterium has recently been sequenced as part of the GEBA (Genomic Encyclopedia of Bacteria and Archaea) project headed by the Joint Genome Institute of the Department of Energy. A goal of GEBA is to better capture the diversity of the microbial world via genomic sequencing. A secondary goal of GEBA is to provide undergraduates an opportunity to contribute to genomics research, through the MGAN (Microbial Genome Annotation Network, supported by the National Science Foundation) network. Grand View is part of MGAN, and as part of this group, has access to bioinformatics tools geared at genome annotations. I am currently working with undergraduate mentees to more closely examine the genomic content of D. maricopensis. In particular, we are collecting and annotating genes believed to be related to stress tolerance phenotypes. The funding requested here will help support these efforts, by providing a means to validate our bioinformatics work via molecular biology techniques. In this project, mentees will clone, sequence, and functionally characterize (in Escherichia coli hosts) putative catalase and superoxide dismutase genes from D. maricopensis."

Michael LaGier, PhD
BFFI Awardee

Mount Mercy University - Joseph Nguyen, PhD

"The purpose of this class project is for the students to determine whether name-brand (Aleve) and generic (CVS and Equate) sodium naproxen are similar. The students are challenged to find or establish procedures that will help them determine this, including isolating, confirming the presence of, and quantifying the amount of the active species as well as the bioefficacy of the drug using a wide variety of instruments and experiments. At Mount Mercy University, we have a 90 MHz NMR spectrometer, but the power supply had broken, so the students could not determine the presence of the active ingredient. Thus, we have approached the CCOM NMR facilities to help the class accomplish one of their tasks. "

Joseph Nguyen, PhD
BFFI Awardee

Mount Mercy University - Kristopher Keuseman, PhD

Glucosamine is commonly used by horse owners to improve mobility and decrease pain associated with osteoarthritis. Despite a large amount of anecdotal evidence for positive therapeutic outcomes, the veterinary literature provides no clear evidence for increased blood serum glucosamine levels after oral or IV administration of glucosamine preparations. The proposed study would seek to study how blood serum glucosamine levels change during administration of oral and IV glucosamine preparations. The study will also compare serum glucosamine concentration to qualitative metrics of mobility and pain in the animals participating in the study. /  / To determine serum glucosamine concentrations, whole blood samples will be collected each day for one week prior to treatment with glucosamine. After glucosamine treatment, whole blood samples will be collected each day and qualitative measurements of mobility and pain will be made. Post administration sampling will continue for one week. /  / We intend to use the University of Iowa Mass Spectroscopy facility to identify glucosamine in prepared serum samples. Quantification will be done using High-Performance Liquid Chromatography at Mount Mercy University. /  / This study will be conducted by Mount Mercy University undergraduate student Mikayla Calloway in collaboration with Prof. Kristopher Keuseman. 

Kristopher Keuseman, PhD
BFFI Awardee

Waldorf College - Gary Coombs, PhD

During the summer of 2015, as participants in the FUTURE in Biomedicine program, Maria Valdes (a Waldorf student) and I conducted studies in Lori Wallrath's lab that demonstrated defects in protein folding and redox homeostasis resulted from expressing lamins in Drosophila with mutations in the head, rod, or Ig-fold domain. We developed a technique using video analysis to quantitate larval locomotion defects, quantitated survival of pupation, and tested several RNAi or overexpression strategies to rescue survival in flies expressing a lamin mutant that normally results in less than 2% survival. Several strategies resulted in up to 30-fold rescue. Another student, Gulnara Novbatova, has taken on the characterization here at Waldorf College of two more mutations known to cause human muscular dystrophy. To date she has quantitated their locomotion defect and determined percent survival to adulthood relative to wild type expressing flies. As a continuation of the project, arrangements have been made for her to spend a week in Iowa City so she can dissect larval muscle, learn to stain for lamin C and possibly for a DNA damage marker, and then perform fluorescence confocal microscopy on the prepared samples with Dr. Wallrath. We hope to be able to publish these results as a follow-up to a manuscript in preparation on the studies performed over the summer. I am requesting support for the microscopy to be performed with Dr. Wallrath’s assistance in December. 

Gary Coombs, PhD
BFFI Awardee