Diabetes is the seventh leading cause of death in the United States, and nearly 34% of U.S. adults are prediabetic. CTRP3 is an adipose secreted protein that has shown to play a key role in glucose metabolism and insulin sensitivity, however, the research on CTRP3 total levels and its relationship to type 2 diabetes is controversial. The oligomeric state (protein structure) of CTRP3 in relation to metabolic dysfunction has not been studied. This study will be the first analysis of the circulating forms of CTRP3 in human blood. Hypothesis: The relative circulating amounts of the three oligomeric states of CTRP3 will differ in patients with type 2 diabetes. Methods: Human serum samples are analyzed using western blotting under native, reduced non-denaturing, and denaturing conditions. Results: In reducing non-denaturing conditions, three oligomeric states of CTRP3 were visualized in human serum: the high molecular weight (HMW) oligomer, the low molecular weight (LMW) oligomer, and the trimer. Conclusion: Reduced, non-denaturing conditions appear to yield the most effective separation of the three oligomeric states of CTRP3, and further studies aim to observe a difference in oligomeric state with a diabetic phenotype. Investigating the relationship of CTRP3’s oligomeric state with diabetic phenotype could present novel understanding of this protein’s possible protective effects against certain metabolic disorders.
Identifer | oai:union.ndltd.org:ETSU/oai:dc.etsu.edu:asrf-1181 |
Date | 05 April 2018 |
Creators | Trogen, Greta, Peterson, Jonathan M |
Publisher | Digital Commons @ East Tennessee State University |
Source Sets | East Tennessee State University |
Detected Language | English |
Type | text |
Format | application/pdf |
Source | Appalachian Student Research Forum |
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