Abstract
Amylin is a fibrillogenic protein co‐secreted with insulin from pancreatic beta cells. Amylin has been shown to function in metabolism through its influence on glucose homeostasis, which includes sending satiety signals to the brain, inhibiting glucagon secretion and delaying gastric emptying. In addition to amylin's direct role on metabolism it has also been proposed to have an impact on amyloid beta, a major component of the amyloid plaques found in Alzheimer's disease. Alzheimer's disease brains have been shown to have amyloid plaque formation and decreased expression of Uncoupling Protein 2 (UCP2), which is a protein that also has a role in metabolism. Traditionally, uncoupling proteins have been known to function as mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane resulting in the dissipation of energy in the form of heat. Knowing that UCP2 is expressed in pancreatic beta cells and has been shown to have diminished levels in Alzheimer's disease brains the focus of this study was to examine the influence of UCP2 on the presence and expression of amylin in RIN‐5F cells (a pancreatic beta cell line). siRNA UCP2 constructs were created and immunocytochemistry experiments and ELISA assays were conducted to examine the presence of amylin and the activity level of amylin, respectively. Initial studies suggest that inhibition of UCP2 may impact the activity level and presence of amylin.Support or Funding InformationTameka Clemons at Spelman College Department of Chemistry and BiochemistryThis abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Published Version
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