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- W3173284907 abstract "Although the role of amyloid beta in Alzheimer's disease has been studied for decades, the link between amyloid beta and amylin is fairly new. Amylin is a protein that is co-secreted from pancreatic beta cells alongside insulin and has been shown to cross the blood-brain barrier and impact the formation of amyloid plaques. The normal function of amylin in the brain is directly correlated to metabolism because amylin is considered a satiety protein. The output involved in the metabolic process involves oxidative phosphorylation and includes a set of proteins known as uncoupling proteins (UCPs), which are proteins that directly impact oxidative phosphorylation. Traditionally, UCPs are known to impact the ATP levels that occur in oxidative phosphorylation. However, recently it has been postulated that UCPs may have an additional role that involves cell signaling. In fact, UCP2 has been shown to be present in pancreatic beta cells and to have diminished protein levels in Alzheimer's disease brains. The experiments conducted in this study analyzed the relationship between UCP2 and amylin. Specifically, immunohistochemistry experiments that examine both the presence of amylin and UCP2 in Alzheimer's disease brains were conducted. Western Blot analysis experiments were also conducted to compare the findings from the immunohistochemistry experiments. The initial studies suggest that the role of UCP2 may influence the role of amylin or the role of amylin may influence the role of UCP2. Support or Funding Information National Science Foundation Research Initiation Award #24430 This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal." @default.
- W3173284907 created "2021-07-05" @default.
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- W3173284907 date "2019-04-01" @default.
- W3173284907 modified "2023-09-27" @default.
- W3173284907 title "Presence of UCP2 and Amylin in human Alzheimer's disease brains" @default.
- W3173284907 doi "https://doi.org/10.1096/fasebj.2019.33.1_supplement.632.11" @default.
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