What we found on the web about HIAPP
Human IAPP (hIAPP) is amyloidogenic and in vitro studies have shown that early aggregates or oligomers of hIAPP are cytotoxic, leading to β-cell death via apoptosis (12, 22).
Any photographer can vouch for the difficulty of capturing a clear picture ... in type II diabetes has been linked to toxic clumps of the protein hIAPP (human ...
To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. In this study, we found that after a long-term ...
It is known that insulin, which is co-secreted with hIAPP from the beta-cell, acts as an inhibitor of hIAPP’s oligomerization and eventual aggregation.
The resulting new (hIAPP×GKKO) line of mice had higher basal plasma glucose ... no islet amyloid was observed in GKKO mice lacking the hIAPP transgene (0 of 13) ...
Why do hIAPP oligomers (and amyloid) form? Given the potent mechanisms in place to prevent intracellular oligomerization of amyloidogenic proteins such as hIAPP, why does this fail in ...
Decreasing the activity of TRPV4 prevented hIAPP-induced [Ca(2+)](i) changes, reduced hIAPP-triggered ER stress and improved cell viability. PMID: 18751967 [PubMed - indexed for ...
hIAPP transgenic mice (C57BL/6 x DBA/2) were bred from a previously described ... These mice produce hIAPP in their islets and secrete the peptide with insulin in ...
Aim 2: To study the mechanism of hIAPP oligomer/protofibril formation on the surface of membrane liposomes and to determine the size of the aggregates leading to pore formation and ...
The presence of fibrillar protein deposits (amyloid) of human islet amyloid polypeptide (hIAPP) in the pancreatic islets of Langerhans is thought to be related to death of the ...
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