The Effect of Cholesterol on Membrane-Bound Islet Amyloid Polypeptide
نویسندگان
چکیده
منابع مشابه
Islet amyloid polypeptide toxicity and membrane interactions.
Islet amyloid polypeptide (IAPP) is responsible for amyloid formation in type 2 diabetes and contributes to the failure of islet cell transplants, however the mechanisms of IAPP-induced cytotoxicity are not known. Interactions with model anionic membranes are known to catalyze IAPP amyloid formation in vitro. Human IAPP damages anionic membranes, promoting vesicle leakage, but the features that...
متن کاملConserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide.
The conversion of soluble protein into beta-sheet-rich amyloid fibers is the hallmark of a number of serious diseases. Precursors for many of these systems (e.g., Abeta from Alzheimer's disease) reside in close association with a biological membrane. Membrane bilayers are reported to accelerate the rate of amyloid assembly. Furthermore, membrane permeabilization by amyloidogenic peptides can le...
متن کاملA foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide.
A small molecule, protein mimetic based approach is shown to specifically inhibit lipid catalysed self-assembly of islet amyloid polypeptide (IAPP). The lipid-bound oligomerization of this peptide is implicated in cellular dysfunction of insulin secreting β-cells in type II diabetes.
متن کاملIslet amyloid polypeptide, islet amyloid, and diabetes mellitus.
Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptyi...
متن کاملInhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation.
Human islet amyloid polypeptide (hIAPP), co-secreted with insulin from pancreatic beta cells, misfolds to form amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). Like many amyloidogenic proteins, hIAPP is membrane-active: this may be significant in the pathogenesis of NIDDM. Non-fibrillar hIAPP induces electrical and physical breakdown in planar lipid bilayers, and IAPP insert...
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ژورنال
عنوان ژورنال: Frontiers in Molecular Biosciences
سال: 2021
ISSN: 2296-889X
DOI: 10.3389/fmolb.2021.657946