Membrane permeabilization by Islet Amyloid Polypeptide [PDF]
Chemistry and Physics of Lipids, 2009 Membrane permeabilization by Islet Amyloid Polypeptide (IAPP) is suggested to be the main mechanism for IAPP-induced cytotoxicity and death of insulin-producing -cells in type 2 diabetes mellitus (T2DM).
Engel, Maarten F.M.
core +4 more sources
O-glycosylated peptides curtail the aggregation and toxicity of human islet amyloid polypeptide [PDF]
Communications BiologyA key pathogenetic pathway of type 2 diabetes (T2D) is pancreatic beta cell failure, losing their capability of producing insulin and regulating blood glucose.
Qian Zhang +9 more
doaj +2 more sources
Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology [PDF]
Journal of Diabetes Research, 2016 The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes to β-cell dysfunction and death in the disease and to the failure of ...
Rehana Akter +10 more
doaj +5 more sources
Islet amyloid polypeptide aggregation exerts cytotoxic and proinflammatory effects on the islet vasculature in mice. [PDF]
Diabetologia, 2022 Castillo JJ +10 more
europepmc +2 more sources
Profiling the serum protein corona of fibrillar human islet amyloid polypeptide [PDF]
ACS Nano, 2018 Amyloids may be regarded as native nanomaterials that form in the presence of complex protein mixtures. By drawing an analogy with the physicochemical properties of nanoparticles in biological fluids, we hypothesized that amyloids should form a protein ...
Davis, Thomas P. +10 more
core +3 more sources
Single-molecular hetero-amyloidosis of human islet amyloid polypeptide.
Nano Letters, 2019 Human amyloids and plaques uncovered post mortem are highly heterogeneous in structure and composition, yet literature concerning the hetero-aggregation of amyloid proteins is extremely scarce. This knowledge deficiency is further exacerbated by the fact
Aleksandr Kakinen +12 more
semanticscholar +5 more sources
Structural and morphological dynamics of "on-path" and "off-path" oligomers of human islet amyloid polypeptide. [PDF]
Protein SciAbstract The deposition of cytotoxic human islet amyloid polypeptide (IAPP) aggregates is a hallmark feature of Type 2 Diabetes. However, the structural evolution and cytotoxicity of IAPP aggregate species remain poorly understood. This study combines kinetics, biophysical and cell assays to resolve the morphological dynamics of IAPP aggregation. Using
Warren D, Sitton J, Kurouski D.
europepmc +2 more sources
The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells. [PDF]
PLoS ONE, 2015 Amyloid formation and mitochondrial dysfunction are characteristics of type 2 diabetes. The major peptide constituent of the amyloid deposits in type 2 diabetes is islet amyloid polypeptide (IAPP).
Hanjun Guan +5 more
doaj +1 more source
International Journal of Biological Macromolecules, 2022 Type 2 diabetes (T2D), a chronic metabolic disease characterized by hyperglycemia, results in significant disease burden and financial costs globally.
Anns Mahboob +5 more
semanticscholar +1 more source
SORLA mediates endocytic uptake of proIAPP and protects against islet amyloid deposition
Molecular Metabolism, 2022 Objective: Sorting-related receptor with type A repeats (SORLA) is a neuronal sorting receptor that prevents accumulation of amyloid-beta peptides, the main constituent of senile plaques in Alzheimer disease. Recent transcriptomic studies show that SORLA
Alexis Z.L. Shih +6 more
doaj +1 more source