The mechanism
of islet amyloid polypeptide toxicity is membrane disruption by intermediate - sized toxic amyloid particles
Islet amyloid deposits, composed predominantly of a misfolded and aggregated form
of the islet amyloid polypeptide (IAPP), are observed in > 90 % of patients with T2D (Westermark, 1972; Clark et al., 1988; Betsholtz et al., 1989; Johnson et al., 1989).
To corroborate the findings, the researchers also developed a novel mouse model that was deficient for autophagy specifically in beta cells with expression of the human form
of islet amyloid polypeptide.
Not exact matches
People with Type 2 diabetes have an excess
of a protein called
islet amyloid polypeptide, or IAPP, and the accumulation
of this protein is linked to the loss
of insulin - producing pancreatic beta cells.
Islet amyloid polypeptide (IAPP): cDNA cloning and identification
of an amyloidogenic region associated with the species - specific occurrence
of age - related diabetes mellitus
The 37 - amino - acid
polypeptide amylin is the principal constituent
of the
amyloid deposits that form in the
islets of Langerhans in patients with type - 2 diabetes mellitus, but its role in the pathogenesis
of this disease is unresolved.
Pancreatic
islet amyloid, formed from
islet amyloid polypeptide, is found in 96 %
of Type II (non-insulin-dependent) diabetic patients.