Recombinant human islet amyloid polypeptide forms shorter fibrils and mediates β-cell apoptosis via generation of oxidative stress

• Published in: Biochemical journal Vol. 474; no. 23; p. 3915
• Main Authors: Dubey, Richa, Minj, Pooja, Malik, Nikita, Sardesai, Devika M, Kulkarni, Shruti H, Acharya, Jhankar D, Bhavesh, Neel Sarovar, Sharma, Shilpy, Kumar, Ashutosh
• Format: Journal Article
• Language: English
• Published: England 01.12.2017
• Subjects: Apoptosis - drug effects; bcl-2-Associated X Protein - biosynthesis; Caspase 3 - biosynthesis; Catalase - biosynthesis; Cell Line; Gene Expression Regulation - drug effects; Humans; Insulin-Secreting Cells - metabolism; Insulin-Secreting Cells - pathology; Islet Amyloid Polypeptide - chemistry; Islet Amyloid Polypeptide - pharmacology; Oxidative Stress - drug effects; Proto-Oncogene Proteins c-bcl-2 - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - pharmacology; Superoxide Dismutase-1 - biosynthesis; apoptosis; human islet amyloid polypeptide; amyloid; solid-state NMR; type 2 diabetes

Protein misfolding and aggregation play an important role in many human diseases including Alzheimer's, Parkinson's and type 2 diabetes mellitus (T2DM). The human islet amyloid polypeptide (hIAPP) forms amyloid plaques in the pancreas of T2DM subjects (>95%) that are involved in deterio...