Open AccessAmylin under examination. Fibrillogenic potential of the troublesome molecule
Author(s) -
Małgorzata Marszałek
Publication year - 2018
Publication title -
postępy higieny i medycyny doświadczalnej
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.275
H-Index - 34
eISSN - 1732-2693
pISSN - 0032-5449
DOI - 10.5604/01.3001.0011.7620
Subject(s) - amylin , diabetes mellitus , amyloid (mycology) , beta cell , disease , pancreas , insulin , islet , pathological , type 2 diabetes mellitus , medicine , cell , chemistry , endocrinology , pancreatic islets , biochemistry , pathology
In patients or animals affected by 2 type diabetes mellitus (diabetes mellitus type 2 DM2, non-insulin dependent diabetes mellitus NIDDM) some pathological deposits, called amyloid are observed among cells of islets of Langerhans. Among others constituents deposits consist of insoluble, fibrillar form of polipeptide neurohormone called amylin, produced by pancreatic beta cells.. It is thought that formation of fibrillar deposits of misfolded and aggregated polipeptide is highly toxic to beta cells and leads to cell dysfunction, cell loss, pancreas destruction and progress of the disease. Due to the extreme insolubility of this polipeptide and its instant fibrillation amylin constitutes a methodological problem and there is a need for a special methodology in experiments. This article reviews the most important experiments aimed at discovering fibrillogenic potential of amylin and models of interaction of the polipeptide’s monomers in man and rat. Numerous methodological difficulties in amylin research has been also emphasized.