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Characterization and Comparison of Human IAPP to Animal IAPPs
Author(s) -
Torres Jaris,
Lamba Arleen,
Nogaj Luiza A.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.04822
Subject(s) - islet , amyloid (mycology) , viability assay , hela , cytotoxicity , protein aggregation , population , biochemistry , cell , chemistry , toxicity , microbiology and biotechnology , biology , insulin , in vitro , endocrinology , medicine , inorganic chemistry , environmental health , organic chemistry
Islet Amyloid Polypeptides (IAPPs), are insoluble amyloids or small oligomers that are notorious for aggregating into deposits that destroy pancreatic β‐islet cells, the primary producers of insulin. The aggregation of the 37‐amino acid polypeptide human islet amyloid polypeptide (hIAPP) seems to play a role in this aggregation and cell death process. IAPP aggregation has been associated with the development of type II diabetes, a disease that affects 30.3 million people of all ages—or 9.4% of the U.S. population, and is an epidemic that has devastated the lives of many. MTT assays were performed to assess cell viability of HeLa cells that were treated with the IAPPs of various animals. Subsequently, LDH Cytotoxicity assays were conducted to test the viability of the cellular membrane upon addition of the same IAPPs. This research explores the relationship between the IAPP sequences, their propensity to aggregate, and their effect on mammalian cell viability. To do this we compared aggregation potential and cellular toxicity of full‐length IAPP from several diabetic and nondiabetic organisms whose aggregation propensities had not yet been determined for full‐length IAPP.