The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet Î² cells

S Zhang; Hong Liu; Chia Lin Chuang; Xiaoling Li; M Au; Lin Zhang; Anthony R. J. Phillips; David W. Scott; Garth Cooper

doi:10.1096/fj.14-251744

The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet Î² cells

S Zhang
, Hong Liu
, Chia Lin Chuang
, Xiaoling Li
, M Au
, Lin Zhang
, Anthony R. J. Phillips
, David W. Scott
, Garth Cooper

University of Auckland

Research output: Contribution to journal › Article › peer-review

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Abstract

The aggregation of human amylin (hA) to form cytotoxic structures has been closely associated with the causation of type 2 diabetes. We sought to advance understanding of how altered expression and aggregation of hA might link Î²-cell degeneration with diabetes onset and progression, by comparing phenotypes between homozygous and hemizygous hA-transgenic mice. The homozygous mice displayed elevated islet hA that correlated positively with measures of oligomer formation (r=0.91; P

Original language	English
Article number	fj.14-251744.
Pages (from-to)	5083-5096
Number of pages	13
Journal	The F A S E B Journal
Volume	28
Issue number	12
DOIs	https://doi.org/10.1096/fj.14-251744
Publication status	Published - 19 Aug 2014

Keywords

gene-dosage effect, apoptosis, peptide, aggregation, transgenic mice, insulin resistance

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1096/fj.14-251744

POST-PEER-REVIEW-PUBLISHERS.PDFFinal published version, 1.2 MB

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AU - Zhang, S

AU - Liu, Hong

AU - Chuang, Chia Lin

AU - Li, Xiaoling

AU - Au, M

AU - Zhang, Lin

AU - Phillips, Anthony R. J.

AU - Scott, David W.

AU - Cooper, Garth

PY - 2014/8/19

Y1 - 2014/8/19

N2 - The aggregation of human amylin (hA) to form cytotoxic structures has been closely associated with the causation of type 2 diabetes. We sought to advance understanding of how altered expression and aggregation of hA might link Î²-cell degeneration with diabetes onset and progression, by comparing phenotypes between homozygous and hemizygous hA-transgenic mice. The homozygous mice displayed elevated islet hA that correlated positively with measures of oligomer formation (r=0.91; P

AB - The aggregation of human amylin (hA) to form cytotoxic structures has been closely associated with the causation of type 2 diabetes. We sought to advance understanding of how altered expression and aggregation of hA might link Î²-cell degeneration with diabetes onset and progression, by comparing phenotypes between homozygous and hemizygous hA-transgenic mice. The homozygous mice displayed elevated islet hA that correlated positively with measures of oligomer formation (r=0.91; P

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DO - 10.1096/fj.14-251744

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JO - The F A S E B Journal

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ER -

The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet Î² cells

Abstract

Keywords

UN SDGs

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