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10.1073/pnas.1715951115 http://scihub22266oqcxt.onion/10.1073/pnas.1715951115 C5866560!5866560 !29507232     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29507232 &cmd=llinks): Failed to open stream: HTTP request failed! 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BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells |pdf=|usr=}}{{29507232 }} gab.com Text BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29507232 #FOAvip Aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils in islets of Langerhans is associated with type 2 diabetes, and formation of toxic IAPP species is believed to contribute to the loss of insulin-producing beta cells. The BRICHOS domain of integral membrane protein 2B (Bri2), a transmembrane protein expressed in several peripheral tissues and in the brain, has recently been shown to prevent fibril formation and toxicity of A?42, an amyloid-forming peptide in Alzheimer disease. In this study, we demonstrate expression of Bri2 in human islets and in the human beta-cell line EndoC-?H1. Bri2 colocalizes with IAPP intracellularly and is present in amyloid deposits in patients with type 2 diabetes. The BRICHOS domain of Bri2 effectively inhibits fibril formation in vitro and instead redirects IAPP into formation of amorphous aggregates. Reduction of endogenous Bri2 in EndoC-?H1 cells with siRNA increases sensitivity to metabolic stress leading to cell death while a concomitant overexpression of Bri2 BRICHOS is protective. Also, coexpression of IAPP and Bri2 BRICHOS in lateral ventral neurons of Drosophila melanogaster results in an increased cell survival. IAPP is considered to be the most amyloidogenic peptide known, and described findings identify Bri2, or in particular its BRICHOS domain, as an important potential endogenous inhibitor of IAPP aggregation and toxicity, with the potential to be a possible target for the treatment of type 2 diabetes. Twit Text FOAVip BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29507232 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29507232 #FOAvip English Wikipedia <ref>{{Cite pmid|29507232 }}</ref> BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells #MMPMID29507232 Oskarsson ME ; Hermansson E ; Wang Y ; Welsh N ; Presto J ; Johansson J ; Westermark GT Proc Natl Acad Sci U S A 2018[Mar]; 115 (12 ): E2752-E2761 PMID29507232 show ga Aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils in islets of Langerhans is associated with type 2 diabetes, and formation of toxic IAPP species is believed to contribute to the loss of insulin-producing beta cells. The BRICHOS domain of integral membrane protein 2B (Bri2), a transmembrane protein expressed in several peripheral tissues and in the brain, has recently been shown to prevent fibril formation and toxicity of A?42, an amyloid-forming peptide in Alzheimer disease. In this study, we demonstrate expression of Bri2 in human islets and in the human beta-cell line EndoC-?H1. Bri2 colocalizes with IAPP intracellularly and is present in amyloid deposits in patients with type 2 diabetes. The BRICHOS domain of Bri2 effectively inhibits fibril formation in vitro and instead redirects IAPP into formation of amorphous aggregates. Reduction of endogenous Bri2 in EndoC-?H1 cells with siRNA increases sensitivity to metabolic stress leading to cell death while a concomitant overexpression of Bri2 BRICHOS is protective. Also, coexpression of IAPP and Bri2 BRICHOS in lateral ventral neurons of Drosophila melanogaster results in an increased cell survival. IAPP is considered to be the most amyloidogenic peptide known, and described findings identify Bri2, or in particular its BRICHOS domain, as an important potential endogenous inhibitor of IAPP aggregation and toxicity, with the potential to be a possible target for the treatment of type 2 diabetes. |Adaptor Proteins, Signal Transducing [MESH] |Amyloid/*metabolism [MESH] |Animals [MESH] |Animals, Genetically Modified [MESH] |Apoptosis/physiology [MESH] |Brain/metabolism/pathology [MESH] |Cells, Cultured [MESH] |Diabetes Mellitus, Type 2/*metabolism/pathology [MESH] |Drosophila melanogaster/genetics [MESH] |Female [MESH] |Glucose/pharmacology [MESH] |Humans [MESH] |Insulin-Secreting Cells/*metabolism/pathology [MESH] |Islet Amyloid Polypeptide/genetics/*metabolism [MESH] |Islets of Langerhans/drug effects/metabolism/pathology [MESH] |Membrane Glycoproteins/genetics/immunology/*metabolism [MESH] |Palmitic Acid/pharmacology [MESH]BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibri(epmc).pdf DeepDyve Pubget Overpricing