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10.1021/bi900608m http://scihub22266oqcxt.onion/10.1021/bi900608m C4394648!4394648!19810772     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochemistry 2009 ; 48 (44): 10568-76 Nephropedia Template TP {{tp|p=19810772|t=2009. Annexin A5 Directly Interacts with Amyloidogenic Proteins and Reduces Their Toxicity? |pdf=|usr=}}{{19810772}} gab.com Text Annexin A5 Directly Interacts with Amyloidogenic Proteins and Reduces Their Toxicity JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=19810772 #FOAvip Protein misfolding is a central mechanism for the development of neurodegenerative diseases and type 2 diabetes mellitus. The accumulation of misfolded ?-synuclein protein inclusions in the Lewy bodies of Parkinson?s disease is thought to play a key role in pathogenesis and disease progression. Similarly, the misfolding of the ?-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers plays a central role in the induction of ?-cell apoptosis in the context of type 2 diabetes. In this study, we show that annexin A5 plays a role in interacting with and reducing the toxicity of the amyloidogenic proteins, h-IAPP and ?-synuclein. We find that annexin A5 is coexpressed in human ?-cells and that exogenous annexin A5 reduces the level of h-IAPP-induced apoptosis in human islets by ~50% and in rodent ?-cells by ~90%. Experiments with transgenic expression of ?-synuclein in Caenorhabditis elegans show that annexin A5 reduces ?-synuclein inclusions in vivo. Using thioflavin T fluorescence, electron microscopy, and electron paramagnetic resonance, we provide evidence that substoichiometric amounts of annexin A5 inhibit h-IAPP and ?-synuclein misfolding and fibril formation. We conclude that annexin A5 might act as a molecular safeguard against the formation of toxic amyloid aggregates. Twit Text FOAVip Annexin A5 Directly Interacts with Amyloidogenic Proteins and Reduces Their Toxicity ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=19810772 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19810772 #FOAvip English Wikipedia <ref>{{Cite pmid|19810772}}</ref> Annexin A5 Directly Interacts with Amyloidogenic Proteins and Reduces Their Toxicity? #MMPMID19810772 Bedrood S; Jayasinghe S; Sieburth D; Chen M; Erbel S; Butler PC; Langen R; Ritzel RA Biochemistry 2009[Nov]; 48 (44): 10568-76 PMID19810772show ga Protein misfolding is a central mechanism for the development of neurodegenerative diseases and type 2 diabetes mellitus. The accumulation of misfolded ?-synuclein protein inclusions in the Lewy bodies of Parkinson?s disease is thought to play a key role in pathogenesis and disease progression. Similarly, the misfolding of the ?-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers plays a central role in the induction of ?-cell apoptosis in the context of type 2 diabetes. In this study, we show that annexin A5 plays a role in interacting with and reducing the toxicity of the amyloidogenic proteins, h-IAPP and ?-synuclein. We find that annexin A5 is coexpressed in human ?-cells and that exogenous annexin A5 reduces the level of h-IAPP-induced apoptosis in human islets by ~50% and in rodent ?-cells by ~90%. Experiments with transgenic expression of ?-synuclein in Caenorhabditis elegans show that annexin A5 reduces ?-synuclein inclusions in vivo. Using thioflavin T fluorescence, electron microscopy, and electron paramagnetic resonance, we provide evidence that substoichiometric amounts of annexin A5 inhibit h-IAPP and ?-synuclein misfolding and fibril formation. We conclude that annexin A5 might act as a molecular safeguard against the formation of toxic amyloid aggregates. äAnnexin A5 Directly Interacts with Amyloidogenic Proteins and Reduces (epmc).pdf DeepDyve Pubget Overpricing