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10.1152/ajpendo.00262.2010 http://scihub22266oqcxt.onion/10.1152/ajpendo.00262.2010 C4459921!4459921 !20858756     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=20858756 &cmd=llinks): Failed to open stream: HTTP request failed! 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In pancreatic ?-cells, ?-synuclein might therefore play a similar role by interacting with organelles involved in insulin secretion. We tested for ?-synuclein localizing to insulin-secretory granules and characterized its role in glucose-stimulated insulin secretion. Immunohistochemistry and fluorescent sulfonylureas were used to test for ?-synuclein localization to insulin granules in ?-cells, immunoprecipitation with Western blot analysis for interaction between ?-synuclein and K(ATP) channels, and ELISA assays for the effect of altering ?-synuclein expression up or down on insulin secretion in INS1 cells or mouse islets, respectively. Differences in cellular phenotype between ?-synuclein knockout and wild-type ?-cells were found by using confocal microscopy to image the fluorescent insulin biosensor Ins-C-emGFP and by using transmission electron microscopy. The results show that anti-?-synuclein antibodies labeled secretory organelles within ?-cells. Anti-?-synuclein antibodies colocalized with K(ATP) channel, anti-insulin, and anti-C-peptide antibodies. ?-Synuclein coimmunoprecipitated in complexes with K(ATP) channels. Expression of ?-synuclein downregulated insulin secretion at 2.8 mM glucose with little effect following 16.7 mM glucose stimulation. ?-Synuclein knockout islets upregulated insulin secretion at 2.8 and 8.4 mM but not 16.7 mM glucose, consistent with the depleted insulin granule density at the ?-cell surface membranes observed in these islets. These findings demonstrate that ?-synuclein interacts with K(ATP) channels and insulin-secretory granules and functionally acts as a brake on secretion that glucose stimulation can override. ?-Synuclein might play similar roles in diabetes as it does in other degenerative diseases, including Alzheimer's and Parkinson's diseases. Twit Text FOAVip -Synuclein binds the K(ATP) channel at insulin-secretory granules and inhibits insulin secretion ????Am J Physiol Endocrinol Metab http://www.kidney.de/pget.php?&tw=1&pmid=20858756 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=20858756 #FOAvip English Wikipedia <ref>{{Cite pmid|20858756 }}</ref> ?-Synuclein binds the K(ATP) channel at insulin-secretory granules and inhibits insulin secretion #MMPMID20858756 Geng X ; Lou H ; Wang J ; Li L ; Swanson AL ; Sun M ; Beers-Stolz D ; Watkins S ; Perez RG ; Drain P Am J Physiol Endocrinol Metab 2011[Feb]; 300 (2 ): E276-86 PMID20858756 show ga ?-Synuclein has been studied in numerous cell types often associated with secretory processes. In pancreatic ?-cells, ?-synuclein might therefore play a similar role by interacting with organelles involved in insulin secretion. We tested for ?-synuclein localizing to insulin-secretory granules and characterized its role in glucose-stimulated insulin secretion. Immunohistochemistry and fluorescent sulfonylureas were used to test for ?-synuclein localization to insulin granules in ?-cells, immunoprecipitation with Western blot analysis for interaction between ?-synuclein and K(ATP) channels, and ELISA assays for the effect of altering ?-synuclein expression up or down on insulin secretion in INS1 cells or mouse islets, respectively. Differences in cellular phenotype between ?-synuclein knockout and wild-type ?-cells were found by using confocal microscopy to image the fluorescent insulin biosensor Ins-C-emGFP and by using transmission electron microscopy. The results show that anti-?-synuclein antibodies labeled secretory organelles within ?-cells. Anti-?-synuclein antibodies colocalized with K(ATP) channel, anti-insulin, and anti-C-peptide antibodies. ?-Synuclein coimmunoprecipitated in complexes with K(ATP) channels. Expression of ?-synuclein downregulated insulin secretion at 2.8 mM glucose with little effect following 16.7 mM glucose stimulation. ?-Synuclein knockout islets upregulated insulin secretion at 2.8 and 8.4 mM but not 16.7 mM glucose, consistent with the depleted insulin granule density at the ?-cell surface membranes observed in these islets. These findings demonstrate that ?-synuclein interacts with K(ATP) channels and insulin-secretory granules and functionally acts as a brake on secretion that glucose stimulation can override. ?-Synuclein might play similar roles in diabetes as it does in other degenerative diseases, including Alzheimer's and Parkinson's diseases. |Animals [MESH] |Cytoplasm/metabolism [MESH] |DNA/biosynthesis/genetics [MESH] |Down-Regulation/physiology [MESH] |Immunohistochemistry [MESH] |Immunoprecipitation [MESH] |Insulin Secretion [MESH] |Insulin-Secreting Cells/drug effects/*metabolism [MESH] |Insulin/*metabolism [MESH] |Islets of Langerhans/cytology [MESH] |KATP Channels/drug effects/*metabolism [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |Mice, Knockout [MESH] |Microscopy, Confocal [MESH] |Microscopy, Electron, Transmission [MESH] |Microscopy, Fluorescence [MESH] |Reverse Transcriptase Polymerase Chain Reaction [MESH] |Secretory Vesicles/drug effects/*metabolism [MESH]?-Synuclein binds the K(ATP) channel at insulin-secretory granules and(epmc).pdf DeepDyve Pubget Overpricing