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10.1038/cddis.2015.186 http://scihub22266oqcxt.onion/10.1038/cddis.2015.186 C4650733!4650733 !26158519     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26158519 &cmd=llinks): Failed to open stream: HTTP request failed! 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Single-cell imaging of inflammatory caspase dimerization reveals differential recruitment to inflammasomes |pdf=|usr=}}{{26158519 }} gab.com Text Single-cell imaging of inflammatory caspase dimerization reveals differential recruitment to inflammasomes JO: Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=26158519 #FOAvip The human inflammatory caspases, including caspase-1, -4, -5 and -12, are considered as key regulators of innate immunity protecting from sepsis and numerous inflammatory diseases. Caspase-1 is activated by proximity-induced dimerization following recruitment to inflammasomes but the roles of the remaining inflammatory caspases in inflammasome assembly are unclear. Here, we use caspase bimolecular fluorescence complementation to visualize the assembly of inflammasomes and dimerization of inflammatory caspases in single cells. We observed caspase-1 dimerization induced by the coexpression of a range of inflammasome proteins and by lipospolysaccharide (LPS) treatment in primary macrophages. Caspase-4 and -5 were only dimerized by select inflammasome proteins, whereas caspase-12 dimerization was not detected by any investigated treatment. Strikingly, we determined that certain inflammasome proteins could induce heterodimerization of caspase-1 with caspase-4 or -5. Caspase-5 homodimerization and caspase-1/-5 heterodimerization was also detected in LPS-primed primary macrophages in response to cholera toxin subunit B. The subcellular localization and organization of the inflammasome complexes varied markedly depending on the upstream trigger and on which caspase or combination of caspases were recruited. Three-dimensional imaging of the ASC (apoptosis-associated speck-like protein containing a caspase recruitment domain)/caspase-1 complexes revealed a large spherical complex of ASC with caspase-1 dimerized on the outer surface. In contrast, NALP1 (NACHT leucine-rich repeat protein 1)/caspase-1 complexes formed large filamentous structures. These results argue that caspase-1, -4 or -5 can be recruited to inflammasomes under specific circumstances, often leading to distinctly organized and localized complexes that may impact the functions of these proteases. Twit Text FOAVip Single-cell imaging of inflammatory caspase dimerization reveals differential recruitment to inflammasomes ????Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=26158519 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26158519 #FOAvip English Wikipedia <ref>{{Cite pmid|26158519 }}</ref> Single-cell imaging of inflammatory caspase dimerization reveals differential recruitment to inflammasomes #MMPMID26158519 Sanders MG ; Parsons MJ ; Howard AG ; Liu J ; Fassio SR ; Martinez JA ; Bouchier-Hayes L Cell Death Dis 2015[Jul]; 6 (7 ): e1813 PMID26158519 show ga The human inflammatory caspases, including caspase-1, -4, -5 and -12, are considered as key regulators of innate immunity protecting from sepsis and numerous inflammatory diseases. Caspase-1 is activated by proximity-induced dimerization following recruitment to inflammasomes but the roles of the remaining inflammatory caspases in inflammasome assembly are unclear. Here, we use caspase bimolecular fluorescence complementation to visualize the assembly of inflammasomes and dimerization of inflammatory caspases in single cells. We observed caspase-1 dimerization induced by the coexpression of a range of inflammasome proteins and by lipospolysaccharide (LPS) treatment in primary macrophages. Caspase-4 and -5 were only dimerized by select inflammasome proteins, whereas caspase-12 dimerization was not detected by any investigated treatment. Strikingly, we determined that certain inflammasome proteins could induce heterodimerization of caspase-1 with caspase-4 or -5. Caspase-5 homodimerization and caspase-1/-5 heterodimerization was also detected in LPS-primed primary macrophages in response to cholera toxin subunit B. The subcellular localization and organization of the inflammasome complexes varied markedly depending on the upstream trigger and on which caspase or combination of caspases were recruited. Three-dimensional imaging of the ASC (apoptosis-associated speck-like protein containing a caspase recruitment domain)/caspase-1 complexes revealed a large spherical complex of ASC with caspase-1 dimerized on the outer surface. In contrast, NALP1 (NACHT leucine-rich repeat protein 1)/caspase-1 complexes formed large filamentous structures. These results argue that caspase-1, -4 or -5 can be recruited to inflammasomes under specific circumstances, often leading to distinctly organized and localized complexes that may impact the functions of these proteases. |Adaptor Proteins, Signal Transducing/metabolism [MESH] |Apoptosis Regulatory Proteins/metabolism [MESH] |Apoptosis/immunology [MESH] |CARD Signaling Adaptor Proteins [MESH] |Caspase 1/chemistry/isolation & purification/*metabolism [MESH] |Caspase 12/chemistry/isolation & purification/metabolism [MESH] |Caspases, Initiator [MESH] |Caspases/chemistry/isolation & purification/*metabolism [MESH] |Cholera Toxin/pharmacology [MESH] |Cytoskeletal Proteins/metabolism [MESH] |Humans [MESH] |Immunity, Innate/genetics [MESH] |Inflammasomes/chemistry/metabolism [MESH] |Inflammation/*enzymology/pathology [MESH] |Macrophages/enzymology [MESH] |Molecular Imaging/methods [MESH] |NLR Proteins [MESH] |Protein Multimerization [MESH]Single-cell imaging of inflammatory caspase dimerization reveals diffe(epmc).pdf DeepDyve Pubget Overpricing