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10.4049/jimmunol.1502122 http://scihub22266oqcxt.onion/10.4049/jimmunol.1502122 C5222549!5222549!27036911     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27036911&cmd=llinks): Failed to open stream: HTTP request failed! 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The C-terminal acidic region of calreticulin mediates phosphatidylserine binding and apoptotic cell phagocytosis |pdf=|usr=}}{{27036911}} gab.com Text The C-terminal acidic region of calreticulin mediates phosphatidylserine binding and apoptotic cell phagocytosis JO: J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=27036911 #FOAvip Calreticulin is a calcium-binding chaperone that is normally localized in the endoplasmic reticulum (ER). Calreticulin is detectable on the surface of apoptotic cell under some apoptosis-inducing conditions, where it promotes phagocytosis and immunogenicity of dying cells. However, the precise mechanism by which calreticulin, a soluble protein, localizes to the outer surface of the plasma membrane of dying cells is unknown, as are the molecular mechanisms that are relevant to calreticulin-induced cellular phagocytosis. Calreticulin comprises three distinct structural domains; a globular domain, an extended arm-like P-domain and a C-terminal acidic region containing multiple low affinity calcium binding sites. We show here that calreticulin, via its C-terminal acidic region, preferentially interacts with phosphatidylserine (PS) compared to other phospholipids, and that this interaction is calcium-dependent. Additionally, exogenous calreticulin binds apoptotic cells via a higher affinity calcium-dependent mode that is acidic-region-dependent. Exogenous calreticulin also binds live cells, including macrophages, via a second, lower affinity P-and globular domain-dependent, but calcium-independent binding mode that likely involves its generic polypeptide-binding site. Truncation constructs lacking the acidic region or arm-like P-domain of calreticulin are impaired in their abilities to induce apoptotic cell phagocytosis by murine peritoneal macrophages. Taken together, the results of this investigation provide the first molecular insights into the phospholipid-binding site of calreticulin as a key anchor point for the cell surface expression of calreticulin on apoptotic cells. These findings also support a role for calreticulin as a PS-bridging molecule that co-operates with other PS-binding factors to promote the phagocytosis of apoptotic cells. Twit Text FOAVip The C-terminal acidic region of calreticulin mediates phosphatidylserine binding and apoptotic cell phagocytosis ????J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=27036911 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27036911 #FOAvip English Wikipedia <ref>{{Cite pmid|27036911}}</ref> The C-terminal acidic region of calreticulin mediates phosphatidylserine binding and apoptotic cell phagocytosis #MMPMID27036911 Wijeyesakere SJ; Bedi SK; Huynh D; Raghavan M J Immunol 2016[May]; 196 (9): 3896-909 PMID27036911show ga Calreticulin is a calcium-binding chaperone that is normally localized in the endoplasmic reticulum (ER). Calreticulin is detectable on the surface of apoptotic cell under some apoptosis-inducing conditions, where it promotes phagocytosis and immunogenicity of dying cells. However, the precise mechanism by which calreticulin, a soluble protein, localizes to the outer surface of the plasma membrane of dying cells is unknown, as are the molecular mechanisms that are relevant to calreticulin-induced cellular phagocytosis. Calreticulin comprises three distinct structural domains; a globular domain, an extended arm-like P-domain and a C-terminal acidic region containing multiple low affinity calcium binding sites. We show here that calreticulin, via its C-terminal acidic region, preferentially interacts with phosphatidylserine (PS) compared to other phospholipids, and that this interaction is calcium-dependent. Additionally, exogenous calreticulin binds apoptotic cells via a higher affinity calcium-dependent mode that is acidic-region-dependent. Exogenous calreticulin also binds live cells, including macrophages, via a second, lower affinity P-and globular domain-dependent, but calcium-independent binding mode that likely involves its generic polypeptide-binding site. Truncation constructs lacking the acidic region or arm-like P-domain of calreticulin are impaired in their abilities to induce apoptotic cell phagocytosis by murine peritoneal macrophages. Taken together, the results of this investigation provide the first molecular insights into the phospholipid-binding site of calreticulin as a key anchor point for the cell surface expression of calreticulin on apoptotic cells. These findings also support a role for calreticulin as a PS-bridging molecule that co-operates with other PS-binding factors to promote the phagocytosis of apoptotic cells. �The C-terminal acidic region of calreticulin mediates phosphatidylseri(epmc).pdf DeepDyve Pubget Overpricing