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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2011-3-1
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pubmed:abstractText |
The endoplasmic reticulum (ER) is responsible for the synthesis and folding of secretory, transmembrane and ER-resident proteins. Conditions that impair protein folding or overwhelm its protein folding capacity disrupt ER homeostasis, thereby causing ER stress. ER stress-induced apoptosis and inflammation are involved in the pathogenesis of inflammatory diseases. Activated protein C (APC) inhibits inflammation and apoptosis in monocytes, and this may partly explain the protective effects of APC treatment in severe sepsis. However, the precise molecular pathways by which APC modulates these effects remain unknown.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Inflammatory Agents,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein C,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin,
http://linkedlifedata.com/resource/pubmed/chemical/Thromboplastin,
http://linkedlifedata.com/resource/pubmed/chemical/drotrecogin alfa activated,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1538-7836
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pubmed:author |
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pubmed:copyrightInfo |
© 2011 International Society on Thrombosis and Haemostasis.
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pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
582-92
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pubmed:meshHeading |
pubmed-meshheading:21166994-Anti-Inflammatory Agents,
pubmed-meshheading:21166994-Apoptosis,
pubmed-meshheading:21166994-Base Sequence,
pubmed-meshheading:21166994-Calcium,
pubmed-meshheading:21166994-Calcium Signaling,
pubmed-meshheading:21166994-Caspase 3,
pubmed-meshheading:21166994-Endoplasmic Reticulum,
pubmed-meshheading:21166994-Gene Expression,
pubmed-meshheading:21166994-Heat-Shock Proteins,
pubmed-meshheading:21166994-Humans,
pubmed-meshheading:21166994-Monocytes,
pubmed-meshheading:21166994-NF-kappa B,
pubmed-meshheading:21166994-Protein C,
pubmed-meshheading:21166994-RNA, Messenger,
pubmed-meshheading:21166994-Reactive Oxygen Species,
pubmed-meshheading:21166994-Recombinant Proteins,
pubmed-meshheading:21166994-Sepsis,
pubmed-meshheading:21166994-Stress, Physiological,
pubmed-meshheading:21166994-Thapsigargin,
pubmed-meshheading:21166994-Thromboplastin
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pubmed:year |
2011
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pubmed:articleTitle |
Activated protein C modulates inflammation, apoptosis and tissue factor procoagulant activity by regulating endoplasmic reticulum calcium depletion in blood monocytes.
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pubmed:affiliation |
Department of Medical Sciences, McMaster University, Hamilton, ON, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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