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Literature summary for 3.4.21.5 extracted from

  • Delekta, P.C.; Apel, I.J.; Gu, S.; Siu, K.; Hattori, Y.; McAllister-Lucas, L.M.; Lucas, P.C.
    Thrombin-dependent NF-kappaB activation and monocyte/endothelial adhesion are mediated by the CARMA3/Bcl10/MALT1 signalosome (2010), J. Biol. Chem., 285, 41432-41442.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
endothelial cell
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 Mus musculus
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SVEC4-10 cell
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 Mus musculus
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General Information

General Information Comment Organism
metabolism PAR-1 signaling to NF-kappaB in endothelial cells via protein kinase C signaling, CARMA3/Bcl10/MALT1, CBM, signalosome, and IkappaB kinase, and involving thrombin, pathway regulation, overview. The CBM signalosome controls thrombin-dependent monocyte/endothelial adhesion. The process is different in lymphocytes where CARMA1 is active instead of CARMA3 Mus musculus
physiological function pro-atherogenic effects of thrombin, thrombin is a potent modulator of endothelial function and, through stimulation of NF-kappaB, induces endothelial expression of intracellular adhesion molecule-1, ICAM-1, and vascular cell adhesion molecule-1, VCAM-1. These cell surface adhesion molecules recruit inflammatory cells to the vessel wall and thereby participate in the development of atherosclerosis, which is increasingly recognized as an inflammatory condition. The principal receptor for thrombin on endothelial cells is protease-activated receptor-1, PAR-1, a member of the G protein-coupled receptor superfamily. Thrombin induces phosphorylation of Akt and NF-kappaB-responsive gene transcription Mus musculus