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10.1073/pnas.1707364114

http://scihub22266oqcxt.onion/10.1073/pnas.1707364114
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suck abstract from ncbi


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pmid28973891      Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (41): 10948-53
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  • Complement-activation fragment C4a mediates effector functions by binding as untethered agonist to protease-activated receptors 1 and 4 #MMPMID28973891
  • Wang H; Ricklin D; Lambris JD
  • Proc Natl Acad Sci U S A 2017[Oct]; 114 (41): 10948-53 PMID28973891show ga
  • How C4a transduces signaling and generates various biological functions has long been unresolved. Using a cell-based reporter assay, we screened C4a against a panel of 168 known and 73 orphan G protein-coupled receptors and now provide evidence that C4a is a ligand for protease-activated receptor (PAR)1 and PAR4. In human endothelial cells, our assessment of ERK activation and calcium mobilization in the presence of various antagonists and inhibitors suggests that C4a-mediated cell activation is mediated through PAR1 and PAR4. Our results demonstrate that C4a is a nontraditional agonist for PAR1 and PAR4 whose direct functional effects indicate a potentially significant direct linkage between the complement, coagulation, and endothelial barrier systems.
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