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Literature summary for 3.4.21.69 extracted from

  • Schuepbach, R.A.; Velez, K.; Riewald, M.
    Activated protein C up-regulates procoagulant tissue factor activity on endothelial cells by shedding the TFPI Kunitz 1 domain (2011), Blood, 117, 6338-6346.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
DAN-Glu-Gly-Arg-CMK dansyl-glutamyl-glycyl-arginyl-chloromethylketone, blocks the enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Homo sapiens 9986
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Homo sapiens
-
endothelial cell
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Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information APC activity is measured using the commercial chromogenic substrate Spectrozyme PCa Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Activated protein C
-
Homo sapiens
APC
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Homo sapiens

General Information

General Information Comment Organism
metabolism the procoagulant role of the protein C pathway may have important implications for the regulation of TF- and TFPI-dependent biologic responses and for fine tuning of the hemostatic balance in the vascular system Homo sapiens
additional information a TFPI Lys86Ala mutation between the Kunitz 1 and 2 domains eliminates both cleavage and the enhanced TF activity in response to APC in overexpression studies Homo sapiens
physiological function activated protein C upregulates TF activity by endothelial cell protein C receptordependent shedding of the Kunitz 1 domain from membrane-associated TFPI. Exogenous or endogenously generated APC leads to increased TF-dependent factor Xa activity. Induction requires APC's proteolytic activity and binding to endothelial cell protein C receptor but not protease activated receptors, mechanism, overview. APC does not affect total TF antigen expression or the availability of anionic phospholipids on the apical cell membrane Homo sapiens