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Literature summary for 3.4.21.69 extracted from

  • Gramling, M.; Beaulieu, L.; Church, F.
    Activated protein C enhances cell motility of endothelial cells and MDA-MB-231 breast cancer cells by intracellular signal transduction (2010), Exp. Cell Res., 316, 314-328.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.69

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Factor Va + H2O Homo sapiens inactivation ?
-
 ?
Factor VIIIa + H2O Homo sapiens inactivation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification thrombin bound to the endothelial cell surface by thrombomodulin cleaves protein C into its active form Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
endothelial cell human umbilical vein endothelial cells, HUVEC Homo sapiens
-
liver the zymogen protein C is localized to the endothelium by binding to endothelial cell protein C receptor Homo sapiens
-
MDA-MB-231 cell breast cancer cells Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Factor Va + H2O
-
 Homo sapiens ?
-
 ?
Factor Va + H2O inactivation Homo sapiens ?
-
 ?
Factor VIIIa + H2O
-
 Homo sapiens ?
-
 ?
Factor VIIIa + H2O inactivation Homo sapiens ?
-
 ?

Synonyms

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

General Information

General Information Comment Organism
malfunction severe thrombophilia occurs with deficiencies in phosphatidylcholine or phosphatidylserine and with a mutation in factor Va that prevents its inactivation by APC, known as Factor V Leiden Homo sapiens
physiological function activated protein C is an anticoagulant serine protease with non-hemostatic functions related to inflammation, cell survival, and cell migration. Activated protein C enhances cell motility of endothelial cells and MDA-MB-231 breast cancer cells by intracellular signal transduction, mechanism by which APC promotes angiogenesis and breast cancer invasion, overview. APC activation of matrix metalloproteases 2 and/or 9 is necessary but not sufficient to increase invasion, and APC does not utilize the endogenous plasminogen activation system to increase invasion. APC activates the ERK, Akt, and NFkappaB, but not the JNK pathway to promote MDA-MB-231 cell motility. APC proteolytically inactivates factors Va and VIIIa in the presence of protein S. APC forms a stable complex with PAI-1, thereby removing a potent inhibitor of urokinase plasminogen activator, EC 3.4.21.73, from the system. APC promotes MDA-MB-231 breast cancer cell invasion through EPCR and PAR-1, and MDA-MB-231 cell chemotaxis through MAPK and PI3K/Akt activation Homo sapiens