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Literature summary for 3.4.21.69 extracted from

  • Gleeson, E.M.; Dichiara, M.G.; Salicio, A.; Quinn, L.M.; Drakeford, C.; Russell, S.E.; Walsh, P.T.; Orbe, J.; Hermida, J.; Smith, O.P.; O'Donnell, J.S.; Montes, R.; Preston, R.J.
    Activated protein C beta-glycoform promotes enhanced noncanonical PAR1 proteolysis and superior resistance to ischemic injury (2015), Blood, 126, 915-919 .
    View publication on PubMed
Search for more literature for 3.4.21.69

Cloned(Commentary)

Cloned (Comment) Organism
recombinant coexpression of hEPCR and PAR1 linked to an N-terminal alkaline phosphatase (AP) cleavage reporter and treatment with recombinant APC-b (APCN329Q) or N-glycosidase PNGase F-treated APC (APCPNG), in which all N-linked glycans are excised, in HEK 293-T cells, detection of PAR1 proteolysis on HEK 293T cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information neuroprotective activity of a murine APC variant with limited anticoagulant activity (mAPCPS) is compared with an identical APC variant except for the absence of glycosylation at the APC-beta sequon (mAPCPS/N329Q). mAPCPS/N329Q limits cerebral ischemic injury and reduces brain lesion volume significantly more effectively than mAPCPS Mus musculus
N329Q the recombinant APC variant APCN329Q mimics the glycosylation pattern of the endogenous plasma APC-beta glycoform and exhibits significantly enhances PAR1-dependent cytoprotective activity on endothelial cells compared with wild-type APC, determination of the molecular basis for superior APC-beta cytoprotective signaling Mus musculus
N329Q the recombinant APC variant mimics the glycosylation pattern of the endogenous plasma APC-beta glycoform and exhibits 4fold enhanced PAR1-dependent cytoprotective activity on endothelial cells compared to wild-type APC, determination of the molecular basis for superior APC-beta cytoprotective signaling Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protease-activated receptor 1 + H2O Homo sapiens PAR1 ?
-
 ?
protease-activated receptor 1 + H2O Mus musculus PAR1 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P04070
-
-
Mus musculus P33587
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein naturally occurring APC-beta plasma glycoform Mus musculus
glycoprotein the enzyme is in naturally occurring APC-beta plasma glycoform, N-glycosidase PNGase F treatment of APC excises all N-linked glycans leading to a fourfold increased PAR1 proteolysis compared to untreated APC Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
macrophage
-
 Homo sapiens
-
macrophage
-
 Mus musculus
-
RAW-264.7 cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protease-activated receptor 1 + H2O PAR1 Homo sapiens ?
-
 ?
protease-activated receptor 1 + H2O PAR1 Mus musculus ?
-
 ?
protease-activated receptor 1 + H2O PAR1, generation of unique tethered ligands by APC by cleavage at Arg46 on PAR1 Mus musculus ?
-
 ?

Synonyms

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

General Information

General Information Comment Organism
malfunction a recombinant APC variant (APCN329Q) mimicking the naturally occurring APC-beta plasma glycoform exhibits superior PAR1 proteolysis at a cleavage site that selectively mediates cytoprotective signaling.Mutant APCN329Q also enhances integrin aMb2-dependent PAR1 proteolysis to exert significantly improved anti-inflammatory activity on macrophages compared with wild-type APC Mus musculus
malfunction a recombinant APC variant (APCN329Q) mimicking the naturally occurring APC-beta plasma glycoform exhibits superior PAR1 proteolysis at a cleavage site that selectively mediates cytoprotective signaling.Mutant APCN329Q also enhances integrin aMb2-dependent PAR1 proteolysis to exert significantly improved anti-inflammatory activity on macrophages compared with wild-type APC. Enhanced cytoprotective PAR1 signaling by APC-beta is a consequence of accelerated EPCR-dependent PAR1 proteolysis Homo sapiens
physiological function activated protein C (APC) is an anticoagulant protease that initiates cell signaling via protease-activated receptor 1 (PAR1) to regulate vascular integrity and inflammatory response. Importance of APC glycosylation in controlling the efficacy of PAR1 proteolysis by APC Homo sapiens
physiological function activated protein C (APC) is an anticoagulant protease that initiates cell signaling via protease-activated receptor 1 (PAR1) to regulate vascular integrity and inflammatory response. Importance of APC glycosylation in controlling the efficacy of PAR1 proteolysis by APC. Analysis of APC inhibition of cytokine secretion from RAW-264.7 cells. APC-beta exhibits superior inhibition of cerebral injury in murine ischemic stroke Mus musculus