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Literature summary for 3.4.21.37 extracted from

  • Ewen, D.; Clarke, S.L.; Smith, J.R.; Berger, C.; Salmon, G.; Trevethick, M.; Shute, J.K.
    The role of protease-activated receptors PAR-1 and PAR-2 in the repair of 16HBE 14o(-) epithelial cell monolayers in vitro (2010), Clin. Exp. Allergy, 40, 435-449.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens neutrophil elastase does not cleave the N-terminal domains and does not disarm either PAR-1 or PAR-2 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelial cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information neutrophil elastase does not cleave the N-terminal domains and does not disarm either PAR-1 or PAR-2 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
neutrophil elastase
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction neutrophil elastase reduces the levels of coagulation factors and inhibits repair of following mechanical wounding of epithelial 16HBE 14o- cell layers. PAR-1 and PAR-2 peptide agonists stimulated the rate of repair and enhanced the formation of a fibrin provisional matrix to support the repair process, overview. But neutrophil elastase does not cleave the N-terminal domains and does not disarm either PAR-1 or PAR-2 Homo sapiens