Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8)

Stable Identifier
R-HSA-2022411
Type
Reaction [transition]
Species
Homo sapiens
Compartment
extracellular region, plasma membrane
Synonyms
Cathepsin G Hydrolyzes Angiotensin I to Yield Angiotensin II
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Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8)
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Cathepsin G hydrolyzes angiotensin-(1-10) (angiotensin I) to yield angiotensin-(1-8) (angiotensin II) (Reilly et al. 1982, Owen and Campbell 1998, Raymond et al. 2010). Cathepsin bound to the plasma membrane of neutrophils has a higher activity than does soluble cathepsin G (Owen and Campbell 1998).

Literature References
PubMed ID Title Journal Year
9570564 Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition

Owen, CA, Campbell, EJ

J Immunol 1998
20889553 How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution

Raymond, WW, Trivedi, NN, Makarova, A, Ray, M, Craik, CS, Caughey, GH

J Immunol 2010
6807977 Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases

Reilly, CF, Tewksbury, DA, Schechter, NM, Travis, J

J Biol Chem 1982
Participants
Input
Output
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as an event of
Event Information
Go Biological Process
angiotensin maturation (0002003)
Catalyst Activity

serine-type endopeptidase activity of Cathepsin G [plasma membrane]

Physical Entity
Cathepsin G [plasma membrane] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Orthologous Events
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (Canis familiaris)
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (Danio rerio)
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (Mus musculus)
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (Sus scrofa)
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (Xenopus tropicalis)
Authored
May, B  (2011-11-19)
Reviewed
Joseph, J  (2012-08-06)
Created
May, B  (2011-11-29)
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