Title : Cleavage and inactivation of alpha 1-antitrypsin by metalloproteinases released from neutrophils.

Pub. Date : 1988 Aug

PMID : 2841359






2 Functional Relationships(s)
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1 Both preparations cleaved and inactivated alpha 1-antitrypsin, with cleavage occurring close to the reactive center, at the Phe-Leu bond between positions P7 and P6. Leucine serpin family A member 1 Homo sapiens
2 However, the unusual cleavage site, and the ability of fMet-Leu-Phe-stimulated neutrophils to cleave alpha 1-antitrypsin without releasing collagenase, suggests that collagenase is not responsible for cleavage by the cells, which, by implication, is due to an as yet uncharacterized metalloenzyme. Leucine serpin family A member 1 Homo sapiens