| Literature DB >> 26497600 |
Jason Z Niehaus1, Mark T Miedel1, Misty Good1, Allyson N Wyatt1, Stephen C Pak1, Gary A Silverman1, Cliff J Luke1.
Abstract
The clade B/intracellular serpins protect cells from peptidase-mediated injury by forming covalent complexes with their targets. SERPINB12 is expressed in most tissues, especially at cellular interfaces with the external environment. This wide tissue distribution pattern is similar to that of granzyme A (GZMA). Because SERPINB12 inhibits trypsin-like serine peptidases, we determined whether it might also neutralize GZMA. SERPINB12 formed a covalent complex with GZMA and inhibited the enzyme with typical serpin slow-binding kinetics. SERPINB12 also inhibited Hepsin. SERPINB12 may function as an endogenous inhibitor of these peptidases.Entities:
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Year: 2015 PMID: 26497600 PMCID: PMC4900762 DOI: 10.1021/acs.biochem.5b01042
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162