SERPINB12 Is a Slow-Binding Inhibitor of Granzyme A and Hepsin

Jason Z. Niehaus, Mark T. Miedel, Misty Good, Allyson N. Wyatt, Stephen C. Pak, Gary A. Silverman, Cliff J. Luke

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish
Pages (from-to)6756-6759
Number of pages4
JournalBiochemistry
Volume54
Issue number45
DOIs
StatePublished - Oct 26 2015
Externally publishedYes

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