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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4900762 | PMC |
| http://dx.doi.org/10.1021/acs.biochem.5b01042 | DOI Listing |
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SERPINB12 Is a Slow-Binding Inhibitor of Granzyme A and Hepsin.
Biochemistry
November 2015
Department of Pediatrics and ‡Cell Biology and Physiology, University of Pittsburgh School of Medicine and The Children's Hospital of Pittsburgh of UPMC, 4401 Penn Avenue, Pittsburgh, Pennsylvania 15224, United States.
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).
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