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Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family
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G. Dubin
Published/Copyright:
June 1, 2005
Abstract
Staphostatins, a novel family of cysteine protease inhibitors with a unique mechanism of action and distinct protein fold has recently been discovered. In this report we describe the properties of Staphylococcus epidermidis staphostatin A (EcpB), a new member of the family. As for other staphostatins, the recombinant S. epidermidis staphostatin A exerted very narrow inhibitory specificity, limited to cysteine protease from the same species. The closely related proteases from S. aureus cleaved the inhibitor at the reactive site peptide bond and inactivated it. The EcpB homologue, S. aureus staphostatin A (ScpB), was also susceptible to proteolytic cleavage at the same site by nontarget cysteine proteases. Conversely, S. aureus staphostatin B (SspC) was resistant to such proteolysis. The difference in the susceptibility of individual inhibitors to proteolytic cleavage at the reactive site suggests subtle variations in the mechanism of interaction with cysteine proteases.
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Published Online: 2005-06-01
Published in Print: 2004-06-07
Copyright © 2004 by Walter de Gruyter GmbH & Co. KG
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- Colon cancer: genomics and apoptotic events
- Interaction of calpastatin with calpain: a review
- Cathepsin L and Arg/Lys aminopeptidase: a distinct prohormone processing pathway for the biosynthesis of peptide neurotransmitters and hormones
- Searching for the most effective screening system to identify cell-active inhibitors of β-secretase
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- Human cathepsin F: expression in baculovirus system, characterization and inhibition by protein inhibitors
- Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages
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- Evidence for an interaction between leptin, T cell costimulatory antigens CD28, CTLA-4 and CD26 (dipeptidyl peptidase IV) in BCG-induced immune responses of leptin- and leptin receptor-deficient mice
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