Quantitative Characterization of Furin Specificity
نویسندگان
چکیده
منابع مشابه
Specificity determinants of the α1PDX-furin reaction
Background: α1PDX and serpin B8 are proprotein convertase (PC) inhibitors whose specificity and selectivity for PCs are not understood. Results: α1PDX-serpin B8 and furin-PC chimeras revealed new serpin and protease (re)active-site and exosite determinants of reactivity. Conclusion: α1PDX reactive-site and exosite determinants may be exploited for engineering specificity and selectivity for inh...
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The PC (proprotein convertase) furin cleaves a large variety of proproteins and hence plays a major role in many pathologies. Therefore furin inhibition might be a good strategy for therapeutic intervention, and several furin inhibitors have been generated, although none are entirely furin-specific. To reduce potential side effects caused by cross-reactivity with other proteases, dromedary heav...
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In eukaryotes, many secreted proteins and peptide hormones are excised from larger precursors by calcium-dependent serine proteinases, the proprotein/prohormone convertases (PCs). These PCs cleave their protein substrates very specifically following multiple basic residues. The seven mammalian PCs and their yeast orthologue kexin are multi-domain proteinases consisting of a subtilisin-related c...
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Furin, a KEX2 protease homolog with high RNA expression in the liver is an excellent candidate as a hepatic proprotein convertase. Here we show that purified recombinant furin has the same proalbumin specificity and serpin inhibitory properties as the in situ hepatic convertase. There was rapid cleavage at the -RRD- site of normal human proalbumin but there no significant cleavage of natural un...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.33.23229