Increased matriptase zymogen activation in inflammatory skin disorders
نویسندگان
چکیده
منابع مشابه
Zymogen activation, inhibition, and ectodomain shedding of matriptase.
Matriptase is a member of an expanding group of type II transmembrane serine proteases. Recently, much has been learned about the biochemistry, cellular biology, normal tissue physiology, and human pathology of this protease, and of its inhibitor, termed the hepatocyte growth factor inhibitor-1 (HAI-1). This review examines the recent literature that has characterized the regulation of matripta...
متن کاملTargeting zymogen activation to control the matriptase-prostasin proteolytic cascade.
Membrane-associated serine protease matriptase has been implicated in human diseases and might be a drug target. In the present study, a novel class of matriptase inhibitors targeting zymogen activation is developed by a combination of the screening of compound library using a cell-based matriptase activation assay and a computer-aided search of commercially available analogues of a selected co...
متن کاملA matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.
Matriptase and prostasin are part of a cell surface proteolytic pathway critical for epithelial development and homeostasis. Here we have used a reconstituted cell-based system and transgenic mice to investigate the mechanistic interrelationship between the two proteases. We show that matriptase and prostasin form a reciprocal zymogen activation complex with unique features. Prostasin serves as...
متن کاملMatriptase shedding is closely coupled with matriptase zymogen activation and requires de novo proteolytic cleavage likely involving its own activity
The type 2 transmembrane serine protease matriptase is involved in many pathophysiological processes probably via its enzymatic activity, which depends on the dynamic relationship between zymogen activation and protease inhibition. Matriptase shedding can prolong the life of enzymatically active matriptase and increase accessibility to substrates. We show here that matriptase shedding occurs vi...
متن کاملNatural Endogenous Human Matriptase and Prostasin Undergo Zymogen Activation via Independent Mechanisms in an Uncoupled Manner
The membrane-associated serine proteases matriptase and prostasin are believed to function in close partnership. Their zymogen activation has been reported to be tightly coupled, either as a matriptase-initiated proteolytic cascade or through a mutually dependent mechanism involving the formation of a reciprocal zymogen activation complex. Here we show that this putative relationship may not ap...
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ژورنال
عنوان ژورنال: American Journal of Physiology-Cell Physiology
سال: 2011
ISSN: 0363-6143,1522-1563
DOI: 10.1152/ajpcell.00403.2010