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Article

Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.

The Biochemical journal - 15 Aug 2010

Stirnberg Marit, Maurer Eva, Horstmeyer Angelika, Kolp Sonja, Frank Stefan, Bald Tobias, Arenz Katharina, Janzer Andreas, Prager Kai, Wunderlich Patrick, Walter Jochen, Gütschow Michael

Abstract excerpt

Matriptase-2 is a member of the TTSPs (type II transmembrane serine proteases), an emerging class of cell surface proteases involved in tissue homoeostasis and several human disorders. Matriptase-2 exhibits a domain organization similar to other TTSPs, with a cytoplasmic N-terminus, a transmembrane domain and an extracellular C-terminus containing the non-catalytic stem region and the protease domain. To gain...

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Identifiers

PMID: 20518742
DOI: 10.1042/BJ20091565

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Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.PMID 20518742Read ↗

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