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...
Topics
- Catalysis
- Catalytic Domain
- Cell Line
- Cell Membrane
- Culture Media, Conditioned
- Enzyme Activation
- Enzyme Precursors
- Extracellular Space
- Humans
- Membrane Proteins
- Mutation
- Protein Binding