ArticleThe Biochemical journal2005
Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Matriptase-dependent epidermal pre-neoplasm in zebrafish embryos caused by a combination of hypotonic stress and epithelial polarity defects.PLoS genetics · 2023Article
- Article
- Recombinant hepatocyte growth factor activator inhibitor 1: expression in Drosophila S2 cells, purification and crystallization.Acta crystallographica. Section F, Structural biology communications · 2017Article
- The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.The Journal of biological chemistry · 2014Article
- A recombinant matriptase causes an increase in caspase-3 activity in a small-intestinal epithelial IEC-6 line cultured on fibronectin-coated plates.Cytotechnology · 2014Article
- Crystal structures of matriptase in complex with its inhibitor hepatocyte growth factor activator inhibitor-1.The Journal of biological chemistry · 2013Article
- Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway.The Journal of biological chemistry · 2013Article
- Hepatocyte growth factor activator inhibitor-2 prevents shedding of matriptase.Experimental cell research · 2013Article
- Roles of CUB and LDL receptor class A domain repeats of a transmembrane serine protease matriptase in its zymogen activation.Journal of biochemistry · 2013Article
- Matriptase protects against experimental colitis and promotes intestinal barrier recovery.Inflammatory bowel diseases · 2012Article
- Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.The Journal of biological chemistry · 2011Article
- Membrane-anchored serine proteases in vertebrate cell and developmental biology.Annual review of cell and developmental biology · 2011Review
- Identification of the matriptase second CUB domain as the secondary site for interaction with hepatocyte growth factor activator inhibitor type-1.The Journal of biological chemistry · 2010Article
- The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.The Biochemical journal · 2010Review
- Article
- Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells.Cytotechnology · 2009Article
- Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.The Biochemical journal · 2008Article
- Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MT-SP1 (membrane-type serine protease 1)/matriptase is an epithelial-derived integral membrane enzyme. The purpose of the present study was to examine whether the enzyme exists on the basolateral side of simple columnar epithelial cells, such as enterocytes, of normal adult animals. Using COS-1 monkey kidney cells transiently transfected with rat MT-SP1/matriptase expression plasmids, we found that the enzyme is post-translationally processed by the cleavage between Gly149 and Ser150, that a portion of the C-terminal part (Ser150-Val855) remains in the cells by association with the NTF (N-terminal fragment) (Met1-Gly149), while the other portions are released into the medium and that the release is increased on activation by co-expression with hepatocyte growth factor activator inhibitor type-1. Western-blot analysis of crude membranes prepared from rat jejunum demonstrated the presence of the NTF but negligible or no occurrence of the C-terminal part of the protein. Fractionation of the crude membranes by ultracentrifugation with Percoll followed by Western-blot analysis showed that the fractionation profile of the NTF correlated significantly with that of E-cadherin, an adhesion molecule on the lateral membrane. Immunostaining of the jejunum demonstrated the occurrence of the NTF on the lateral membranes but not on the apical membranes. These results suggest that considerable MT-SP1/matriptase molecules occur on the basolateral sides of normal epithelial cells and support our hypothesis that a possible physiological function of this enzyme is the control of epithelial-cell turnover by regulating cell-cell and/or cell-substratum adhesions.
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Registered trials
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