ArticleThe Biochemical journal2008
Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.
Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Membrane-Anchored Serine Protease Inhibitors: Physiological Functions, Mechanisms, and Roles in Cancer.International journal of molecular sciences · 2026Review
- A biochemical difference between HAI-2 variants causing syndromic and non-syndromic Congenital Sodium Diarrhea.PloS one · 2026Article
- Efficient production of fully active, SARS-CoV-2-priming, wildtype TMPRSS2 ectodomain via co-expression of HAI-2 allows for both auto- and cross-activation mechanisms.The Biochemical journal · 2025Article
- Article
- Hemagglutinin Cleavability, Acid Stability, and Temperature Dependence Optimize Influenza B Virus for Replication in Human Airways.Journal of virology · 2019Article
- Expression of serine peptidase inhibitor Kunitz type 1 in differentiated thyroid cancer.Histochemistry and cell biology · 2018Article
- Article
- 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
- Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses.Journal of virology · 2013Article
- Article
- Matriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cells.American journal of physiology. Cell physiology · 2011Article
- Membrane-bound serine protease inhibitor HAI-1 is required for maintenance of intestinal epithelial integrity.The American journal of pathology · 2011Article
- Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.The Journal of biological chemistry · 2011Article
- Tumor detection by imaging proteolytic activity.Cancer research · 2010Article
- Local protease signaling contributes to neural tube closure in the mouse embryo.Developmental cell · 2010Article
- Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.American journal of physiology. Cell physiology · 2009Article
- Expression of prostasin and its inhibitors during colorectal cancer carcinogenesis.BMC cancer · 2009Article
- 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
- Tissue injury alters the site of expression of hepatocyte growth factor activator inhibitor type 1 in bronchial epithelial cells.Human cell · 2009Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
HAI-1 [HGF (hepatocyte growth factor) activator inhibitor-1] is a Kunitz-type transmembrane serine protease inhibitor that forms inhibitor complexes with the trypsin-like serine protease, matriptase. HAI-1 is essential for mouse placental development and embryo survival and together with matriptase it is a key regulator of carcinogenesis. HAI-1 is expressed in polarized epithelial cells, which have the plasma membrane divided by tight junctions into an apical and a basolateral domain. In the present study we show that HAI-1 at steady-state is mainly located on the basolateral membrane of both Madin-Darby canine kidney cells and mammary gland epithelial cells. After biosynthesis, HAI-1 is exocytosed mainly to the basolateral plasma membrane from where 15% of the HAI-1 molecules are proteolytically cleaved and released into the basolateral medium. The remaining membrane-associated HAI-1 is endocytosed and then recycles between the basolateral plasma membrane and endosomes for hours until it is transcytosed to the apical plasma membrane. Minor amounts of HAI-1 present at the apical plasma membrane are proteolytically cleaved and released into the apical medium. Full-length membrane-bound HAI-1 has a half-life of 1.5 h and is eventually degraded in the lysosomes, whereas proteolytically released HAI-1 is more stable. HAI-1 is co-localized with its cognate protease, matriptase, at the basolateral plasma membrane. We suggest that HAI-1, in addition to its protease inhibitory function, plays a role in transporting matriptase as a matriptase-HAI-1 complex from the basolateral plama membrane to the apical plasma membrane, as matriptase is known to interact with prostasin, located at the apical plasma membrane.
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Registered trials
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