ArticleThe Journal of biological chemistry2011
Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- A start methionine mutation in matriptase causes the membrane anchor to be skipped and replaced by a cryptic signal peptide.The Journal of biological chemistry · 2026Article
- A biochemical difference between HAI-2 variants causing syndromic and non-syndromic Congenital Sodium Diarrhea.PloS one · 2026Article
- The cell-surface serine protease prostasin is lost during cervical squamous cell carcinogenesis.Human cell · 2025Article
- Understanding HAIs: Ally proteins in the fight against cancer.The FEBS journal · 2022Article
- Targeted HAI-2 deletion causes excessive proteolysis with prolonged active prostasin and depletion of HAI-1 monomer in intestinal but not epidermal epithelial cells.Human molecular genetics · 2021Article
- Targeted deletion of HAI-1 increases prostasin proteolysis but decreases matriptase proteolysis in human keratinocytes.Human cell · 2021Article
- Article
- Membrane-Anchored Serine Proteases and Protease-Activated Receptor-2-Mediated Signaling: Co-Conspirators in Cancer Progression.Cancer research · 2019Review
- Alpha-1 Antitrypsin-Deficient Macrophages Have Increased Matriptase-Mediated Proteolytic Activity.American journal of respiratory cell and molecular biology · 2017Article
- Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.The Journal of biological chemistry · 2017Article
- Article
- Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis.The Journal of clinical investigation · 2017Article
- Article
- The serine protease-mediated increase in intestinal epithelial barrier function is dependent on occludin and requires an intact tight junction.American journal of physiology. Gastrointestinal and liver physiology · 2016Article
- Natural Endogenous Human Matriptase and Prostasin Undergo Zymogen Activation via Independent Mechanisms in an Uncoupled Manner.PloS one · 2016Article
- Matriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in Lactation.PloS one · 2016Article
- The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.The Journal of biological chemistry · 2014Article
- A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.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
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The matriptase-prostasin proteolytic cascade is essential for epidermal tight junction formation and terminal epidermal differentiation. This proteolytic pathway may also be operative in a variety of other epithelia, as both matriptase and prostasin are involved in tight junction formation in epithelial monolayers. However, in polarized epithelial cells matriptase is mainly located on the basolateral plasma membrane whereas prostasin is mainly located on the apical plasma membrane. To determine how matriptase and prostasin interact, we mapped the subcellular itinerary of matriptase and prostasin in polarized colonic epithelial cells. We show that zymogen matriptase is activated on the basolateral plasma membrane where it is able to cleave relevant substrates. After activation, matriptase forms a complex with the cognate matriptase inhibitor, hepatocyte growth factor activator inhibitor (HAI)-1 and is efficiently endocytosed. The majority of prostasin is located on the apical plasma membrane albeit a minor fraction of prostasin is present on the basolateral plasma membrane. Basolateral prostasin is endocytosed and transcytosed to the apical plasma membrane where a long retention time causes an accumulation of prostasin. Furthermore, we show that prostasin on the basolateral membrane is activated before it is transcytosed. This study shows that matriptase and prostasin co-localize for a brief period of time at the basolateral plasma membrane after which prostasin is transported to the apical membrane as an active protease. This study suggests a possible explanation for how matriptase or other basolateral serine proteases activate prostasin on its way to its apical destination.
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