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Literature summary for 3.4.21.109 extracted from

  • Wu, C.J.; Feng, X.; Lu, M.; Morimura, S.; Udey, M.C.
    Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis (2017), J. Clin. Invest., 127, 623-634 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
medicine loss of cell surface protease inhibitor HAI-2 in intestinal epithelial cells leads to unrestrained matriptase activity and efficient cleavage of epithelial cell adhesion molecule EPCAM. Congenital tufting enteropathy-associated HAI-2 mutant proteins exhibit reduced ability to inhibit matriptase and also fail to efficiently stabilize claudin-7 in intestinal epithelial cells Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
EpCAM + H2O i.e. epithelial cell adhesion molecule CD326 Homo sapiens ?
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 ?

General Information

General Information Comment Organism
physiological function loss of cell surface protease inhibitor HAI-2 in intestinal epithelial cells leads to unrestrained matriptase activity and efficient cleavage of epithelial cell adhesion molecule EPCAM. Congenital tufting enteropathy-associated HAI-2 mutant proteins exhibit reduced ability to inhibit matriptase and also fail to efficiently stabilize claudin-7 in intestinal epithelial cells Homo sapiens