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Literature summary for 3.4.21.B6 extracted from

  • Miller, G.S.; List, K.
    The matriptase-prostasin proteolytic cascade in epithelial development and pathology (2013), Cell Tissue Res., 351, 245-253.
    View publication on PubMed
Search for more literature for 3.4.21.B6

Inhibitors

Inhibitors Comment Organism Structure
hepatocyte growth factor activator inhibitor-1 HAI-1 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Mus musculus 9986
-
membrane prostasin contains an N-terminal secretion signal that is cleaved during intracellular transport in the endoplasmic reticulum and a GPI-anchor is attached at the C-terminal. Subsequent to surface localization, prostasin is cleaved at a conserved activation site in the pro-domain and remains attached to the serine protease domain via a disulfide bridge Mus musculus 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
proform filaggrin + H2O Mus musculus
-
 mature filaggrin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9ESD1
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification prostasin zymogen is incapable of auto-activation and requires proteolytic processing by a second protease, i.e. matriptase, for conversion into an active protease Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
epidermis
-
 Mus musculus
-
epithelium in polarized epithelium, matriptase and prostasin co-localize briefly at the basolateral plasma membrane prior to HAI-1-mediated matriptase endocytosis Mus musculus
-
additional information in nearly all murine epithelial tissues, matriptase is coexpressed with the membrane serine protease prostasin Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
proform filaggrin + H2O
-
 Mus musculus mature filaggrin + ?
-
 ?

Subunits

Subunits Comment Organism
More from the N-terminus, prostasin comprises a pro-domain and a serine protease domain with trypsin-like activity, prostasin contains an N-terminal secretion signal that is cleaved during intracellular transport in the endoplasmic reticulum and a GPI-anchor is attached at the C-terminal Mus musculus

Synonyms

Synonyms Comment Organism
CAP-1
-
 Mus musculus
channel-activating protease 1
-
 Mus musculus

General Information

General Information Comment Organism
malfunction matriptase and prostasin null mice have identical phenotypes. mice deficient for matriptase phenocopy mice deficient for epidermal prostasin and show impaired corneocyte differentiation, imparied lipid matrix formation, loss of profilaggrin processing and loss of tight junction formation and function. Together, these defects lead to a compromised epidermal barrier and result in fatal dehydration during the neonatal period. The proteolytic processing of prostasin as well as profilaggrin is greatly reduced in matriptase hypomorphic mice Mus musculus
additional information spatial and temporal co-expression of matriptase and prostasin Mus musculus
physiological function the enzyme has the ability to activate epithelial sodium channels and effect the sodium current across the plasma membrane in vitro. In the epidermis, the glycosylphosphatidylinositol anchored membrane serine protease prostasin is activated by matriptase to initiate a proteolytic cascade that is required for the development of the stratum corneum barrier function. Proteolytic activity of the matriptase-prostasin cascade is regulated in the epidermis via inhibition by the Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-1 Mus musculus