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Literature summary for 3.4.21.7 extracted from

  • Christensen, B.; Schack, L.; Klaening, E.; Sorensen, E.S.
    Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D (2010), J. Biol. Chem., 285, 7929-7937.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
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 Homo sapiens
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
osteopontin + H2O Homo sapiens osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a substrate for plasmin and cathepsin D ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk plasmin is the principal protease in milk Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
osteopontin + H2O osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a substrate for plasmin and cathepsin D Homo sapiens ?
-
 ?
osteopontin + H2O osteopontin, purified from human milk, is cleaved at multiple sites close to its integrin-binding motifs, e.g. cleavage at Arg152-Ser153, detailed overview Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function plasmin is the principal protease in milk. Plasmin, but not cathepsin D, cleavage of osteopontin increases cell adhesion mediated by the alphaVbeta3- or alpha5beta1-integrins. Similar cellular adhesion is mediated by plasmin and thrombin-cleaved osteopontin, plasmin can be a potent regulator of osteopontin activity Homo sapiens