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Literature summary for 3.4.24.23 extracted from

  • Tsunezumi, J.; Higashi, S.; Miyazaki, K.
    Matrilysin (MMP-7) cleaves C-type lectin domain family 3 member A (CLEC3A) on tumor cell surface and modulates its cell adhesion activity (2009), J. Cell. Biochem., 106, 693-702.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
C-type lectin domain family 3 member A + H2O i.e. CLEC3A. MMP-7 cleaves the 20 kDa CLEC3A protein, dividing it to a 15 kDa COOH-terminal fragment and an NH2-terminal fragment with the basic sequence. The 15 kDa fragment no longer has heparin-binding activity. Treatment of the CLEC3A-expressing cells with MMP-7 releases the 15 kDa CLEC3A into the culture supernatant. The native 20 kDa CLEC3A promotes cell adhesion to laminin-332 and fibronectin substrates, but this activity is abrogated by the cleavage by MMP-7 Homo sapiens ?
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