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Literature summary for 3.4.24.23 extracted from

  • Tsunezumi, J.; Yamamoto, K.; Higashi, S.; Miyazaki, K.
    Matrilysin (matrix metalloprotease-7) cleaves membrane-bound annexin II and enhances binding of tissue-type plasminogen activator to cancer cell surfaces (2008), FEBS J., 275, 4810-4823.
    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.
annexin II + H2O treatment of human colon cancer cell lines with active matrilysin releases a 35 kDa annexin II form, which lacked its N-terminal region, into the culture supernatant. The release of the 35 kDa annexin II by matrilysin is significantly enhanced in the presence of serotonin or heparin. Matrilysin hydrolyzes annexin II at the Lys9-Leu10 bond, thus dividing the protein into an N-terminal nonapeptide and the C-terminal 35 kDa fragment. The nonapeptide generated by matrilysin treatment might be anchored to the cell membrane, possibly by binding to intact annexin II, and interact with tissue-type plasminogen activator via its C-terminal lysine Homo sapiens ?
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