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Literature summary for 3.4.24.23 extracted from

  • Thiolloy, S.; Halpern, J.; Holt, G.E.; Schwartz, H.S.; Mundy, G.R.; Matrisian, L.M.; Lynch, C.C.
    Osteoclast-derived matrix metalloproteinase-7, but not matrix metalloproteinase-9, contributes to tumor-induced osteolysis (2009), Cancer Res., 69, 6747-6755.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information host MMP-7 contributes to mammary tumor growth in the bone microenvironment after injection of human tumor cells into tibias of mice Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
bone cancer cell the matrix metalloproteinases MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 are highly expressed in the tumor-bone microenvironment, and, of these, MMP-7 and MMP-9 are found to be localized to bone-resorbing osteoclasts in human breast-to-bone metastases Homo sapiens
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osteoclast
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 Homo sapiens
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Synonyms

Synonyms Comment Organism
Matrix metalloproteinase-7
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function osteoclast-derived MMP-7 significantly contributes to tumor growth and tumor-induced osteolysis, overview. Solubilization of RANKL by MMP-7 is a potential mechanism through which MMP-7 mediates mammary tumor-induced osteolysis, mechanism, overview. MMP-7 is capable of processing a number of nonmatrix molecules to soluble active forms that have profound effects on cell-cell communication, such as RANKL, a crucial mediator of osteoclast precursor recruitment and maturation Homo sapiens