MMP9
MMP9 (Matrix metalloproteinase-9) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
Overview
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond.
CIViC holds 1 clinical evidence item and 0 assertions across 1 variant, naming Bevacizumab.
- Target · the protein and the cell it sits on
- Drug · antibody, small molecule, cell or radioligand
- Effect · signal, damage or kill
In plain words · MMP9 (Matrix metalloproteinase-9) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
- 1 · What it is
MMP9 (Matrix metalloproteinase-9) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
- 2 · What goes wrong in cancer
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption.
- 3 · How drugs use it
No product in this corpus aims at MMP9 yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
External identifiers
Sources: HGNC HGNC:7176 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P14780 (protein name, function text, keywords and locations (REST API)); CIViC gene MMP9 (1 evidence items, 0 assertions, 1 variants; diseases: Inflammatory Breast Carcinoma (GraphQL API, CC0))
Biology
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves NINJ1 to generate the Secreted ninjurin-1 form. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Location: Secreted, extracellular space, extracellular matrix (UniProt). Locus 20q13.12 (HGNC).
Notes
top- Written by scripts/fetch-cancer-genes.ts from CIViC, Open Targets, IntOGen, HGNC and UniProt; the function text is UniProt's, condensed and in UK spelling. Roles: CIViC lists 1 therapies; CIViC holds 1 clinical evidence items on its variants. Evidence tier "clinical-evidence" is the strongest of those signals.
- Prevalence not recorded: none of the sources gives a positivity rate.
- Diseases the sources name that have no OnCo cancer page yet, so they are not linked: Inflammatory Breast Carcinoma.
Latest papers
topQuery for this target: (TITLE:"MMP9" OR ABSTRACT:"MMP9" OR TITLE:"matrix metallopeptidase 9" OR ABSTRACT:"matrix metallopeptidase 9" OR TITLE:"Matrix metalloproteinase-9" OR ABSTRACT:"Matrix metalloproteinase-9" OR TITLE:"CLG4B" OR ABSTRACT:"CLG4B") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about MMP9, not a curated reading list.