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Symbol MMP7 contributors: mct/pgu - updated : 20-03-2015
HGNC name matrix metallopeptidase 7 (matrilysin, uterine)
HGNC id 7174
  • a signal sequence
  • a prodomain with a cysteine residue,essential for latency and involved in autocatalytic activation
  • a catalytic domain with the zinc-binding site and lacking the hemopexin-like (PEX) C terminal domain
  • conjugated HemoP , MetalloP
    isoforms Precursor pro-form consists of only a propeptide and a catalytic domain and lacks the C-terminal hemopexin-like domain (.PMID: 18955490)
  • zinc dependent endopeptidases family
  • stromelysin subclass of MMP family
  • peptidase M10A family
  • CATEGORY enzyme , regulatory
    text secreted protein, extracellular matrix
    basic FUNCTION
  • regulator of matrix remodeling and mediator of pulmonary fibrosis (and potential therapeutic target)
  • generating angiostatin fragments by hydrolyzing plasminogen
  • may be responsible for the activation of prodefensins and thereby participating in innate host defense
  • remodeling of elastotic areas in sun damaged skin
  • required for the activation of defensin in small bowel
  • processes cell surface molecules such as pro-alpha-defensin, fas-ligand, pro-tumor necrosis factor alpha, E-cadherin
  • involved in adipocyte differentiation, enhanced collagen affinity, increased bioavailability of TGF beta, disrupted cell aggregation and increased cell invasion anf Fas-receptor-mediated apoptosis
  • degrades casein, gelatins of type I, III, IV, V, fibronectin and elastin
  • activating procollagenase
  • involved in wound healing
  • may regulate the activity of defensins in intestinal mucosa
  • potent modulator of synaptic vesicle recycling and synaptic ultrastructure and elevated levels of the enzyme, as may occur with brain inflammation, may adversely influence neurotransmission
  • involved in tumor angiogenesis, thereby contributing to malignant growth and hence associated with decreased survival
  • may be involved in the aging process of human mammary epithelial cells by affecting extracellular remodeling and intracellular signaling pathways
  • LAMB3, LAMC2, in conjunction with MMP7, play a key role in the progression of biliary tract cancer
  • is involved in the cleavage of CDH2 and modulates vascular smooth muscle cell (VSMC) apoptosis, and may therefore contribute to plaque development and rupture
  • new role for MMP7 in attenuating ciliated cell differentiation during wound repair
  • CELLULAR PROCESS cell life, differentiation
    cell life, cell death/apoptosis
    nucleotide, repair
    protein, degradation
    a component
    small molecule metal binding, cofactor,
  • binding two ions calcium Ca2+ per subunit
  • binding two ions zinc Zn2+ per subunit
  • protein
  • colocalizing and regulating DEFA5
  • interaction with ETS1 (contribution to the progression of HCC)
  • HAS2, HAS3 and HA may mediate cellular invasion via changes in MMP7 expression
  • binding TIMPs in a 1:1 stoechiometry
  • directly interacts with SDC2
  • MSLN enhances ovarian cancer invasion by MMP7 expression through the MAPK/ERK and JNK signal transduction pathways
  • MMP7 inhibition of BMP7 induced renal tubular branching morphogenesis suggests a role in the pathogenesis of human renal dysplasia
  • is a key downstream effector of FOXC1-mediated invasiveness in breast cancer
  • MMP7 is a target gene of EPCAM signalling via EpICD nuclear translocation
  • MMP7 is a bona fide ETV1 target gene, implicating that MMP7 upregulation is partially responsible for the oncogenic effects of ETV1 in the prostate
  • in the small intestine, MMP7 is responsible for activating DEFAs, which are broad-spectrum anti-microbial peptides produced by the Paneth cells
  • functions to degrade extracellular matrix and other pericellular substrates including the adherens junction protein CDH1 to promote wound healing and tissue remodeling
  • regulator of CTNNB1 function in injured lung epithelium and may link extracellular proteolytic activity to cell junction disassembly and intracellular signaling
  • cell & other
  • binding of MMP7 to cell surface cholesterol sulfate (CS) is essential for the cell membrane-associated proteolytic action of the protease
    activated by proteinases and plasmin
    binding of sulfated glycosaminoglycans, such as heparin, chondroitin-4,6-sulfate or dermatan sulfate
    inhibited by TIMPs and TFPI2
    binding a catalytic zinc ion
    Other regulated by beta catenin/CF4
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral       gain of function
    with ETS1 in hepatocellular carcinomas
    tumoral     --over  
    in colorectal cancer with metastasis
    tumoral       gain of function
    differentially up-regulated in germ cells teratomas
    constitutional     --over  
    in epithelium by bacterial infection, inflammation and fibrosis
    constitutional     --over  
    in congenital renal dysplasia (RD)
    Susceptibility to esophageal squamous cell carcinoma, gastric cardiac adenocarcinoma and non-small cell lung carcinoma
    Variant & Polymorphism SNP , other
  • polymorphism in the promoter increasing susceptibility to esophageal squamous cell carcinoma, gastric cardiac adenocarcinoma and non-small cell lung carcinoma
  • snp Gly137Asp confers risk of liver cirrhosis
  • functional variants of MMP7 are associated with susceptibility to H.pylori-induced precancerous gastric lesions
  • Candidate gene
  • positive expression may serve as a predictor of lymph node metastasis in gastric cancer
  • elevated expression is predictor of disease recurrence of colon cancer and is related to decreased survival
  • higher expression of MMP7 supports the notion of a role in the growth of lung carcinoma
  • Marker
    Therapy target
    develop MMP7-targeted novel anti-cancer drugs that block specifically the membrane-associated proteolytic action of this MMP, thereby having restricted side effects
    may be a useful therapeutic target for treatment of this disease
  • Paneth cells (in mice)
  • MMP7(-/-) mice are resistant to LPS-induced lethality and that this resistance is correlated with reduced levels of systemic cytokines