MMP9

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.

Matrix Metallopeptidase 9

Matrix Metallopeptidase 9; Matrix Metalloproteinase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); EC 3.4.24.35; CLG4B; MMP-9; GELB; Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); Matrix Metalloproteinase-9;

Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:2551898, PubMed:1480034, PubMed:12879005).

Could play a role in bone osteoclastic resorption (By similarity).

Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005).

Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094).

Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034).

Degrades fibronectin but not laminin or Pz-peptide.

Cellular response to cadmium ion Source: CAFA
Cellular response to reactive oxygen species Source: CAFA
Cellular response to UV-A Source: UniProtKB
Collagen catabolic process Source: GO_Central
Embryo implantation Source: Ensembl
Endodermal cell differentiation Source: UniProtKB
Ephrin receptor signaling pathway Source: Reactome
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Leukocyte migration Source: InterPro
Macrophage differentiation Source: UniProtKB
Negative regulation of apoptotic process Source: CACAO
Negative regulation of cation channel activity Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: CACAO
Negative regulation of epithelial cell differentiation involved in kidney development Source: ARUK-UCL
Negative regulation of intrinsic apoptotic signaling pathway Source: CACAO
Ossification Source: InterPro
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of cell migration Source: ARUK-UCL
Positive regulation of DNA binding Source: CACAO
Positive regulation of epidermal growth factor receptor signaling pathway Source: CACAO
Positive regulation of keratinocyte migration Source: BHF-UCL
Positive regulation of protein phosphorylation Source: CACAO
Positive regulation of receptor binding Source: UniProtKB
Positive regulation of release of cytochrome c from mitochondria Source: CACAO
Positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Proteolysis Source: UniProtKB
Regulation of neuroinflammatory response Source: ARUK-UCL
Response to amyloid-beta Source: ARUK-UCL
Skeletal system development Source: Ensembl

Extracellular matrix

Intervertebral disc disease (IDD):
A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
Metaphyseal anadysplasia 2 (MANDP2):
A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.

Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
N- and O-glycosylated.