MMP9
GeneName
MMP9
Summary
MMP9, also known as MMP-9 or matrix metalloproteinase-9, is a 78kDa enzyme that is secreted into the extracellular space and is a member of the matrix metalloproteinase family. It plays a crucial role in the degradation of the extracellular matrix, particularly collagen, and is involved in various physiological processes such as tissue remodelling, wound healing, and inflammation. MMP9 is expressed in various tissues and is particularly active during processes like cell migration, macrophage differentiation, and embryonic development. Its enzymatic activity is mediated by its ability to bind zinc ions and perform endopeptidase functions, facilitating the breakdown of extracellular matrix components and influencing cell behaviour through signalling pathways.
Importance
MMP9 is relevant to: - Cancer progression and metastasis due to its role in extracellular matrix remodelling and facilitating tumour invasion - Inflammatory diseases as it contributes to the regulation of immune cell migration and tissue repair - Cardiovascular diseases where it is implicated in atherosclerosis and vascular remodelling - Neurodegenerative disorders, including Alzheimer’s disease, through its involvement in neuroinflammatory responses and amyloid-beta processing
Top Products
For researchers investigating MMP9, we highly recommend the top-selling recombinant antibody, Anti-MMP9 antibody [EP1254] (ab76003). This well-cited product has garnered 806 citations, underscoring its reliability and trust within the scientific community. It has been validated in knockout models and is suitable for a variety of applications, including Western blotting (WB), immunohistochemistry (IHC), immunocytochemistry (ICC), and flow cytometry (FC). This versatility makes it an excellent choice for those requiring consistent and effective detection of MMP9 in their studies. "The Human MMP9 ELISA Kit (ab246539), supported by 23 citations, is an excellent option for researchers looking to accurately measure MMP9 levels in their samples."
Abcam Product Citation Summary
The data indicates a significant focus on the role of MMP9 in various cancer types, particularly in studies related to cell migration, invasion, and epithelial-mesenchymal transition. Additionally, MMP9 is being investigated in the context of inflammatory responses and ischemia, highlighting its potential involvement in both cancer progression and tissue repair mechanisms. The use of multiple species, including human and rat models, suggests a broad interest in understanding MMP9's biological functions across different contexts.
Abcam Product Citation Table
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Function
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). 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.
Involvement in disease
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.
None
Disease susceptibility is associated with variants affecting the gene represented in this entry.
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
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.
Sequence Similarities
Belongs to the peptidase M10A family.
Tissue Specificity
Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
CLG4B, MMP9, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB
Database links
swissprot:P14780 omim:120361 entrezGene:4318
Other research areas
- Cardiovascular
- Immunology & Infectious Disease
- Neuroscience