From Wikipedia, the free encyclopedia
Jump to: navigation, search
Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)

PDB rendering based on 1itv.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols MMP9 ; CLG4B; GELB; MANDP2; MMP-9
External IDs OMIM120361 MGI97011 HomoloGene3659 ChEMBL: 321 GeneCards: MMP9 Gene
EC number
RNA expression pattern
PBB GE MMP9 203936 s at.png
More reference expression data
Species Human Mouse
Entrez 4318 17395
Ensembl ENSG00000100985 ENSMUSG00000017737
UniProt P14780 P41245
RefSeq (mRNA) NM_004994 NM_013599
RefSeq (protein) NP_004985 NP_038627
Location (UCSC) Chr 20:
44.64 – 44.65 Mb
Chr 2:
164.94 – 164.96 Mb
PubMed search [1] [2]

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is an enzyme that in humans is encoded by the MMP9 gene.[1]


Proteases of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage,[2] and metastasis.[3] Most MMPs 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 and other extracellular matrix proteins.[4] 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.[1]

Thrombospondins, intervertebral disc proteins, regulate the effective levels of matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling.[5]

Clinical significance[edit]

MMP's play a role in inflammation associated with aortic aneurysms. Doxycycline suppresses the growth of aortic aneurysms through its inhibition of matrix metalloproteinase 9.[6]

MMPs such as MMP9 can be involved in the development of several human malignancies, as degradation of collagen IV in basement membrane and extracellular matrix facilitates tumor progression, including invasion, metastasis, growth and angiogenesis.[7]


  1. ^ a b "Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)". 
  2. ^ Wang J, Tsirka SE (2005). "Neuroprotection by inhibition of matrix metalloproteinases in a mouse model of intracerebral haemorrhage.". Brain 128 (7): 1622–33. doi:10.1093/brain/awh489. PMID 15800021. 
  3. ^ Vandooren J, Van den Steen PE, Opdenakker G. (2013). "Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade". Crit Rev Biochem Mol Biol. PMID 23547785
  4. ^ Van den Steen PE, Dubois B, Nelissen I, Rudd PM, Dwek RA, Opdenakker G (2002). "Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9)". Crit Rev Biochem Mol Biol 37(6):375-536. PMID 12540195
  5. ^ Hirose Y, Chiba K, Karasugi T, Nakajima M, Kawaguchi Y, Mikami Y, Furuichi T, Mio F, Miyake A, Miyamoto T, Ozaki K, Takahashi A, Mizuta H, Kubo T, Kimura T, Tanaka T, Toyama Y, Ikegawa S (May 2008). "A Functional Polymorphism in THBS2 that Affects Alternative Splicing and MMP Binding Is Associated with Lumbar-Disc Herniation". Am. J. Hum. Genet. 82 (5): 1122–9. doi:10.1016/j.ajhg.2008.03.013. PMC 2427305. PMID 18455130. 
  6. ^ Lindeman JH, Abdul-Hussien H, van Bockel JH, Wolterbeek R, Kleemann R (April 2009). "Clinical trial of doxycycline for matrix metalloproteinase-9 inhibition in patients with an abdominal aneurysm: doxycycline selectively depletes aortic wall neutrophils and cytotoxic T cells". Circulation 119 (16): 2209–16. doi:10.1161/CIRCULATIONAHA.108.806505. PMID 19364980. 
  7. ^ Groblewska, M; Siewko M, Mroczko B, Szmitkowski M (2012). "The role of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in the development of esophageal cancer.". Folia Histochem Cytobiol 50: 12–19. PMID 22532131. 

Further reading[edit]

  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
  • Starckx S, Van den Steen PE, Wuyts A, et al. (2003). "Neutrophil gelatinase B and chemokines in leukocytosis and stem cell mobilization". Leuk. Lymphoma 43 (2): 233–41. doi:10.1080/10428190290005982. PMID 11999552. 
  • Bischof P, Meisser A, Campana A (2002). "Control of MMP-9 expression at the maternal-fetal interface". J. Reprod. Immunol. 55 (1–2): 3–10. doi:10.1016/S0165-0378(01)00142-5. PMID 12062817. 
  • St-Pierre Y, Van Themsche C, Estève PO (2003). "Emerging features in the regulation of MMP-9 gene expression for the development of novel molecular targets and therapeutic strategies". Current drug targets. Inflammation and allergy 2 (3): 206–15. doi:10.2174/1568010033484133. PMID 14561155. 
  • Lee JM, Yin K, Hsin I, et al. (2005). "Matrix metalloproteinase-9 in cerebral-amyloid-angiopathy-related hemorrhage". J. Neurol. Sci. 229-230: 249–54. doi:10.1016/j.jns.2004.11.041. PMID 15760647. 
  • Nair RR, Boyd DD (2006). "Expression cloning of novel regulators of 92 kDa type IV collagenase expression". Biochem. Soc. Trans. 33 (Pt 5): 1135–6. doi:10.1042/BST20051135. PMID 16246065. 
  • Ram M, Sherer Y, Shoenfeld Y (2006). "Matrix metalloproteinase-9 and autoimmune diseases". J. Clin. Immunol. 26 (4): 299–307. doi:10.1007/s10875-006-9022-6. PMID 16652230. 

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: M10.009