MMP9
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]
Function
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 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. 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.[2]
References
- ^ a b "Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4318.
- ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2427305.
Further reading
- 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
- The MEROPS online database for peptidases and their inhibitors: M10.009
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ADAM proteins |
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Matrix metalloproteinases |
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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PDB gallery
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1itv: Dimeric form of the haemopexin domain of MMP9
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1l6j: Crystal structure of human matrix metalloproteinase MMP9 (gelatinase B).
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