MMP23B explained

Matrix metalloproteinase-23 is an enzyme that in humans is encoded by the MMP23B gene.^{[1] [2] [3]}

Function

This gene (MMP23B) encodes a member of the matrix metalloproteinase (MMP) family, and it is part of a duplicated region of chromosome 1p36.3. 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. This gene belongs to the copy of the duplicated region of the gene that is closer to the end of the chromosome (more telemeric).

MMP23B is strongly expressed in ovary and heart.^[4]

Further reading

• Nagase H, Woessner JF . Matrix metalloproteinases . J. Biol. Chem. . 274 . 31 . 21491–4 . 1999 . 10419448 . 10.1074/jbc.274.31.21491 . free .
• Velasco G, Pendás AM, Fueyo A, etal . Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members . J. Biol. Chem. . 274 . 8 . 4570–6 . 1999 . 9988691 . 10.1074/jbc.274.8.4570 . free .
• Terp GE, Christensen IT, Jørgensen FS . Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes . J. Biomol. Struct. Dyn. . 17 . 6 . 933–46 . 2000 . 10949161 . 10.1080/07391102.2000.10506582. 1270176 .
• Ohnishi J, Ohnishi E, Jin M, etal . Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development . Mol. Endocrinol. . 15 . 5 . 747–64 . 2001 . 11328856 . 10.1210/mend.15.5.0638 . 22774708 . free .
• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Gajecka M, Yu W, Ballif BC, etal . Delineation of mechanisms and regions of dosage imbalance in complex rearrangements of 1p36 leads to a putative gene for regulation of cranial suture closure . Eur. J. Hum. Genet. . 13 . 2 . 139–49 . 2005 . 15483646 . 10.1038/sj.ejhg.5201302 . free .
• Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Gregory SG, Barlow KF, McLay KE, etal . The DNA sequence and biological annotation of human chromosome 1 . Nature . 441 . 7091 . 315–21 . 2006 . 16710414 . 10.1038/nature04727 . 2006Natur.441..315G . free .

External links

• The MEROPS online database for peptidases and their inhibitors: M10.022

Notes and References

1. Gururajan R, Grenet J, Lahti JM, Kidd VJ . Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3 . Genomics . 52 . 1 . 101–6 . May 1999 . 9740677 . 10.1006/geno.1998.5401 .
2. Gururajan R, Lahti JM, Grenet J, Easton J, Gruber I, Ambros PF, Kidd VJ . Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2 . Genome Res . 8 . 9 . 929–39 . Nov 1998 . 9750192 . 310781 . 10.1101/gr.8.9.929.
3. Web site: Entrez Gene: MMP23B matrix metallopeptidase 23B.
4. Zhao S, Zhao Y, Niu P, Wang N, Tang Z, Zan L, Li K . Molecular characterization of porcine MMP19 and MMP23B genes and its association with immune traits . Int. J. Biol. Sci. . 7 . 8 . 1101–13 . 2011 . 21927579 . 10.7150/ijbs.7.1101 . 3174387.