Matrix Metalloproteinase-23 OKDB#: 377
 Symbols: Matrix Metalloproteinase-23 Species: human
 Synonyms:  Locus:


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R-L INTERACTIONS   MGI

DNA Microarrays
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General Comment A cDNA encoding a new human matrix metalloproteinase (MMP), tentatively called MMP-23, has been cloned from an ovary cDNA library by Velasco et al . This protein exhibits sequence similarity with MMPs, but displays a different domain structure. Thus, MMP-23 lacks a recognizable signal sequence and has a short prodomain, although it contains a single cysteine residue that can be part of the cysteine-switch mechanism operating for maintaining enzyme latency. The C-terminal domain is considerably shortened and shows no sequence similarity to hemopexin, whereas all human MMPs, with the exception of matrilysin, contain four hemopexin-like repeats. Furthermore, MMP-23 is devoid of structural features distinctive of the diverse MMP subclasses, including the specific residues located close to the zinc-binding site in collagenases, the transmembrane domain of membrane-type MMPs, or the fibronectin-like domain of gelatinases. Recombinant MMP-23 produced in Escherichia coli exhibits low, but significant proteolytic activity against a synthetic substrate commonly used for assaying MMPs. Northern blot analysis demonstrated that MMP-23 is predominantly expressed in ovary, testis, and prostate, suggesting that this new MMP may play a specialized role in reproductive processes.
General function Enzyme, Hydrolase, Peptidase/Protease
Comment
Cellular localization Extracellular Matrix
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Ovarian function
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Expression regulated by
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Ovarian localization
Comment This gene was found in a rat ovarian cDNA library
Follicle stages
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created: 2000-01-09 00:00:00 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu
home page: http://reprobio.stanford.edu/hsueh
last update: 2001-07-18 14:11:21 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu



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