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Ovarian Kaleidoscope Database (OKdb)

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Hsueh lab

HPMR

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


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R-L INTERACTIONS   MGI

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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
Comment
Ovarian function
Comment
Expression regulated by
Comment
Ovarian localization
Comment This gene was found in a rat ovarian cDNA library
Follicle stages
Comment
Phenotypes
Mutations 0 mutations
SNPs
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created: Jan. 9, 2000, midnight by: hsueh   email:
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last update: July 18, 2001, 2:11 p.m. by: hsueh    email:



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