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Titolo:
CLONING OF 3 CAENORHABDITIS-ELEGANS GENES POTENTIALLY ENCODING NOVEL MATRIX METALLOPROTEINASES
Autore:
WADA K; SATO H; KINOH H; KAJITA M; YAMAMOTO H; SEIKI M;
Indirizzi:
KANAZAWA UNIV,DEPT MOL ONCOL & VIROL,CANC RES INST KANAZAWA ISHIKAWA 920 JAPAN KANAZAWA UNIV,DEPT MOL ONCOL & VIROL,CANC RES INST KANAZAWA ISHIKAWA 920 JAPAN UNIV TOKYO,INST MED SCI,DEPT CANC CELL TOKYO 108 JAPAN KANAZAWA UNIV,SCH MED,DEPT BIOCHEM KANAZAWA ISHIKAWA 920 JAPAN
Titolo Testata:
Gene
fascicolo: 1, volume: 211, anno: 1998,
pagine: 57 - 62
SICI:
0378-1119(1998)211:1<57:CO3CGP>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
BASEMENT-MEMBRANE COLLAGEN; CELLS; INHIBITORS; ACTIVATION; METASTASIS; FURIN;
Keywords:
EXTRACELLULAR MATRIX; REMODELING; MORPHOGENESIS; GENOME DATABASE; TIMP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
K. Wada et al., "CLONING OF 3 CAENORHABDITIS-ELEGANS GENES POTENTIALLY ENCODING NOVEL MATRIX METALLOPROTEINASES", Gene, 211(1), 1998, pp. 57-62

Abstract

Three genes potentially encoding novel matrix metalloproteinases (MMPs) were identified by sequence similarity searching of Caenorhabditis elegans genome database, and cDNAs for these MMPs were cloned. The predicted gene products (MMP-C31, -H19 and -Y19) display a similar domainorganization to human MMPs. MMP-H19 and -Y19 are unique in that they have an RXKR motif between the propeptide and catalytic domains that is a furin-like cleavage site, and conserved only in stromelysin-3 and membrane-type MMPs. The amino acid sequence homology with MMP-1/human interstitial collagenase at the catalytic domain is 45%, 34% and 23% for MMP-C31, -H19 and -Y19, respectively. Recombinant proteins of C. elegans MMPs cleaved an MMP peptide substrate with efficiency proportional to their amino acid homology with human MMPs. Digestion of gelatin was observed only with MMP-C31. Enzyme activity of MMP-C31 and -H19 was inhibited by human tissue inhibitor of MMPs (TIMP)-1, TIMP-2 and synthetic MMP inhibitors, BB94 and CT543, indicating that the catalytic sites of these C. elegans MMPs are structurally closely related with those of mammalian MMPs. (C) 1998 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 06:50:55