KMID : 0603519990040010017
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Journal of Korean Association of Cancer Prevention 1999 Volume.4 No. 1 p.17 ~ p.24
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Cloning of Membrane Type-3 Matrix Metalloproteinase (MT3-MMP) Gene from Scyliorhinus Torazame
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Kim Myung-Soon
Bae Moon-Kyoung Kim Ji-Tae Song Hyun-Seok Ahn Mee-Young Kim Jong-Won Lim Woon-Ki Kim Kyu-Won Kim Yung-Jin
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Abstract
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Matrix metalloproteinases (MMPs) are zinc-binding endopeptides that collectively degrade the constituent macromolecules of the extracellular matrix. Thus, the MMPs are thought to play important roles during organ morphogenesis, embryonic development and pathological processes. However, MMP genes, including MT-MMPs, were previously cloned and their functions were studied in mammalians such as human, mouse, and chick, but not yet in fishes. In this study, we cloned the 5¡¯region and 3¡¯region of shark MT3-MMP gene and analyzed their sequences in comparison with those of other species. The nucleotide sequence of the 450 bp PCR product by 5¡¯RACE is 74% identical to MT3-MMP genes of human, rat, and chick, by the Genbank nucleotide data base search. Also, 5¡¯region of shark MT3-MMP contains 37 bp 5¡¯UTR (untranslated region), start codon (ATG), the putative signal peptide, and cystein switch domain (RXKR motif). The nucleotide sequence of the 1,400 bp 3¡¯LD-PCR product shows 80% homologies to the MT3-MMP of them. 5¡¯region of shark MT3-MMP contains stop codon (TGA) and 76 bp of the putative transmembrane domain.
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KEYWORD
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Membrane type matrix metalloproteinase, Shark
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