Presence of Two Distinct Transcripts for Matrilysin in Porcine Ovary(Biochemistry)
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概要
- 論文の詳細を見る
A cDNA encoding a matrix metalloproteinase-related protein has been cloned from a porcine ovary cDNA library. This putative protein comprises 119 amino acid residues, and exhibits sequence similarity with the NH_2-terminal half of rat matrilysin with 264 amino acid residues. A porcine ovary matrilysin cDNA clone was also isolated and characterized. A structural comparison of the matrilysin-related protein with porcine matrilysin suggests that both proteins are the products of the same gene. To further clarify their relationship, PCR amplification was carried out using porcine genomic DNA with two appropriate primers. The sequence analysis of a resulting 3.5kb PCR product revealed that a processing step involving internal exons of the gene produces the matrilysin-related protein. Relative amounts of the two distinct mRNAs in the porcine ovary were estimated by the competitive PCR method. The levels of mRNA for the matrilysin-related protein were approximately 4% of the wild-type matrilysin. The results indicate that the matrilysin-related protein is specifically expressed in the porcine ovary.
- 社団法人日本動物学会の論文
- 2000-05-20
著者
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Kimura Atsushi
Division of Biological Sciences, Graduate School of Science, Hokkaido University
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Kimura Atsushi
Laboratory Of Molecular And Cellular Interactions Faculty Of Advanced Life Science Hokkaido Universi
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Takahashi Takayuki
Division Of Biological Science Graduate School Of Science Hokkaido University
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Hirano Wakako
Division of Biological Sciences, Graduate School of Science, Hokkaido University
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Hirano Wakako
Division Of Biological Sciences Graduate School Of Science Hokkaido University
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Kimura Atsushi
Division Of Biological Sciences Graduate School Of Life Science Hokkaido University
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