Molecular cloning of cDNA for pro-phenol-oxidase-activating factor i, a serine protease is induced by lipopolysaccharide or 1,3-β-glucan in coleopteran insect, Holotrichia diomphalia larvae

So Young Lee, Mi Young Cho, Ji Hoon Hyun, Kwang Moon Lee, Ko Ichi Homma, Shunji Natori, Shun-Ichiro Kawabata, Sadaaki Iwanaga, Bok Luel Lee

研究成果: ジャーナルへの寄稿記事

103 引用 (Scopus)

抄録

Previously, we identified two pro-phenol oxidase-activating factors, named PPAF-I and PPAF-II, directly involved in the activation of the purified pro-phenol oxidase (pro-PO) from the hemolymph of the coleopteran, Holotrichia diomphalia larvae [Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S. I., Iwanga, S, and Lee, B. L. (1998) Eur. J. Biochem. 254, 90-97]. Here, we report molecular cloning of cDNA for PPAF-I. Based on the sequence of the cloned cDNA, the PPAF-I gene appears to encode a member of serine protease zymogen consisting of 365 amino acid residues with a molecular mass of 40193 Da. The 109 amino acid residues preceding the amino- terminus Ile residue of the mature protein seem to constitute a prepro- sequence. The mature protein is a serine protease composed of 256 amino acids with a calculated molecular mass of 28009 Da. The overall structure is highly similar to that of Drosophila easter serine protease (42.9% identity), an essential serine protease zymogen for pattern formation in normal embryonic development. The locations of disulfide linkages in the pro-segment of PPAF- I were similar to those of Tachypleus proclotting enzyme and the mammalian neutrophil-derived defensin. Furthermore, [3H]diisopropylphosphate (iPr2P)- labeled PPAF-I was specifically produced from the crude preparation of PPAF- I zymogen by incubation with lipopolysaccharide or 1,3-β-glucan, whereas [3H]iPr2P-labeled PPAF-I was not produced under the same conditions in the absence of these microbial polysaccharides. These results indicate that the pro-PO-activation system in H. diomphalia larvae may proceed with the activation of PPAF-I zymogen by microbial polysaccharides.

元の言語英語
ページ(範囲)615-621
ページ数7
ジャーナルEuropean Journal of Biochemistry
257
発行部数3
DOI
出版物ステータス出版済み - 11 1 1998

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Enzyme Precursors
Glucans
Monophenol Monooxygenase
Cloning
Molecular Cloning
Serine Proteases
Larva
Insects
Lipopolysaccharides
Complementary DNA
Chemical activation
Molecular mass
Amino Acids
Polysaccharides
Defensins
Horseshoe Crabs
Hemolymph
Disulfides
Drosophila
Embryonic Development

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Molecular cloning of cDNA for pro-phenol-oxidase-activating factor i, a serine protease is induced by lipopolysaccharide or 1,3-β-glucan in coleopteran insect, Holotrichia diomphalia larvae. / Lee, So Young; Cho, Mi Young; Hyun, Ji Hoon; Lee, Kwang Moon; Homma, Ko Ichi; Natori, Shunji; Kawabata, Shun-Ichiro; Iwanaga, Sadaaki; Lee, Bok Luel.

:: European Journal of Biochemistry, 巻 257, 番号 3, 01.11.1998, p. 615-621.

研究成果: ジャーナルへの寄稿記事

Lee, So Young ; Cho, Mi Young ; Hyun, Ji Hoon ; Lee, Kwang Moon ; Homma, Ko Ichi ; Natori, Shunji ; Kawabata, Shun-Ichiro ; Iwanaga, Sadaaki ; Lee, Bok Luel. / Molecular cloning of cDNA for pro-phenol-oxidase-activating factor i, a serine protease is induced by lipopolysaccharide or 1,3-β-glucan in coleopteran insect, Holotrichia diomphalia larvae. :: European Journal of Biochemistry. 1998 ; 巻 257, 番号 3. pp. 615-621.
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abstract = "Previously, we identified two pro-phenol oxidase-activating factors, named PPAF-I and PPAF-II, directly involved in the activation of the purified pro-phenol oxidase (pro-PO) from the hemolymph of the coleopteran, Holotrichia diomphalia larvae [Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S. I., Iwanga, S, and Lee, B. L. (1998) Eur. J. Biochem. 254, 90-97]. Here, we report molecular cloning of cDNA for PPAF-I. Based on the sequence of the cloned cDNA, the PPAF-I gene appears to encode a member of serine protease zymogen consisting of 365 amino acid residues with a molecular mass of 40193 Da. The 109 amino acid residues preceding the amino- terminus Ile residue of the mature protein seem to constitute a prepro- sequence. The mature protein is a serine protease composed of 256 amino acids with a calculated molecular mass of 28009 Da. The overall structure is highly similar to that of Drosophila easter serine protease (42.9{\%} identity), an essential serine protease zymogen for pattern formation in normal embryonic development. The locations of disulfide linkages in the pro-segment of PPAF- I were similar to those of Tachypleus proclotting enzyme and the mammalian neutrophil-derived defensin. Furthermore, [3H]diisopropylphosphate (iPr2P)- labeled PPAF-I was specifically produced from the crude preparation of PPAF- I zymogen by incubation with lipopolysaccharide or 1,3-β-glucan, whereas [3H]iPr2P-labeled PPAF-I was not produced under the same conditions in the absence of these microbial polysaccharides. These results indicate that the pro-PO-activation system in H. diomphalia larvae may proceed with the activation of PPAF-I zymogen by microbial polysaccharides.",
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T1 - Molecular cloning of cDNA for pro-phenol-oxidase-activating factor i, a serine protease is induced by lipopolysaccharide or 1,3-β-glucan in coleopteran insect, Holotrichia diomphalia larvae

AU - Lee, So Young

AU - Cho, Mi Young

AU - Hyun, Ji Hoon

AU - Lee, Kwang Moon

AU - Homma, Ko Ichi

AU - Natori, Shunji

AU - Kawabata, Shun-Ichiro

AU - Iwanaga, Sadaaki

AU - Lee, Bok Luel

PY - 1998/11/1

Y1 - 1998/11/1

N2 - Previously, we identified two pro-phenol oxidase-activating factors, named PPAF-I and PPAF-II, directly involved in the activation of the purified pro-phenol oxidase (pro-PO) from the hemolymph of the coleopteran, Holotrichia diomphalia larvae [Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S. I., Iwanga, S, and Lee, B. L. (1998) Eur. J. Biochem. 254, 90-97]. Here, we report molecular cloning of cDNA for PPAF-I. Based on the sequence of the cloned cDNA, the PPAF-I gene appears to encode a member of serine protease zymogen consisting of 365 amino acid residues with a molecular mass of 40193 Da. The 109 amino acid residues preceding the amino- terminus Ile residue of the mature protein seem to constitute a prepro- sequence. The mature protein is a serine protease composed of 256 amino acids with a calculated molecular mass of 28009 Da. The overall structure is highly similar to that of Drosophila easter serine protease (42.9% identity), an essential serine protease zymogen for pattern formation in normal embryonic development. The locations of disulfide linkages in the pro-segment of PPAF- I were similar to those of Tachypleus proclotting enzyme and the mammalian neutrophil-derived defensin. Furthermore, [3H]diisopropylphosphate (iPr2P)- labeled PPAF-I was specifically produced from the crude preparation of PPAF- I zymogen by incubation with lipopolysaccharide or 1,3-β-glucan, whereas [3H]iPr2P-labeled PPAF-I was not produced under the same conditions in the absence of these microbial polysaccharides. These results indicate that the pro-PO-activation system in H. diomphalia larvae may proceed with the activation of PPAF-I zymogen by microbial polysaccharides.

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