An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent mesh

Yasuyuki Matsuda, Takumi Koshiba, Tsukasa Osaki, Haruka Suyama, Fumio Arisaka, Yoshihiro Toh, Shun-Ichiro Kawabata

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抄録

In mammals, the cornified cell envelope forms beneath the plasma membrane in epithelia and provides a vital physical barrier consisting of insoluble proteins cross-linked by transglutaminase (TGase). In the horseshoe crab Tachypleus tridentatus, TGase is stored in hemocytes and secreted in response to the simulation of bacterial lipopolysaccharides. Here we characterized a TGase substrate designated as caraxin that was identified in horseshoe crab cuticle. One of the homologs, caraxin-1, possessed a unique domain structure consisting of N- and C-terminal heptad repeats and a central domain with a tandem-repeated structure of a pentapeptide. Western blotting showed the specific localization of caraxin-1 in sub-cuticular epidermis. Moreover, we identified the pentapeptide motif to be a chitin-binding unit. Analytical ultracentrifugation revealed that caraxin-1 exists as an oligomer with 310-350 kDa, which is ∼20-mer based on the molecular mass of the monomer. The oligomers were cross-linked by TGase to form an elaborate mesh with honeycomb structures, which was electron-microscopically found to be different from the clotting mesh triggered by lipopolysaccharide-induced hemocyte exocytosis. We determined several cross-linking sites in the N- and C-terminal domains of caraxin-1. The replacements of Leu to Pro at positions 36 and 118 in caraxin-1 reduced the α-helix content, which destroyed the TGase-dependent mesh, thus indicating the importance of the N- and C-terminal domains for the proper mesh formation. In arthropods, TGase-dependent protein cross-linking may be involved in the initial stage of host defense at the sub-cuticular epidermis, as in the case of mammalian skin.

元の言語英語
ページ(範囲)37316-37324
ページ数9
ジャーナルJournal of Biological Chemistry
282
発行部数52
DOI
出版物ステータス出版済み - 12 28 2007

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Transglutaminases
Chitin
Arthropods
Carrier Proteins
Horseshoe Crabs
Hemocytes
Oligomers
Epidermis
Lipopolysaccharides
Honeycomb structures
Architectural Accessibility
Mammals
Terminal Repeat Sequences
Ultracentrifugation
Exocytosis
Molecular mass
Cell membranes
Skin
Proteins
Epithelium

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent mesh. / Matsuda, Yasuyuki; Koshiba, Takumi; Osaki, Tsukasa; Suyama, Haruka; Arisaka, Fumio; Toh, Yoshihiro; Kawabata, Shun-Ichiro.

:: Journal of Biological Chemistry, 巻 282, 番号 52, 28.12.2007, p. 37316-37324.

研究成果: ジャーナルへの寄稿記事

Matsuda, Yasuyuki ; Koshiba, Takumi ; Osaki, Tsukasa ; Suyama, Haruka ; Arisaka, Fumio ; Toh, Yoshihiro ; Kawabata, Shun-Ichiro. / An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent mesh. :: Journal of Biological Chemistry. 2007 ; 巻 282, 番号 52. pp. 37316-37324.
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abstract = "In mammals, the cornified cell envelope forms beneath the plasma membrane in epithelia and provides a vital physical barrier consisting of insoluble proteins cross-linked by transglutaminase (TGase). In the horseshoe crab Tachypleus tridentatus, TGase is stored in hemocytes and secreted in response to the simulation of bacterial lipopolysaccharides. Here we characterized a TGase substrate designated as caraxin that was identified in horseshoe crab cuticle. One of the homologs, caraxin-1, possessed a unique domain structure consisting of N- and C-terminal heptad repeats and a central domain with a tandem-repeated structure of a pentapeptide. Western blotting showed the specific localization of caraxin-1 in sub-cuticular epidermis. Moreover, we identified the pentapeptide motif to be a chitin-binding unit. Analytical ultracentrifugation revealed that caraxin-1 exists as an oligomer with 310-350 kDa, which is ∼20-mer based on the molecular mass of the monomer. The oligomers were cross-linked by TGase to form an elaborate mesh with honeycomb structures, which was electron-microscopically found to be different from the clotting mesh triggered by lipopolysaccharide-induced hemocyte exocytosis. We determined several cross-linking sites in the N- and C-terminal domains of caraxin-1. The replacements of Leu to Pro at positions 36 and 118 in caraxin-1 reduced the α-helix content, which destroyed the TGase-dependent mesh, thus indicating the importance of the N- and C-terminal domains for the proper mesh formation. In arthropods, TGase-dependent protein cross-linking may be involved in the initial stage of host defense at the sub-cuticular epidermis, as in the case of mammalian skin.",
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AU - Arisaka, Fumio

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AU - Kawabata, Shun-Ichiro

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