A link between blood coagulation and prophenol oxidase activation in arthropod host defense

研究成果: ジャーナルへの寄稿記事

128 引用 (Scopus)

抄録

Phenol oxidase, a copper-containing enzyme, is widely distributed not only in animals but also in plants and fungi, which is responsible for initiating the biosynthesis of melanin. Activation of prophenol oxidase in arthropods is important in host defense. However, the prophenol oxidase-activating system remains poorly understood at the molecular level. Here we show that the coagulation cascade of the horseshoe crab Tachypleus tridentatus is linked to prophenol oxidase activation, with the oxygen carrier hemocyanin functioning as a substitute for prophenol oxidase. Tachypleus clotting enzyme functionally transforms hemocyanin to phenol oxidase, and the conversion reaches a plateau at 1:1 stoichiometry without proteolytic cleavage. The active site-masked clotting enzyme also has the same effect, suggesting that complex formation of the clotting enzyme with hemocyanin is critical for the conversion. The two systems of blood coagulation and prophenol oxidase activation may have evolved from a common ancestral protease cascade.

元の言語英語
ページ(範囲)29264-29267
ページ数4
ジャーナルJournal of Biological Chemistry
275
発行部数38
DOI
出版物ステータス出版済み - 9 22 2000

Fingerprint

Arthropods
Blood Coagulation
Coagulation
Blood
Horseshoe Crabs
Chemical activation
Hemocyanin
Monophenol Monooxygenase
Biosynthesis
Melanins
Fungi
Stoichiometry
Copper
Catalytic Domain
Animals
Peptide Hydrolases
pro-phenoloxidase
Oxygen
Enzymes
clotting enzyme

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

A link between blood coagulation and prophenol oxidase activation in arthropod host defense. / Nagai, Taku; Kawabata, Shun-Ichiro.

:: Journal of Biological Chemistry, 巻 275, 番号 38, 22.09.2000, p. 29264-29267.

研究成果: ジャーナルへの寄稿記事

@article{09e0f6e91eb1495eaa7c897f6046f988,
title = "A link between blood coagulation and prophenol oxidase activation in arthropod host defense",
abstract = "Phenol oxidase, a copper-containing enzyme, is widely distributed not only in animals but also in plants and fungi, which is responsible for initiating the biosynthesis of melanin. Activation of prophenol oxidase in arthropods is important in host defense. However, the prophenol oxidase-activating system remains poorly understood at the molecular level. Here we show that the coagulation cascade of the horseshoe crab Tachypleus tridentatus is linked to prophenol oxidase activation, with the oxygen carrier hemocyanin functioning as a substitute for prophenol oxidase. Tachypleus clotting enzyme functionally transforms hemocyanin to phenol oxidase, and the conversion reaches a plateau at 1:1 stoichiometry without proteolytic cleavage. The active site-masked clotting enzyme also has the same effect, suggesting that complex formation of the clotting enzyme with hemocyanin is critical for the conversion. The two systems of blood coagulation and prophenol oxidase activation may have evolved from a common ancestral protease cascade.",
author = "Taku Nagai and Shun-Ichiro Kawabata",
year = "2000",
month = "9",
day = "22",
doi = "10.1074/jbc.M002556200",
language = "English",
volume = "275",
pages = "29264--29267",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "38",

}

TY - JOUR

T1 - A link between blood coagulation and prophenol oxidase activation in arthropod host defense

AU - Nagai, Taku

AU - Kawabata, Shun-Ichiro

PY - 2000/9/22

Y1 - 2000/9/22

N2 - Phenol oxidase, a copper-containing enzyme, is widely distributed not only in animals but also in plants and fungi, which is responsible for initiating the biosynthesis of melanin. Activation of prophenol oxidase in arthropods is important in host defense. However, the prophenol oxidase-activating system remains poorly understood at the molecular level. Here we show that the coagulation cascade of the horseshoe crab Tachypleus tridentatus is linked to prophenol oxidase activation, with the oxygen carrier hemocyanin functioning as a substitute for prophenol oxidase. Tachypleus clotting enzyme functionally transforms hemocyanin to phenol oxidase, and the conversion reaches a plateau at 1:1 stoichiometry without proteolytic cleavage. The active site-masked clotting enzyme also has the same effect, suggesting that complex formation of the clotting enzyme with hemocyanin is critical for the conversion. The two systems of blood coagulation and prophenol oxidase activation may have evolved from a common ancestral protease cascade.

AB - Phenol oxidase, a copper-containing enzyme, is widely distributed not only in animals but also in plants and fungi, which is responsible for initiating the biosynthesis of melanin. Activation of prophenol oxidase in arthropods is important in host defense. However, the prophenol oxidase-activating system remains poorly understood at the molecular level. Here we show that the coagulation cascade of the horseshoe crab Tachypleus tridentatus is linked to prophenol oxidase activation, with the oxygen carrier hemocyanin functioning as a substitute for prophenol oxidase. Tachypleus clotting enzyme functionally transforms hemocyanin to phenol oxidase, and the conversion reaches a plateau at 1:1 stoichiometry without proteolytic cleavage. The active site-masked clotting enzyme also has the same effect, suggesting that complex formation of the clotting enzyme with hemocyanin is critical for the conversion. The two systems of blood coagulation and prophenol oxidase activation may have evolved from a common ancestral protease cascade.

UR - http://www.scopus.com/inward/record.url?scp=0034703094&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034703094&partnerID=8YFLogxK

U2 - 10.1074/jbc.M002556200

DO - 10.1074/jbc.M002556200

M3 - Article

C2 - 10880508

AN - SCOPUS:0034703094

VL - 275

SP - 29264

EP - 29267

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 38

ER -