Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin

Tsukasa Osaki, Nozomu Okino, Fuminori Tokunaga, Sadaaki Iwanaga, Shun-Ichiro Kawabata

研究成果: ジャーナルへの寄稿記事

44 引用 (Scopus)

抄録

Monoclonal antibodies were raised against hemocytes of the horseshoe crab Tachypleus tridentatus. All of the antibodies obtained reacted with the same protein bands on SDS-PAGE of hemocyte lysate. Flow cytometry and biotinylation of surface substances on the hemocytes indicated that the antigens are major peripheral proteins of hemocytes. The antigens were purified from hemocyte lysate and were good substrates for the horseshoe crab hemocyte transglutaminase (HcTGase). Transglutaminases play an important role during the final stage of blood coagulation in mammals and crustaceans. Although HcTGase did not intermolecularly cross-link a clottable protein coagulogen or its proteolytic product coagulin, HcTGase promoted the cross-linking of coagulin with the surface antigens, resulting in the formation of a stable polymer. We determined the nucleotide sequences for two isoproteins of the antigens. The two proteins containing 271 and 284 residues (66% identity) were composed of tandem repeats of proline-rich segments. We named them proxins-1 and -2 after proline-rich proteins for protein cross-linking. Proxins may form a stable physical barrier against invading pathogens in cooperation with hemolymph coagulation at injured sites.

元の言語英語
ページ(範囲)40084-40090
ページ数7
ジャーナルJournal of Biological Chemistry
277
発行部数42
DOI
出版物ステータス出版済み - 10 18 2002

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Horseshoe Crabs
Hemocytes
Thromboplastin
Surface Antigens
Proline
Transglutaminases
Substrates
Proteins
Coagulation
Antigens
Tandem Repeat Sequences
Mammals
Flow cytometry
Pathogens
Biotinylation
Architectural Accessibility
Hemolymph
Polymers
Blood Coagulation
Blood

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin. / Osaki, Tsukasa; Okino, Nozomu; Tokunaga, Fuminori; Iwanaga, Sadaaki; Kawabata, Shun-Ichiro.

:: Journal of Biological Chemistry, 巻 277, 番号 42, 18.10.2002, p. 40084-40090.

研究成果: ジャーナルへの寄稿記事

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abstract = "Monoclonal antibodies were raised against hemocytes of the horseshoe crab Tachypleus tridentatus. All of the antibodies obtained reacted with the same protein bands on SDS-PAGE of hemocyte lysate. Flow cytometry and biotinylation of surface substances on the hemocytes indicated that the antigens are major peripheral proteins of hemocytes. The antigens were purified from hemocyte lysate and were good substrates for the horseshoe crab hemocyte transglutaminase (HcTGase). Transglutaminases play an important role during the final stage of blood coagulation in mammals and crustaceans. Although HcTGase did not intermolecularly cross-link a clottable protein coagulogen or its proteolytic product coagulin, HcTGase promoted the cross-linking of coagulin with the surface antigens, resulting in the formation of a stable polymer. We determined the nucleotide sequences for two isoproteins of the antigens. The two proteins containing 271 and 284 residues (66{\%} identity) were composed of tandem repeats of proline-rich segments. We named them proxins-1 and -2 after proline-rich proteins for protein cross-linking. Proxins may form a stable physical barrier against invading pathogens in cooperation with hemolymph coagulation at injured sites.",
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