메뉴 건너뛰기




Volumn 83, Issue 4, 2007, Pages 110-119

Biochemical principle of Limulus test for detecting bacterial endotoxins

(1)  Iwanaga, Sadaaki a,b  

b NONE   (Japan)

Author keywords

Bacterial endotoxins; Clotting factors; Horseshoe crab (Tachypleus tridentatus); Innate immunity; Limulus test; Lipopolysacchalides (LPS)

Indexed keywords

BACTERIA (MICROORGANISMS); LIMULUS; MEROSTOMATA; NEGIBACTERIA; TACHYPLEUS TRIDENTATUS;

EID: 34249033051     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.83.110     Document Type: Review
Times cited : (57)

References (49)
  • 1
    • 0003125585 scopus 로고
    • High, K. and Roberts, H.R, eds, Marcel Dekker, Inc. New York, Basel, Hong Kong
    • High, K. and Roberts, H.R. (eds.) (1995) Molecular Basis of Thrombosis and Hemostasis. Marcel Dekker, Inc. New York, Basel, Hong Kong.
    • (1995) Molecular Basis of Thrombosis and Hemostasis
  • 2
    • 34249073559 scopus 로고    scopus 로고
    • Klein, J. and Horejsi, V, eds, Blackwell Science Inc, USA, pp
    • Klein, J. and Horejsi, V. (eds.) (1997) Complement and complement receptors in Immunology. Blackwell Science Inc., USA, pp. 348-392.
    • (1997) Complement and complement receptors in Immunology , pp. 348-392
  • 3
    • 0033973826 scopus 로고    scopus 로고
    • Signaling mechanisms in the antimicrobial host defense of Drosophila
    • Imler, J.-L. and Hoffmann, J.R. (2000) Signaling mechanisms in the antimicrobial host defense of Drosophila. Curr. Opin. Microbial. 3, 16-22.
    • (2000) Curr. Opin. Microbial , vol.3 , pp. 16-22
    • Imler, J.-L.1    Hoffmann, J.R.2
  • 5
    • 0000631035 scopus 로고
    • The role of endotoxin in the extracellular coagulation of Limulus blood
    • Levin, J. and Bang, F.B. (1964) The role of endotoxin in the extracellular coagulation of Limulus blood. Bull. Johns Hopkins Hosp. 115, 265-274.
    • (1964) Bull. Johns Hopkins Hosp , vol.115 , pp. 265-274
    • Levin, J.1    Bang, F.B.2
  • 7
    • 0027279714 scopus 로고
    • Primitive coagulation systems and their message to modern biology
    • Iwanaga, S. (1993) Primitive coagulation systems and their message to modern biology. Thromb. Haemost. 70, 48-55.
    • (1993) Thromb. Haemost , vol.70 , pp. 48-55
    • Iwanaga, S.1
  • 8
    • 0027394999 scopus 로고
    • The limulus clotting reaction
    • Iwanaga, S. (1993) The limulus clotting reaction. Curr. Opin. Immunol. 5, 74-82.
    • (1993) Curr. Opin. Immunol , vol.5 , pp. 74-82
    • Iwanaga, S.1
  • 10
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga, S., Kawabata, S. and Muta, T. (1998) New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. (Tokyo) 123, 1-15.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 12
    • 0017855434 scopus 로고
    • Chromogenic substrates for horseshoe crab clotting enzyme. Its application for the assay of bacterial endotoxins
    • Iwanaga, S., Morita, T., Harada, T., Niwa, M., Takada, K., Kimura, T. and Sakakibara, S. (1978) Chromogenic substrates for horseshoe crab clotting enzyme. Its application for the assay of bacterial endotoxins. Haemostasis 7, 183-188.
    • (1978) Haemostasis , vol.7 , pp. 183-188
    • Iwanaga, S.1    Morita, T.2    Harada, T.3    Niwa, M.4    Takada, K.5    Kimura, T.6    Sakakibara, S.7
  • 13
    • 0026760884 scopus 로고
    • Molecular mechanism of hemolymph clotting system in Limulus
    • Iwanaga, S., Miyata, T. Tokunaga, F. and Muta, T. (1992) Molecular mechanism of hemolymph clotting system in Limulus. Thrombosis Res. 68, 1-32.
    • (1992) Thrombosis Res , vol.68 , pp. 1-32
    • Iwanaga, S.1    Miyata, T.2    Tokunaga, F.3    Muta, T.4
  • 14
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga, S. (2002) The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14, 87-95.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 15
    • 0032159526 scopus 로고    scopus 로고
    • Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab
    • Iwanaga, S. and Kawabata, S. (1998) Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab. Front. Biosci. 3, 973-984.
    • (1998) Front. Biosci , vol.3 , pp. 973-984
    • Iwanaga, S.1    Kawabata, S.2
  • 16
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta, T. and Iwanaga, S. (1996) The role of hemolymph coagulation in innate immunity. Curr. Opin. Immunol. 8, 41-47.
    • (1996) Curr. Opin. Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 17
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga, S. and Lee, B.L. (2005) Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 38, 128-150.
    • (2005) J. Biochem. Mol. Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 18
    • 0000929276 scopus 로고    scopus 로고
    • Clotting cascade and defense molecules found in the hemolymph of the horseshoe crab
    • eds. Söderhäll, K, Iwanaga, S. and Vasta, G, SOS Publication, Fair Haven, USA, pp
    • Kawabata, S., Muta, T. and Iwanaga, S. (1996) Clotting cascade and defense molecules found in the hemolymph of the horseshoe crab; in New Directions in Invertebrate Immunology (eds. Söderhäll, K., Iwanaga, S. and Vasta, G.). SOS Publication, Fair Haven, USA, pp. 255-283.
    • (1996) New Directions in Invertebrate Immunology , pp. 255-283
    • Kawabata, S.1    Muta, T.2    Iwanaga, S.3
  • 19
    • 3042523021 scopus 로고    scopus 로고
    • Structure and function of coagulogen, a clottable protein in horseshoe crabs
    • Osaki, T. and Kawabata, S. (2004) Structure and function of coagulogen, a clottable protein in horseshoe crabs. Cell Mol. Life Sci. (CMLS) 61, 1257-1265.
    • (2004) Cell Mol. Life Sci. (CMLS) , vol.61 , pp. 1257-1265
    • Osaki, T.1    Kawabata, S.2
  • 20
    • 0029692452 scopus 로고    scopus 로고
    • Clotting and immune defense in Limulidae
    • Muta, T. and Iwanaga, S. (1996) Clotting and immune defense in Limulidae. Prog. Mol. Subcell. Biol. 15, 154-189.
    • (1996) Prog. Mol. Subcell. Biol , vol.15 , pp. 154-189
    • Muta, T.1    Iwanaga, S.2
  • 21
    • 0033522446 scopus 로고    scopus 로고
    • Tachylectin-2: Crystal structure of a specific GlcNAc/GalNAc binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
    • Beisel, H.G., Kawabata, S., Iwanaga, S., Huber, R. and Bode, W. (1999) Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J. 18, 2313-2322.
    • (1999) EMBO J , vol.18 , pp. 2313-2322
    • Beisel, H.G.1    Kawabata, S.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 23
    • 0035923237 scopus 로고    scopus 로고
    • The 2.0Å crystal structure of tachylectin 5A provide evidence for the common origin of the innate immunity and the blood coagulation system
    • Kairies, N., Beisel, H.G., Fuentes-Prior, P., Tsuda, R., Muta, T., Iwanaga, S., Bode, W., Huber, R. and Kawabata, S. (2001) The 2.0Å crystal structure of tachylectin 5A provide evidence for the common origin of the innate immunity and the blood coagulation system. Proc. Natl. Acad. Sci. USA 98, 13519-13524.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13519-13524
    • Kairies, N.1    Beisel, H.G.2    Fuentes-Prior, P.3    Tsuda, R.4    Muta, T.5    Iwanaga, S.6    Bode, W.7    Huber, R.8    Kawabata, S.9
  • 25
    • 0032992548 scopus 로고    scopus 로고
    • Role of lectins in the innate immunity of horseshoe crab
    • Kawabata, S. and Iwanaga, S. (1999) Role of lectins in the innate immunity of horseshoe crab. Dev. Comp. Immunol. 23, 391-400.
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 391-400
    • Kawabata, S.1    Iwanaga, S.2
  • 27
    • 0034674709 scopus 로고    scopus 로고
    • Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif
    • Suetake, T., Tsuda, S., Kawabata, S., Miura, K., Iawnaga, S., Hikichi, K., Nitta, K. and Kawano, K. (2000) Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. J. Biol. Chem. 275, 17929-17932.
    • (2000) J. Biol. Chem , vol.275 , pp. 17929-17932
    • Suetake, T.1    Tsuda, S.2    Kawabata, S.3    Miura, K.4    Iawnaga, S.5    Hikichi, K.6    Nitta, K.7    Kawano, K.8
  • 28
    • 0028897416 scopus 로고
    • Purified horseshoe crab factor G. Reconstitution and characterization of the (1->3)-beta-D-glucan-sensitive serine protease cascade
    • Muta, T., Seki, N., Takaki, Y., Hashimoto, R., Oda, T., Iwanaga, A., Tokunaga, F. and Iwanaga, S. (1995) Purified horseshoe crab factor G. Reconstitution and characterization of the (1->3)-beta-D-glucan-sensitive serine protease cascade. J. Biol. Chem. 270, 892-897.
    • (1995) J. Biol. Chem , vol.270 , pp. 892-897
    • Muta, T.1    Seki, N.2    Takaki, Y.3    Hashimoto, R.4    Oda, T.5    Iwanaga, A.6    Tokunaga, F.7    Iwanaga, S.8
  • 29
    • 29244478349 scopus 로고    scopus 로고
    • Crystal structure of a clip-domain serine protease and functional roles of the clip domains
    • Piao, S., Song, Y.-L., Kim, J.H., Park, S.Y., Park, J.W., Lee, B.L., Oh, B.-H. and Ha, N.-C. (2005) Crystal structure of a clip-domain serine protease and functional roles of the clip domains. EMBO J. 24, 4404-4414.
    • (2005) EMBO J , vol.24 , pp. 4404-4414
    • Piao, S.1    Song, Y.-L.2    Kim, J.H.3    Park, S.Y.4    Park, J.W.5    Lee, B.L.6    Oh, B.-H.7    Ha, N.-C.8
  • 30
    • 0027445392 scopus 로고
    • Horseshoe crab transglutaminase
    • Tokunaga, F. and Iwanaga, S. (1993) Horseshoe crab transglutaminase. Methods Enzymol. 223, 378-388.
    • (1993) Methods Enzymol , vol.223 , pp. 378-388
    • Tokunaga, F.1    Iwanaga, S.2
  • 31
    • 0037131348 scopus 로고    scopus 로고
    • Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin
    • Osaki, T., Okino, N., Tokunaga, F., Iwanaga, S. and Kawabata, S. (2002) Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin. J. Biol. Chem. 277, 40084-40090.
    • (2002) J. Biol. Chem , vol.277 , pp. 40084-40090
    • Osaki, T.1    Okino, N.2    Tokunaga, F.3    Iwanaga, S.4    Kawabata, S.5
  • 33
    • 0030918084 scopus 로고    scopus 로고
    • Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain
    • Bergner, A., Muta, T., Iwanaga, S., Beisel, H.G., Delotto, R. and Bode, W. (1997) Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain. Biol. Chem. 378, 283-287.
    • (1997) Biol. Chem , vol.378 , pp. 283-287
    • Bergner, A.1    Muta, T.2    Iwanaga, S.3    Beisel, H.G.4    Delotto, R.5    Bode, W.6
  • 34
    • 0030462561 scopus 로고    scopus 로고
    • Crystal structure of a coagulogen, the clotting protein from horseshoe crab: A structural homologue of nerve growth factor
    • Bergner, A., Oganessyan, V., Muta, T., Iwanaga, S., Typke, D., Huber, R. and Bode, W. (1996) Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor. EMBO J. 15, 6789-6797.
    • (1996) EMBO J , vol.15 , pp. 6789-6797
    • Bergner, A.1    Oganessyan, V.2    Muta, T.3    Iwanaga, S.4    Typke, D.5    Huber, R.6    Bode, W.7
  • 35
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • Sugumaran, M. (2002) Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Prigment Cell Res. 15, 2-9.
    • (2002) Prigment Cell Res , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 36
    • 0034703094 scopus 로고    scopus 로고
    • A link between blood coagulation and prophenoloxidase activation in arthropod host defense
    • Nagai, T. and Kawabata, S. (2000) A link between blood coagulation and prophenoloxidase activation in arthropod host defense. J. Biol. Chem. 275, 29264-29267.
    • (2000) J. Biol. Chem , vol.275 , pp. 29264-29267
    • Nagai, T.1    Kawabata, S.2
  • 37
    • 0035920142 scopus 로고    scopus 로고
    • Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides
    • Nagai, T., Osaki, T. and Kawabata, S. (2001) Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J. Biol. Chem. 276, 27166-27170.
    • (2001) J. Biol. Chem , vol.276 , pp. 27166-27170
    • Nagai, T.1    Osaki, T.2    Kawabata, S.3
  • 38
    • 0034634579 scopus 로고    scopus 로고
    • Head-to-tail polymerization of coagulin, a clottable protein of the horseshoe crab
    • Kawasaki, H., Nose, T., Muta, T., Iwanaga, S., Shimohigashi, Y. and Kawabata, S. (2000) Head-to-tail polymerization of coagulin, a clottable protein of the horseshoe crab. J. Biol. Chem. 275, 35297-35301.
    • (2000) J. Biol. Chem , vol.275 , pp. 35297-35301
    • Kawasaki, H.1    Nose, T.2    Muta, T.3    Iwanaga, S.4    Shimohigashi, Y.5    Kawabata, S.6
  • 39
    • 0037134532 scopus 로고    scopus 로고
    • Duplicated binding sites for (1->3)-beta-D-glucan in the horseshoe crab coagulation factor G: Implications for a molecular basis of the pattern recognition in innate immunity
    • Takaki, Y., Seki, N., Kawabata, S., Iwanaga, S. and Muta, T. (2002) Duplicated binding sites for (1->3)-beta-D-glucan in the horseshoe crab coagulation factor G: Implications for a molecular basis of the pattern recognition in innate immunity. J. Biol. Chem. 277, 14281-14287.
    • (2002) J. Biol. Chem , vol.277 , pp. 14281-14287
    • Takaki, Y.1    Seki, N.2    Kawabata, S.3    Iwanaga, S.4    Muta, T.5
  • 41
    • 0029818516 scopus 로고    scopus 로고
    • Limulus intracellular coagulation inhibitor type 3. Purification, characterization, cDNA cloning, and tissue localization
    • Agarwara, K.L., Kawabata, S., Miura, Y., Kuroki, Y. and Iwanaga, S. (1996) Limulus intracellular coagulation inhibitor type 3. Purification, characterization, cDNA cloning, and tissue localization. J. Biol. Chem. 271, 23768-23774.
    • (1996) J. Biol. Chem , vol.271 , pp. 23768-23774
    • Agarwara, K.L.1    Kawabata, S.2    Miura, Y.3    Kuroki, Y.4    Iwanaga, S.5
  • 42
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost, M.R. (1999) Serine proteinase inhibitors in arthropod immunity. Dev. Comp. Immunol. 23, 291-301.
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 43
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune responses of a lepidopteran insect, Manuduca Sexta
    • Kanost, M.R., Jiang, H. and Yu, X.Q. (2004) Innate immune responses of a lepidopteran insect, Manuduca Sexta. Immunol Rev. 198, 97-105.
    • (2004) Immunol Rev , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.Q.3
  • 44
    • 0027364986 scopus 로고
    • Limulus test for detecting bacterial endotoxins
    • Tanaka, S. and Iwanaga, S. (1993) Limulus test for detecting bacterial endotoxins. Methods Enzymol. 223, 358-364.
    • (1993) Methods Enzymol , vol.223 , pp. 358-364
    • Tanaka, S.1    Iwanaga, S.2
  • 45
    • 0021811032 scopus 로고
    • A new chromogenic endotoxin-specific assay using recombined Limulus coagulation enzyme and its clinical application
    • Obayashi, T., Tamura, H., Tanaka, S., Ohki, M., Takahashi, M., Arai, M., Matsuda, M. and Kawai, T. (1985) A new chromogenic endotoxin-specific assay using recombined Limulus coagulation enzyme and its clinical application. Clin. Chim. Acta 149, 55-65.
    • (1985) Clin. Chim. Acta , vol.149 , pp. 55-65
    • Obayashi, T.1    Tamura, H.2    Tanaka, S.3    Ohki, M.4    Takahashi, M.5    Arai, M.6    Matsuda, M.7    Kawai, T.8
  • 46
    • 33646370200 scopus 로고    scopus 로고
    • Recognition of pathogens and activation of immunoresponses in Drosophila and horseshoe crab innate immunity
    • Kurata, S., Ariki, S. and Kawabata, S. (2006) Recognition of pathogens and activation of immunoresponses in Drosophila and horseshoe crab innate immunity. Immunobiology 211, 237-249.
    • (2006) Immunobiology , vol.211 , pp. 237-249
    • Kurata, S.1    Ariki, S.2    Kawabata, S.3
  • 47
    • 0742305683 scopus 로고    scopus 로고
    • A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides
    • Ariki, S., Koori, K., Osaki, T., Motoyama, K., Inamori, K. and Kawabata, S. (2004) A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides. Proc. Natl. Acad. Sci. USA 101, 953-958.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 953-958
    • Ariki, S.1    Koori, K.2    Osaki, T.3    Motoyama, K.4    Inamori, K.5    Kawabata, S.6
  • 48
    • 33947507505 scopus 로고    scopus 로고
    • A structural perspective on the interaction between lipopolysaccharide and factor C, a receptor involved in recognition of Gram-negative bacteria
    • Koshiba, T., Hashii, T. and Kawabata, S. (2007) A structural perspective on the interaction between lipopolysaccharide and factor C, a receptor involved in recognition of Gram-negative bacteria. J. Biol. Chem. 282, 3962-3967.
    • (2007) J. Biol. Chem , vol.282 , pp. 3962-3967
    • Koshiba, T.1    Hashii, T.2    Kawabata, S.3
  • 49
    • 0028278001 scopus 로고
    • Automated kinetic assay for endotoxin and (1→3)-β-D-glucan in human blood
    • Tamura, H., Arimoto, Y., Tanaka, S., Yoshida, M., Obayashi, T. and Kawai, T. (1994) Automated kinetic assay for endotoxin and (1→3)-β-D-glucan in human blood. Clin. Chim. Acta 226, 109-112.
    • (1994) Clin. Chim. Acta , vol.226 , pp. 109-112
    • Tamura, H.1    Arimoto, Y.2    Tanaka, S.3    Yoshida, M.4    Obayashi, T.5    Kawai, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.