I ) 自然免疫の分子機構の研究
I-1. Srimal, S., Miyata, T., Kawabata, S., and Iwanaga, S.: The complete amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Carcinoscorpius rotundicauda. J. Biochem.
98, 305-318 (1985).
I-2. Nakamura, T., Hirai, T., Tokunaga, F., Kawabata, S., and Iwanaga, S.: Purification and amino acid sequence of Kunitz-type protease inhibitor found in the hemocytes of horseshoe crab
(Tachypleus tridentatus). J. Biochem. 101, 1297-1306 (1987).
I-3. Miura, Y., Kawabata, S., and Iwanaga, S.: A limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily, purification, characterization, and cDNA cloning. J.
Biol. Chem. 269, 542-547 (1994).
I-4. Miura, Y., Kawabata, S., Wakamiya, Y., Nakamura, T., and Iwanaga, S.: A limulus intracellular coagulation inhibitor type 2. Purification, characterization, cDNA cloning, and tissue
localization. J. Biol. Chem. 270, 558-565 (1995).
I-5. Saito, T., Kawabata, S., Shigenaga, T., Cho, J., Nakajima, H., Hirata, M., Iwanaga, S.: A novel big defensin identified in horseshoe crab hemocytes. Isolation, amino acid sequence and
antibacterial activity. J. Biochem. 117, 1131-1137 (1995).
I-6. Lee, S. Y., Moon, H. J., Kawabata, S., Kurata, S., Natori, S., and Lee, B. L.: A sapecin homologue of Holotrichia diompalia: Purification, sequencing and determination of disulfide pairs.
Biol. Pharm. Bull. 18, 457-459 (1995).
I-7. Saito, T., Kawabata, S., Hirata, M., and Iwanaga, S.: A novel type of limulus lectin-L6. Purification, primary structure and antibacterial activity. J. Biol. Chem. 270, 14493-14499
(1995).
I-8. Okino, N., Kawabata, S., Saito, T., Hirata, M., Takagi, T., and Iwanaga, S.: Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J. Biol.
Chem. 270, 31008-31015 (1995).
I-9. Fujimoto, K., Okino, N., Kawabata, S., Iwanaga, S., and Ohnishi, E.: Nucleotide sequence of the cDNA encoding prophenoloxidase A1 of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 92,
7769-7773 (1995).
I-10. Lal Agarwala, K., Kawabata, S., Hirata, M., Miyagi, M., Tsunasawa, S., and Iwanaga, S.: A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes. Purification,
characterization, cDNA cloning and tissue localization. J. Biochem. 119, 85-94 (1996).
I-11. Kawabata, S., Saeki, K., and Iwanaga, S.: Limulus kexin: A new type of Kex2-like endoprotease specifically expressed in hemocytes of horseshoe crab. FEBS Lett. 386, 201-204 (1996).
I-12. Lal Agarwala, K., Kawabata, S., Miura, Y., Kuroki, Y., and Iwanaga, S.: Limulus intracellular coagulation inhibitor type 3. Purification, characterization, cDNA cloning, and tissue
localization. J. Biol. Chem. 271, 23768-23774 (1996).
I-13. Kawabata, S., Nagayama, R., Hirata, M., Shigenaga, T., Agarwala, K. L., Saito, T., Cho, J., Nakajima, H., and Iwanaga, S.: Tachycitin, a small granular component in horseshoe crab
hemocytes, is an antimicrobial protein with chitin-binding activity. J. Biochem. 120, 1253-1260 (1996).
I-14. Kawabata, S., Tokunaga, F., Kugi, Y., Motoyama, S., Miura, Y., Hirata, M., Iwanaga, S.: Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease
homologue with antimicrobial activity. FEBS Lett. 398, 146-150 (1996).
I-15. Iwaki, D., Kawabata, S., Miura, Y., Kato, A., Armstrong, P. B., Quigley, J. P., Nielsen, K. L., Dolmer, K., Sottrup-Jensen, L., and Iwanaga, S.: Molecular cloning of limulus
a2-macroglobulin. Eur. J. Biochem. 242, 822-831 (1996).
I-16. Kawabata, S., Saito, T., Saeki, K., Okino, N., Mizutani, A., Toh, Y., and Iwanaga, S: cDNA cloning, tissue distribution, and subcellular localization of horseshoe crab big defensin. Biol.
Chem. 378, 289-292 (1997).
I-17. Kwon, T. H., Lee, S. Y., Lee, J. H., Choi, J. S., Kawabata, S., Iwanaga, S., and Lee, B.L.: Purification and characterization of prophenoloxidase from the hemolymph of coleopteran insect,
Holotrichia diomphalia larvae. Mol. Cells. 7, 90-97 (1997).
I-18. Saito, T., Hatada, M., Iwanaga, S., and Kawabata, S.: A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J. Biol. Chem. 272,
30703-30708 (1997).
I-19. Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S., Iwanaga, S., Lee, B. L.: In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors
isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. Eur. J. Biochem. 254, 50-57 (1998).
I-20. Lee, S.Y., Cho, M. Y., Hyun, J. H., Lee, K. M., Homma, K., Natori, S., Kawabata, S., Iwanaga, S., Lee, B.L.: Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine
protease, is induced by lipopolysaccharide or 1,3-b-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur. J. Biochem. 257, 615-621 (1998).
I-21. Koo, J. C., Lee, S. Y., Chun, H. J., Cheong, Y. H., Choi, J. S., Kawabata, S., Miyagi, M, Tsunasawa, S., Ha, K. S., Bae, D. W., Han, C. D., Lee, B. L., and Cho, M. J.: Two hevein homologs
isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1382, 80-90 (1998).
I-22. Inamori, K., Saito, T., Iwaki, D., Nagira, T., Iwanaga, S., Arisaka, F., and Kawabata, S.: A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes
specific O-antigens of bacterial lipopolysaccharides. J. Biol. Chem. 274, 3272-3278 (1999).
I-23. Beisel, H.-G., Kawabata, S., Iwanaga, S., Huber, R., and Bode, W.: 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).
I-24. Iwaki, D., Osaki, T., Yoshimitsu, M., Wai, S. N., Iwanaga, S., and Kawabata, S.: Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma.
Eur. J. Biochem. 264, 314-326 (1999).
I-25. Gokudan, S., Muta, T., Tsuda, R., Koori, K., Kawahara, T., Seki, N., Mizunoe, Y., Wai, S. N., Iwanaga, S., and Kawabata, S.: Horseshoe crab acetyl group-recognizing lectins involved in
innate immunity are structurally related to fibrinogen. Proc. Natl. Acad. Sci. USA 96, 10086-10091 (1999).
I-26. Osaki, T., Omotezako, M., Nagayama, R., Hirata, M., Iwanaga, S., Kasahara, J., Hattori, J., Ito, I., Sugiyama, H., and Kawabata, S.: Horseshoe crab hemocyte-derived antimicrobial
polypeptides, tachystatins, with sequence similarity to spider neurotoxins. J. Biol. Chem. 274, 26172-26178 (1999).
I-27. Nagai, T., Kawabata, S., Shishikura, F., and Sugita, H.: Purification, characterization, and amino acid sequence of an embryonic lectin in perivitelline fluid of the horseshoe crab. J.
Biol. Chem. 274, 37673-37678 (1999).
I-28. Suetake, T., Tsuda, S., Kawabata, S., Miura, K., Iwanaga, S., Hikichi, K., Nitta, K., and Kawano, K.: Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding
structural motif. J. Biol. Chem. 275, 17929-17932 (2000).
I-29. Lee, K. M., Lee, K. Y, Choi, H. W., Cho, M. Y., Kwon, T. H., Kawabata, S., and Lee, B. L.: Activated phenoloxidase from Tenebrio molitor larvae enhances the synthesis of melanin by using a
vitellogenin-like protein in the presence of dopamine. Eur. J. Biochem. 267, 3695-3703 (2000).
I-30. Nagai, T., and Kawabata, S.: A link between blood coagulation and prophenoloxidase activation in arthropod host defense. J. Biol. Chem. 275, 29264-29267 (2000).
I-31. Kawasaki, H., Nose, T., Muta, T., Iwanaga, S., Shimohigashi, Y., and Kawabata, S.: Head-to-tail polymerization of coagulogen, a clottable protein of the horseshoe crab. J. Biol. Chem. 275,
35297-35301 (2000).
I-32. Nagai, T., Osaki, T., and Kawabata, S.: Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J. Biol. Chem. 276, 27166-27170 (2001).
I-33. Kairies, N., Beisel, H.-G., Fuentes-Prior, P., Tsuda, R., Muta, T., Iwanaga, S., Bode, W., Huber, R., and Kawabata, S.: The 2.0-Å crystal structure of tachylectin 5 provides evidence for
the common origin of the innate immunity and the blood coagulation systems. Proc. Natl. Acad. Sci. USA 98, 13519-13524 (2001).
I-34. Takaki, Y., Seki, N., Kawabata, S., Iwanaga, S., and Muta, T.: Duplicated binding site for 1,3-b-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).
I-35. Kakiuchi, M., Okino, N., Sueyoshi, N., Ichinose, S., Omori, A., Kawabata, S., Yamaguchi, K., and Ito, M.: Purification, characterization, and cDNA cloning of
a-N-acetylgalactosamine-specific lectin from starfish, Asterina pectinifera. Glycobiology, 12, 85-94 (2002).
I-36. Fujitani, N., Kawabata, S., Osaki, T., Kumaki, Y., Demura, M., Nitta, K., and Kawano, K.: Structure of the antimicrobial peptide tachystatin A. J. Biol. Chem. 277, 23651-23657 (2002).
I-37. Lee, K. Y., Zhang, R., Kim, M. S., Park, J. W., Kawabata, S., and Lee, B. L.: A zymogen form of masquerade-like serine protease homologue is cleaved during pro-phenoloxidase activation by
Ca2+ in coleopteran and Tenebrio molitor larvae. Eur. J. Biochem. 269, 4375-4383 (2002).
I-38. Gregorio, E. D., Han, S-J., Lee, W.-J., Baek, M.-J., Osaki, T., Kawabata, S., Lee, B. L., Iwanaga, S. Lemaitre, B., and Brey, P. T.: An immune responsive serpin regulates the melanization
cascade in Drosophila. Develop. Cell 3, 581-592 (2002).
I-39. Osaki, T., Okino, N., Tokunaga, F., Iwanaga, S., and Kawabata, S.: 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).
I-40. Suetake, T., Aizawa, T., Koganesawa, N., Osaki, T., Kobashigawa, Y., Demura, T., Kawabata, S., Kawano, K., Tsuda, S., and Nitta, K.: Production and characterization of recombinant
tachycitin, the chitin-binding protein. Protein Engineering, 15, 763-769 (2002).
I-41. Zhang, R., Cho, H. Y., Kim, H. S., Ma, Y. G., Osaki, T., Kawabata, S.,Söderhäll, K., and Lee, B. L.: Characterization and properties of a 1,3--b-D-glucan pattern recognition protein of
Tenebrio molitor larvae which is specifically degraded by serine protease during prophenoloxidase activation. J. Biol. Chem. 278, 42072-42079 (2003).
I-42. Zhang, R., Cho, H. Y., Kim, H. S., Ma, Y., Söderhäll, K., and Lee, B. L.: Characterization and properties of a 1, 3-b-D-glucan-dependent prophenoloxidase activation system of insect. J.
Biol. Chem. 279, 3218-3227 (2004).
I-43. Ariki, S., Koori, K., Osaki, T., Motoyama, K., Inamori, K., and Kawabata, S.: A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides. Proc. Natl.
Acad. Sci. USA. 101, 953-958 (2004).
I-44. Ozaki, A., Ariki, S., and Kawabata, S.: An antimicrobial peptide tachyplesin acts as a secondary secretagogue and amplifies lipopolysaccharide-induced hemocyte exocytosis. FEBS J. 272,
3863-3871 (2005).
I-45. Iijima, M., Hashimoto, T., Matsuda, Y., Nagai, T., Yamano, Y., Ichi, T., Osaki, T., and Kawabata, S.: Comprehensive sequence analysis of horseshoe crab cuticular proteins and their
involvement in transglutaminase-dependent cross-linking. FEBS J. 272, 4774-4786 (2005).
I-46. Koshiba, T., Hashii, T., and Kawabata, S.: 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).
I-47. Fujitani, N., Kouno, T., Nakahara, T., Takaya, K., Osaki, T., Kawabata, S., Mizuguchi, M., Aizawa, T., Demura, M., Nishimura, S., and Kawano, K.: The solution structure of horseshoe crab
antimicrobial peptide tachystatin B with an inhibitory cysteine-knot motif. J. Pept. Sci. 13, 269-279 (2007).
I-48. Matsuda, Y., Osaki, T., Hashii, T., Koshiba, T., and Kawabata, S.: A cysteine-rich protein from an arthropod stabilizes clotting mesh and immobilizes bacteria at injured sites. J. Biol.
Chem. 282, 33543-33552 (2007)
I-49. Matsuda, Y., Koshiba, T., Osaki, T., Suyama, H., Arisaka, F., Toh, Y., and Kawabata, S.: An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent
mesh. J. Biol. Chem. 282, 37316-37324 (2007).
I-50. Kouno, T., Fujitani, N., Mizuguchi, M., Osaki, T., Nishimura, S., Kawabata, S., Aizawa, T., Demura, M., Nitta, K., and Kawano, K.: A novel beta-defensin structure: a potential strategy of
big defensin to overcome resistance by Gram-positive bacteria. Biochemistry 47, 10611-10619 (2008).
I-51. Ariki, S., Takahara, S., Shibata, T., Fukuoka, T., Ozaki, A., Endo, Y., Fujita, T., Koshiba, T., and Kawabata, S.: Factor C acts as a lipopolysaccharide-responsive C3 convertase in
horseshoe crab complement activation. J. Immunol. 181, 7794-8001 (2008).
I-52. Yasukawa, K., Oshiumi, H., Takeda, M., Ishihara, N., Yanagai, Y., Seya, T., Kawabata, S., and Koshiba, T.: Mitofusin 2 inhibits mitochondorial antiviral signaling. Science Signaling 2, ra47
(2009).
I-53. Ueda, Y., Ohwada, S., Abe, Y., Shibata, T., Iijima, M., Yoshimitsu, Y., Koshiba, T., Nakata, M., Ueda, T., and Kawabata, S.: Factor G utilizes a carbohydrate-binding cleft that is conserved
between horseshoe crab and bacteria for the recognition of β-1,3-D-glucans. J. Immunol. 183, 3810-3818 (2009).
I-54. Shibata, T., Ariki, S., Shinzawa, N., Miyaji, R., Suyama, H., Sako, M., Inomata, N., Koshiba, T., Kanuka, H., and Kawabata, S.: Protein crosslinking by transglutaminase controls cuticle
morphogenesis in Drosophila. PLoS ONE 5, e13477. (2010). (doi: 10.1371/journal.pone.0013477).
I-55. Koshiba, T., Holman, H. A., Kubara, K., Yasukawa, K., Kawabata, S., Okamoto, K., Macfarlane, and Shaw, J. M.: Structure-function analysis of the yeast Miro GTPase, Gem1p: implications for
mitochondrial inheritance. J. Biol. Chem. 286, 354-362 (2011). (doi: 10.1074/jbc.M110.180034)
I-56. Haipeng, L., Wu, C., Matsuda, Y., Kawabata, S., Lee, B. L., Söderhäll, K., and Söderhäll, I.: Peptidoglycan activation of the proPO-system without a peptidoglycan receptor protein (PGRP)?
Dev. Comp. Immunol. 35, 51-61 (2011).
I-57. Koshiba, T., Yasukawa, K., Yanagi, Y., and Kawabata, S.: Mitochondrial membrane potential is involved in the MAVS-mediated antiviral signaling. Science Signaling, 4, ra7 (2011).
(doi:10.1126/scisignal.2001147).
I-58. Tagawa, K., Yoshihara, Y., Shibata, T., Kitazaki, K., Endo, Y., Fujita, T., Koshiba, T., and Kawabata, S.: Microbe-specific C3b deposition in the horseshoe crab complement system in a
C2/factor B-dependent or -independent manner. PLoS ONE 7, e36783 (2012). (doi: 10.1371/journal.pone.0036783).
I-59. Sasaki, O., Yoshizumi, T., Kuboyama, M., Ishihara, T., Suzuki, E., Kawabata, S., and Koshiba, T.: A structural perspective of the MAVS-regulatory mechanism on the mitochondrial outer
membrane using bioluminescence resonance energy transfer. Biochim. Biophys. Acta, 1833, 1017-1027 (2012).
I-60. Shibata, T., Sekihara, S., Fujikawa, T., Miyaji, R., Maki, K., Ishihara, T., Koshiba, T., and Kawabata, S.: Transglutaminase-catalyzed protein-protein cross-linking suppresses the activity
of the NF-κB-like transcription factor Relish. Science Signaling, 6, ra61 (2013). (doi:10.1126/scisignal.2003970)
I-61. Yoshizumi, T., Ichinohe T., Sasaki, O., Otera, H., Kawabata, S., Mihara, K., and Koshiba, T.: Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs
innate immunity. Nat. Communications 5, 4713- (2014).
I-62. Kobayashi, Y., Shiga, T., Shibata, T., Sako, M., Maenaka, K., Koshiba, T., Mizumura, H., Oda, T., and Kawabata, S.: The N-terminal Arg residue is essential for autocatalytic activation of a
lipopolysaccharide-responsive protease zymogen. J. Biol. Chem., 289, 25987-25995 (2014). (doi: 10.1074/jbc.M114.586933).
I-63. Kobayashi, Y., Takahashi, T., Shibata, T., Ikeda, S., Koshiba, T., Mizumura, H., Oda, T., and Kawabata, S.: Factor B is the second lipopolysaccharide-binding protease zymogen in the
horseshoe crab coagulation cascade. J. Biol. Chem. 290, 19379-19386 (2015). (doi:10.1074/jbc.M115.653196).
I-64. Shibata, T., Maki, K., Hadano, J., Fujikawa, T., Kitazaki, K., Koshiba, T., and Kawabata, S.: Crosslinking of a peritrophic matrix protein protects gut epithelia from bacterial exotoxins.
PLoS Pathog. 11, e1005244 (2015). (doi: 10.1371/journal.ppat.1005244).
I-65. Sekihara, S., Shibata, T., Hyakkendani, M., and Kawabata, S.: RNA interference directed against the transglutaminase gene triggers dysbiosis of gut microbiota in Drosophila. J. Biol. Chem.
291, 25077-25087 (2016). (doi:10.1074/jbc.M116.761791)
I-66. Mizumura, H., Ogura, N., Aketagawa, J., Aizawa, M., Kobayashi, Y., Kawabata, S., and Oda, T.: Genetic engineering approach to develop next-generation reagents for endotoxin quantification.
Innate Immunity 23, 136-146 (2017). (doi: 10.1177/1753425916681074).
I-67. Maki, K., Shibata, T., and Kawabata, S. Transglutaminase-catalyzed incorporation of polyamines masks the DNA-binding region of the transcription factor relish. J. Biol. Chem., 292,
6369-6380 (2017). (doi:10.1074/jbc.M117.779579).
I-68. Shibata, T., Hadano, J., Kawasaki, D., Dong, X., and Kawabata, S.: Drosophila TG-A transglutaminase is secreted via an unconventional Golgi-independent mechanism involving exosomes and two
types of fatty acylations. J. Biol. Chem., 292, 10723-10734 (2017). (doi: 10.1074/jbc.M117.779710). *This article was selected to appear in a special virtual issue on "Extracellular vesicles" at
JBC, published in June 2019 assembled by Phyllis Hanson.
I-69. Shibata, T., Kobayashi, Y., Ikeda, Y., and Kawabata, S.: Intermolecular autocatalytic activation of serine protease zymogen factor C through an active transition state responding to
lipopolysaccharide. J. Biol. Chem. 293, 11589-11599 (2018). (doi: 10.1074/jbc. RA118.002311).
I-70. Yamashita, K., Shibata, T., Takahashi, T., Kobayashi, Y., and Kawabata, S.: Roles of the clip domains of two protease zymogens in the coagulation cascade in horseshoe crabs. J. Biol. Chem.
295, 8857-8866 (2020). (doi: 10.1074/jbc. RA119.012452)
I-71. Yamashita, K., Takeshita, N., Arita, A., Shibata, T., Kobayashi, Y., and Kawabata, S.: A mutant equipped with a regenerated disulfide for the missing His loop of a serine protease zymogen
in the horseshoe crab coagulation cascade. J. Biochem. 170, 489-500 (2021). (doi: 10.1093/jb/mvab064)
I-72. Yamashita, K., Takahashi, D., Yamamoto, Y., Kiyomoto, S., Shibata, T., and Kawabata, S.: Effects of Ca2+ ions on the horseshoe crab coagulation cascade triggered by lipopolysaccharide.
J. Biochem. 173, 47-58 (2023). (doi: 10.1093/jb/mvad018)
II ) スタフィロコアグラーゼの構造と機能の研究
II-1. Kawabata, S., Morita, T., Iwanaga, S., and Igarashi, H.: Staphylocoagulase-binding region in human prothrombin. J. Biochem. 97, 325-331 (1985).
II-2. Kawabata, S., Morita, T., Iwanaga, S., and Igarashi, H.: Difference in enzymatic properties between a-thrombin and staphylocoagulase complex and free a-thrombin. J. Biochem. 97, 1073-1078
(1985).
II-3. Kawabata, S., Morita, T., Iwanaga, S., and Igarashi, H.: Enzymatic properties of staphylothrombin, an active molecular complex formed between staphylocoagulase and prothrombin. J. Biochem.
98, 1603-1614 (1985).
II-4. Kawabata, S., Miyata, T., Morita, T., Miyata, T., Iwanaga, S., and Igarashi, H.: The amino acid sequence of the procoagulant- and prothrombin-binding domain isolated from staphylocoagulase.
J. Biol. Chem. 261, 527-531 (1986).
II-5. Kawabata, S., Morita, T., Miyata, T., Iwanaga, S., and Igarashi, H.: Isolation and characterization of staphylocoagulase chymotryptic fragment. Localization of the procoagulant- and
prothrombin-binding domain of this protein. J. Biol. Chem. 261, 1427-1433 (1986).
II-6. Kaida, S., Miyata, T., Yoshizawa, Y., Kawabata, S., Morita, T., Igarashi, H., and Iwanaga, S.: Nucleotide sequence of the staphylocoagulase gene. Its unique COOH-terminal 8 tandem repeats.
J. Biochem. 102, 1177-1186 (1987).
II-7. Friedrich, R., Panizzi, P., Fuentes-Prior, P., Richer, K., Verhmme, I., Anderson P. J., Kawabata, S., Huber, R., Bode, W., and Bock, P. E.: Staphylocoagulase is a prototype for the
mechanism of cofactor-induced zymogen activation. Nature 425, 535-539 (2003).
II-8. Friedrich, R., Bode, W R., Panizzi, P., I., Kawabata, S., Bock, P. E., and Fuentes-Prior, P.: Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation. J. Biol.
Chem. 281, 1188-1195 (2006).
III) 哺乳類血液凝固因子の構造と機能の研究
III-1. Morita, T., Mizuguchi, J., Kawabata, S., Iwanaga, S.: Proteolytic cleavage of vitamin K-dependent bovine plasma protein S by a-thrombin and plasma serine protease. J. Biochem. 99, 561-568
(1986).
III-2. Kawabata, S., Miura, T., Morita, T., Kato, H., Fujikawa, K., Iwanaga, S., Takada, K., Kimura, T., and Sakakibara, S.: Highly sensitive peptide-4-methylcoumaryl-7-amide substrates for
blood-clotting proteases and trypsin. Eur. J. Biochem. 172, 17-25 (1988).
III-3. Takeya, H., Kawabata, S., Nakagawa, K., Yamamichi, Y., Miyata, T., Iwanaga, S., Takao, T., and Shimonishi, Y.: Bovine factor VII. Its purification and complete amino acid sequence. J.
Biol. Chem. 263, 14868-14877 (1988).
III-4. Morita, T., Kaetsu, H., Mizuguchi, J., Kawabata, S., and Iwanaga, S.: A characteristic property of vitamin K-dependent plasma protein Z. J. Biochem. 104, 368-374 (1988).
III-5. Shieh, T. C., Kawabata, S., Kihara, H., Ohno, M., and Iwanaga, S.: Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom. J. Biochem. 103, 596-605
(1988).
III-6. Higashi, S., Kawabata, S., Nishimura, H., Funakoshi, H., Ohyama, S., Miyamoto, S., Funatsu, A., and Iwanaga, S.: Monoclonal antibody (VII-M31) to bovine factor VII. A specific epitope in
the g-carboxyglutamic acid domain. J. Biochem. 108, 645-662 (1990).
III-7. Nishida, S., Fujita, T., Kohno, N., Atoda, H., Morita, T., Takeya, H., Kido, I., Paine, M. J. I., Kawabata, S., and Iwanaga, S.: cDNA cloning and deduced amino acid sequence of prothrombin
activator (ecarin) from Kenyan Echis carinatus venom. Biochemistry 34, 1771-1778 (1995).
IV) 哺乳類血液凝固因子に見い出された新しいオリゴ糖鎖の研究
IV-1. Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T.: A new trisaccharide sugar chain linked to a serine
residue in bovine blood coagulation factors VII and IX. J. Biochem. 104, 867-868 (1988).
IV-2. Nishimura, H., Kawabata, S., Kisiel, W., Hase, S., Ikenaka, T., Takao, T., Shimonishi, Y., and Iwanaga, S.: Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)
O-glycocidically linked to a serine residue in the first epidermal growth factor-like domain of human factor VII and IX and protein Z and bovine protein Z. J. Biol. Chem. 264, 20320-20325
(1989).
IV-3. Hase, S., Nishimura, H., Kawabata, S., Iwanaga, S., and Ikenaka, T.: The structure of (xylose)2 glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood
clotting factor IX. J. Biol. Chem. 265, 1858-1861 (1990).
IV-4. Lal Agarwala, K., Kawabata, S., Takao, T., Murata, H., Shimonishi, Y., Nishimura, H., and Iwanaga, S.: Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to
threonine residues at 159 and 169. Biochemistry 33, 5167-5171 (1994).
V) ヒト血液凝固因子の分子異常症の研究
V-1. Sugimoto, M., Miyata, T., Kawabata, S., Yoshioka, A., Fukui, H., Takahashi, H., and Iwanaga, S.: Blood clotting factor IX Niigata. Substitution of alanine-390 by valine in the catalytic
domain. J. Biochem. 104, 878-880 (1988).
V-2. Miyata, T., Kawabata, S., Iwanaga, S., Takahashi, I., Alving, B., and Saito, H.: Coagulation factor XII (Hageman factor) Washington D.C. Inactive factor XIIa results from Cys 571-Ser
substitution. Proc. Natl. Acad. Sci. USA 86, 8319-8322 (1989).
V-3. Suehiro, K., Kawabata, S., Miyata, T., Takeya, H., Takamatsu, J., Ogata, K., Kamiya, T., Saito, H., Niho, Y., and Iwanaga, S.: Blood clotting factor IX Bm Nagoya. Substitution of arginine
180 by tryptophan and its activation by a-chymotrypsin and rat mast cell chymase. J. Biol. Chem. 264, 21257-21265 (1989).
V-4. Sugimoto, M., Miyata, T., Kawabata, S., Yoshioka, A., Fukui, H., and Iwanaga, S.: Factor IX Kawachinagano. Impaired function of the Gla-domain caused by attached propeptide region due to
substitution of arginine by glutamine at position -4. Br. J. Haematology 72, 216-221 (1989).
V-5. Kamura, T., Tsuda, H., Yae, Y., Hattori, S., Ohaga, S., Shibata, Y., Kawabata, S., and Hamasaki, N.: An abnormal fibrinogen Fukuoka II (Gly-Bb15-Cys) characterized by defective fibrin
lateral association and mixed disulfide formation. J. Biol. Chem. 270, 29392-29399 (1995)
VI) 哺乳類の新規メタルエンドペプチダーゼの研究
VI-1. Kawabata, S. and Davie, E. W.: A microsomal endopeptidase from liver with substrate specificity for processing proproteins such as the vitamin K-dependent proteins of plasma. J. Biol. Chem.
267, 10331-10336 (1992).
VI-2. Kawabata, S., Nakagawa K., Muta, T., Iwanaga, S., and Davie, E. W.: Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to
rat testes metalloendopeptidase 24.15. J. Biol. Chem. 268, 12498-12503 (1993).
VI-3. Kojima, N., Kawabata, S., Makinose, Y., Nishino, N., and Iwanaga, S.: Substrate specificity of rabbit liver metalloendopeptidase and its new fluorogenic peptide substrates. J. Biochem. 118,
855-861 (1995).
VI-4. Nakagawa, K., Kawabata, S., Iwanaga, S., and Sueishi, K.: Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase. J. Histochem. Cytochem.45, 41-47
(1997).
VII) その他の共同研究
VII-1. Igarashi, H., Fujikawa, H., Usami, H., Kawabata, S., and Morita, T.: Purification and characterization of Staphylococcus aureus FRI 1169 and 587 toxic shock syndrome exotoxins. Infect.
Immun. 44, 175-181 (1984).
VII-2. Nakabeppu, Y., Kondo, H., Kawabata, S., Iwanaga, S., and Sekiguchi, M.: Purification and structure of the intact Ada regulatory protein of Escherichia coli K12, O6-methylguanine-DNA
methyltransferase. J. Biol. Chem. 260, 7281-7288 (1985).
VII-3. Sakumi, K., Nakabeppu, Y., Yamamoto, Y., Kawabata, S., Iwanaga, S., and Sekiguchi, M.: Purification and structure of 3-methyladenine-DNA glycosylase I of Escherichia coli. J. Biol. Chem.
261, 15761-15766 (1986).
VII-4. Kondo, H., Nakabeppu, Y., Kataoka, H., Kuhara, S., Kawabata, S., and Sekiguchi, M.: Structure and expression of the alkB gene of Escherichia coli related to the repair of alkylated DNA. J.
Biol. Chem. 261, 15772-15777 (1986).
VII-5. Matsumoto, T., Emi, Y., Kawabata, S., and Omura, T.: Purification and characterization of three male-specific and one female-specific forms of cytochrome P-450 from rat liver microsomes.
J. Biochem. 100, 1359-1371 (1986).
VII-6. Kini, M., R., Kawabata, S., and Iwanaga, S.: Comparison of amino terminal region of three isoenzymes of phospholipase A2 (TFV Pl-Ia, TFV-Ib, TFV PL-X) from Trimeresurus flavoviridis (Habu
snake) venom and the complete amino acid sequence of the basic phospholipase, TFV PL-X. Toxicon 24, 1117-1129 (1986).
VII-7. Tamura, M., Yubisui, T., Takeshita, M., Kawabata, S., Miyata, T., and Iwanaga, S.: Structure comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC
mapping. J. Biochem. 101, 1147-1159 (1987).
VII-8. Jingushi, S., Mitsuyama, M., Moriya, T., Kawabata, S., Iwanaga, S., and Amako, K.: Antigenic determinant on fimbriae of Serratia marcescens US5 analyzed using monoclonal antibodies.
Microbiol. Immunol. 31, 876-889 (1987).
VII-9. Hashimoto, T., Matsumoto, T., Nishizawa, M., Kawabata, S., Morohashi, K., Handa, S., and Omura, T.: A mutant rat strain deficient in induction of a phenobarbital-inducible form of
cytochrome P-450 in liver microsomes. J. Biochem. 103, 487-492 (1988).
VII-10. Mizunoe, Y., Nakabeppu, Y., Sekiguchi, M., Kawabata, S., Moriya, T., and Amako, K.: Cloning and sequence of the gene coding the major structural component of mannose-resistant fimbriae of
Serratia marcescens. J. Bacteriol. 170, 3567-3574 (1988).
VII-11. Takagi, Y., Morohashi, K., Kawabata, S., Go, M., and Omura, T.: Molecular cloning and nucleotide sequence of cDNA of microsomal carboxyesterase E1 of rat liver. J. Biochem. 104, 801-806
(1988).
VII-12. Moriya, T., Kawabata, S., Mizunoe, Y., and Amako, K.: A cryptic fimbrial gene in Serratia marcescens. J. Bacteriology, 171, 6629-6636 (1989).
VII-13. Ishihara, S., Morohashi, K., Sadano, H., Kawabata, S., Gotoh, O., and Omura, T.: Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450. J. Biochem. 108,
899-902 (1990).
VII-14. Ikura, T., Go, N., Kohda, D., Inagaki, F., Yanagawa, H., Kawabata, M., Kawabata, S., Iwanaga, S., Noguti, T., and Go, M.: Secondary structural features of modules M2 and M3 of barnase in
solution by NMR experiment and distance geometry calculation. Proteins 16, 341-356 (1993).
VII-15. Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., Kawabata, S., Maki, H., and Sekiguchi, M.: Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-Oxo-dGTP, a mutagenic
substrate for DNA synthesis. J. Biol. Chem. 268, 23524-23530 (1993).
VII-16. Kusumi, K., Inada, H., Kawabata, S., Iba, K., and Nishimura, M.: Chlorophyll deficiency caused by a specific blockage of the C5-pathway in seedlings of virescent mutant rice. Plant Cell
Phytsiol. 35, 445-449 (1994).
VII-17. Alam, R., Hachiya, N., Sakaguchi, M., Kawabata, S., Iwanaga, S., Kitajima, M., Mihara, K., and Omura, T.: cDNA cloning and characterization of mitochondorial import stimulation factor
(MSF) purified from rat liver cytosol. J. Biochem. 116, 416-425 (1994).
VII-18. Fernando, M. R., Sumimoto, H., Nanri, H., Kawabata, S., Iwanaga, S., Minakami, S., Fukumaki, Y., and Takeshige, K.: Cloning and sequencing of the cDNA encoding human glutaredoxin.
Biochim. Biophys. Acta 1218, 229-231 (1994).
VII-19. Wang, L., Rahman, M. M., Iida, H., Inai, T., Kawabata, S., Iwanaga, S., and Shibata, Y.: Annexin V is located in association with Z-line of rat cardiac myocytes. Cardiovasc. Res. 30,
363-371 (1995).
VII-20. Wai, N. S., Mizunoe, Y., Takade, A., Kawabata, S., and Yoshida, S.: Vibrio cholerae O1 Strain TSI-4 produces the exopolysaccharide materials that determine colony morphology, stress
resistance, and biofilm formation. Appl. Environ. Microbiol. 64, 3648-3655 (1998).
VII-21. Hayashi, T., Takeshita, K., Tsuchida, N., Kitano, K., Kawabata, S., Iwanaga, S., and Ito, T.: Purification of a novel muscle cell growth factor S-myotrophin from porcine skeletal muscle.
International J. Bichem. Cell Biol. 30, 897-908 (1998).
VII-22. Mizunoe, Y., Wai, S. N., Umene, K., Kokubo, T., Kawabata, S., and Yoshida, S.: Cloning, sequencing, and functional expression in Escherichia coli of chaperonin (groESL) genes from Vibrio
cholerae. Microbiol. Immunol. 43, 513-520 (1999).
VII-23. Matsuda, Y., Inamori, K., Osaki, T., Eguchi, A., Watanabe, A., Kawabata, S., Iba, K., and Arata, H.: Nitric oxide-reductase homologue that contains a copper atom and has cytochrome
c-oxidase activity from an aerobic phototrophic bacterium Roseobacter denitrificans. J. Biochem. 131, 791-800 (2002).
VII-24. Ishikawa, T., Mizunoe, Y., Kawabata, S., Takade, A., Harada, M., Wai, S.-N., and Yoshida, S.: The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter
jejuni. J. Bacteriol. 185, 1010-1017 (2003).
VII-25. Oba, Y., Shimasaki, Y., Oshima, Y., Satone, H., Kitano, T., Nakao, M., Kawabata, S., and Honjo, T.: Purification and characterization of Tributyltin-binding protein type 2 from plasma of
Japanese flounder, Paralichthys olivaceus. J. Biochem. 142, 229-238 (2007).
VII-26. Matsushima, A., Kakuta, Y., Teramoto, T., Koshiba, T., Liu, X., Okada, H., Tokunaga, T., Kawabata, S., Kimura, M., and Shimohigashi, Y.: Structural evidence for endocrine disruptor
bisphenol A binding to human nuclear receptor ERR. J. Biochem. 142, 517-524 (2007).
VII-27. Satone, H., Oshima, Y., Shimasakai, Y., Tawaratsumita, T., Oba, Y., Takahashi, E., Kitanao, T., Kawabata, S., Kakuta, Y., and Honjo, T.: Tributyltin-binding protein type 1 has a
distinctive lipocalin-like structure and is involved in the excretion of tributyltin in Japanese flounder, Paralichthys olivaceus. Aquatic Toxicol. 90, 292-299 (2008).
VII-28. Oba, Y., Yamauchi, A., Hashiguchi, Y., Satone, H., Miki, S., Nassef, M., Shimasaki, Y., Kitano, T., Nakao, M., Kawabata, S., Honjo, T., and Oshima, Y. Purification and characterization of
tributyltin-binding protein of tiger puffer, Takifugu rubripes. Comp. Biochem. Physiol. Part C 153, 17-23 (2011).
VII-29. Satone, H., Nonaka, S., Lee, J. M., Shimasaki, Y., Kusakabe, T., Kawabata, S., and Oshima, Y.: Tetrodotoxin- and tributyltin-binding abilities of recombinant pufferfish saxitoxin and
tetrodotoxin binding proteins of Takifugu rubripes. Toxicon 125, 50-52 (2017).
VII-30. Lee, S. A., Jang, S. H., Kim, B. H., Shibata, T., Kawabata, S., and Lee, B. L.: Insecticidal activity of the metalloprotease AprA occurs through suppression of host cellular and humoral
immunity. Dev. Comp. Immunol. 81, 116-126 (2018).
VII-31. Ito, D., Kawamura, H., Oikawa, A., Ihara, Y., Shibata, T., Nakamura, N., Asano, T., Kawabata, S., Suzuki, T., and Masuda, S. ppGpp functions as an alarmone in metazoan. Commun. Biol. 3,
671-681 (2020). (https://doi.org/10.1038/s42003-020-01368-4)