Autologous extracellular cytochrome c is an endogenous ligand for leucine-rich α2-glycoprotein and β-type phospholipase A2 inhibitor

Journal of Biological Chemistry

Volumn 285, Issue 28, 2010, Pages 21607-21614

  Shirai, Ryoichi ^a   Gotou, Rikiya ^a   Hirano, Fumiyasu ^a   Ikeda, Kiyoshi ^a   Inoue, Seiji ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; CYTOCHROME C; DEAD CELLS; DISSOCIATION CONSTANT; EXTRACELLULAR; INHIBITORY ACTIVITY; INHIBITORY PROTEINS; PHOSPHOLIPASE A; SEQUENCE HOMOLOGY; SERUM PROTEINS; SURFACE PLASMONS;

AMINO ACIDS; BODY FLUIDS; CELL DEATH; GLYCOPROTEINS; LIGANDS; PROTEINS; SURFACE PLASMON RESONANCE; YEAST;

DISSOCIATION;

ALPHA2 GLYCOPROTEIN; CYTOCHROME C; LEUCINE RICH ALPHA2 GLYCOPROTEIN; LIGAND; PHOSPHOLIPASE A2 INHIBITOR; PHOSPHOLIPASE A2 INHIBITOR BETA; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; ENZYME INHIBITION; GEL FILTRATION CHROMATOGRAPHY; HORSE; HUMAN; IMMUNODETECTION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE HOMOLOGY; SNAKE; SURFACE PLASMON RESONANCE; YEAST;

ANIMALS; BLOOD PROTEINS; CIRCULAR DICHROISM; CYTOCHROMES C; DOSE-RESPONSE RELATIONSHIP, DRUG; FUNGAL PROTEINS; GLYCOPROTEINS; HORSES; HUMANS; LEUCINE; LIGANDS; PHOSPHOLIPASES A2; PROTEIN BINDING; SNAKES; SURFACE PLASMON RESONANCE;

EQUIDAE; GLOYDIUS BLOMHOFFI BREVICAUDUS;

EID: 77954377278     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.122788     Document Type: Article

References (37)

1. Ohkura, N., Okuhara, H., Inoue, S., Ikeda, K., and Hayashi, K. (1997) Biochem. J. 325, 527-531
2. Lambeau, G., and Lazdunski, M. (1999) Trends. Pharmacol. Sci. 20, 162-170
3. Okumura, K., Ohkura, N., Inoue, S., Ikeda, K., and Hayashi, K. (1998) J. Biol. Chem. 273, 19469-19475
4. Okumura, K., Inoue, S., Ikeda, K., and Hayashi, K. (2002) Arch. Biochem. Biophys. 408, 124-130
5. Shirai, R., Toriba, M., Hayashi, K., Ikeda, K., and Inoue, S. (2009) Toxicon 53, 685-692
6. Haupt, H., and Baudner, S. (1977) Hoppe Seylers Z. Physiol. Chem. 358, 639-646
7. Takahashi, N., Takahashi, Y., and Putnam, F. W. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1906-1910
8. O'Donnell, L. C., Druhan, L. J., and Avalos, B. R. (2002) J. Leukoc. Biol. 72, 478-485
9. Cummings, C., Walder, J., Treeful, A., and Jemmerson, R. (2006) Apoptosis. 11, 1121-1129
10. Weivoda, S., Andersen, J. D., Skogen, A., Schlievert, P. M., Fontana, D., Schacker, T., Tuite, P., Dubinsky, J. M., and Jemmerson, R. (2008) J. Immunol. Methods 336, 22-29
11. Shirai, R., Hirano, F., Ohkura, N., Ikeda, K., and Inoue, S. (2009) Biochem. Biophys. Res. Commun. 382, 776-779
12. Codina, R., Vanasse, A., Kelekar, A., Vezys, V., and Jemmerson, R. (2010) Apoptosis 15, 139-152
13. Inoue, S., Shimada, A., Ohkura, N., Ikeda, K., Samejima, Y., Omori-Satoh, T., and Hayashi, K. (1997) Biochem. Mol. Biol. Int. 41, 529-537
14. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326
15. Inoue, S., Hiroyoshi, T., Matsubara, H., and Yamanaka, T. (1984) Biochim. Biophys. Acta 790, 188-195
16. Margoliash, E., and Frohwirt, N. (1959) Biochem. J. 71, 570-572
17. Ornstein, L. (1964) Ann. N. Y. Acad. Sci. 121, 321-349
18. Radvanyi, F., Jordan, L., Russo-Marie, F., and Bon, C. (1989) Anal. Biochem. 177, 103-109
19. Okumura, K., Inoue, S., Ikeda, K., and Hayashi, K. (1999) Biochim. Biophys. Acta 1441, 51-60
20. Stumpp, M. T., Forrer, P., Binz, H. K., and Plückthun, A. (2003) J. Mol. Biol. 332, 471-487
21. Kobe, B., and Kajava, A. V. (2001) Curr. Opin. Struct. Biol. 11, 725-732
22. Schubert, W. D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., and Heinz, D. W. (2002) Cell 111, 825-836
23. Fan, Q. R., and Hendrickson, W. A. (2005) Nature 433, 269-277
24. Johnson, R. J., McCoy, J. G., Bingman, C. A., Phillips, G. N., Jr., and Raines, R. T. (2007) J. Mol. Biol. 368, 434-449
25. Huizinga, E. G., Tsuji, S., Romijn, R. A., Schiphorst, M. E., de Groot, P. G., Sixma, J. J., and Gros, P. (2002) Science 297, 1176-1179
26. Kluck, R. M., Ellerby, L. M., Ellerby, H. M., Naiem, S., Yaffe, M. P., Margoliash, E., Bredesen, D., Mauk, A. G., Sherman, F., and Newmeyer, D. D. (2000) J. Biol. Chem. 275, 16127-16133
27. Kini, R. M. (2003) Toxicon 42, 827-840
28. Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. (1996) Cell 86, 147-157
29. Zou, H., Li, Y., Liu, X., and Wang, X. (1999) J. Biol. Chem. 274, 11549-11556
30. Jiang, X., and Wang, X. (2004) Annu. Rev. Biochem. 73, 87-106
31. Renz, A., Berdel, W. E., Kreuter, M., Belka, C., Schulze-Osthoff, K., and Los, M. (2001) Blood 98, 1542-1548
32. Jemmerson, R., LaPlante, B., and Treeful, A. (2002) Cell Death. Differ. 9, 538-548
33. Hiraoka, Y., Yamada, T., Goto, M., Das Gupta, T. K., and Chakrabarty, A. M. (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 6427-6432
34. Lin, M. L., Zhan, Y., Proietto, A. I., Prato, S., Wu, L., Heath, W. R., Villadangos, J. A., and Lew, A. M. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 3029-3034
35. Pullerits, R., Bokarewa, M., Jonsson, I. M., Verdrengh, M., and Tarkowski, A. (2005) Rheumatology 44, 32-39
36. Zhang, Q., Raoof, M., Chen, Y., Sumi, Y., Sursal, T., Junger, W., Brohi, K., Itagaki, K., and Hauser, C. J. (2010) Nature 464, 104-107
37. Ai, J., Druhan, L. J., Hunter, M. G., Loveland, M. J., and Avalos, B. R. (2008) J. Leukoc. Biol. 83, 1277-1285