Jeltraxin, a Frog Egg Jelly Glycoprotein, Has Calcium-Dependent Lectin Properties and is Related to Human Serum Pentraxins CRP and SAP

Biochemistry

Volumn 42, Issue 44, 2003, Pages 12761-12769

  Peavy, Thomas R ^a   Hernandez, Cesar ^b   Carroll Jr , Edward J ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b CALIFORNIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BODY FLUIDS; CALCIUM; RNA; SUGARS;

AMPHIBIAN EGGS;

PROTEINS;

ACUTE PHASE PROTEIN; BETA GALACTOSE; C REACTIVE PROTEIN; CALCIUM DEPENDENT LECTIN; CALCIUM ION; FROG EGG JELLY GLYCOPROTEIN; GALACTOSE; GLYCOPROTEIN; JELTRAXIN; LECTIN; OLIGOMER; PENTRAXIN; PROTEIN SUBUNIT; SERUM AMYLOID P; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIOTINYLATION; CELL ENCAPSULATION; CHEMICAL COMPOSITION; CONTROLLED STUDY; CRYSTALLOGRAPHY; EGG; EGG JELLY COAT; ENZYME SPECIFICITY; FERTILIZATION; FROG; HOMOLOGY MODELING; IMMUNE RESPONSE; LEPIDOBATRACHUS LAEVIS; LIVER; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; OVIDUCT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; AMPHIBIAN PROTEINS; ANIMALS; ANURA; BASE SEQUENCE; C-REACTIVE PROTEIN; CALCIUM; CLONING, MOLECULAR; EGG PROTEINS; FEMALE; GLYCOPROTEINS; HUMANS; LECTINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PROTEIN BINDING; RNA, MESSENGER; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SERUM AMYLOID P-COMPONENT; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

AMPHIBIA; ANIMALIA; ANURA; LEPIDOBATRACHUS; LEPIDOBATRACHUS LAEVIS; MAMMALIA; XENOPUS LAEVIS;

EID: 0242675982     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035314o     Document Type: Article

References (50)

1. Hedrick, J. L., and Hardy, D. M. (1991) Methods Cell Biol. 36, 231-247.
2. Iwao, Y. (2000) in Fertilization in Protozoans and Metazoan Animals (Tarin, J. J., and Cano, A., Eds.) pp 147-191, Springer-Verlag, New York.
3. Olson, J. H., Xiang, X., Ziegert, T., Kittelson, A., Rawls, A., Bieber, A. L., and Chandler, D. E. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 11205-11210.
4. Olson, J. H., and Chandler, D. E. (1999) Dev. Biol. 210, 401-410.
5. Campanella, C., Carotenuto, R., Infante, V., Maturi, G., and Atripaldi, U. (1997) Mol. Reprod. Dev. 47, 323-333.
6. Picheral, B. (1977) J. Ultrastruct. Res. 60, 181-202.
7. Onitake, K., Takai, H., Ukita, M., Mizuno, J. I., Sasaki, T., and Watanabe, A. (2000) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 126, 121-128.
8. Ueda, Y., Yoshizaki, N., and Iwao, Y. (2002) Dev. Biol. 243, 55-64.
9. Wyrick, R. E., Nishihara, T., and Hedrick, J. L. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 2067-2071.
10. Ishihara, K., Hosono, J., Kanatani, H., and Katagiri, C. (1984) Dev. Biol. 105, 435-442.
11. Bonnell, B. S., and Chandler, D. E. (1996) Mol. Reprod. Dev. 44, 212-220.
12. Bonnell, B. S., Reinhart, D., and Chandler, D. E. (1996) Dev. Biol. 174, 32-42.
13. Shimoda, Y., Kitajima, K., Inoue, S., and Inoue, Y. (1994) Eur. J. Biochem. 223, 223-231.
14. Arranz, S. E., and Cabada, M. O. (2000) Mol. Reprod. Dev. 56, 392-400.
15. Quill, T. A., and Hedrick, J. L. (1994) Dev. Growth Differ. 36, 615-620.
16. Quill, T. A., and Hedrick, J. L. (1996) Arch. Biochem. Biophys. 333, 326-332.
17. Carroll, E. J., Jr., Wei, S. H., and Nagel, G. M. (1991) Arch. Biochem. Biophys. 284, 346-351.
18. Perchez, M. A., and Carroll, E. J., Jr. (1996) Dev. Growth Differ. 38, 15-22.
19. Gewurz, H., Zhang, X. H., and Lint, T. F. (1995) Curr. Opin. Immunol. 7, 54-64.
20. Hohenester, E., Hutchinson, W. L., Pepys, M. B., and Wood, S. P. (1997) J. Mol. Biol. 269, 570-578.
21. Thompson, D., Pepys, M. B., and Wood, S. P. (1999) Struct. Folding Des. 7, 169-177.
22. Emsley, J., White, H. E., O'Hara, B. P., Oliva, G., Srinivasan, N., Tickle, I. J., Blundell, T. L., Pepys, M. B., and Wood, S. P. (1994) Nature 367, 338-345.
23. Steel, D. M., and Whitehead, A. S. (1994) Immunol. Today 15, 81-88.
24. Lin, L., and Liu, T. Y. (1993) J. Biol. Chem. 268, 6809-6815.
25. Jensen, L. E., Hiney, M. P., Shields, D. C., Uhlar, C. M., Lindsay, A. J., and Whitehead, A. S. (1997) J. Immunol. 158, 384-392.
26. Lund, V., and Olafsen, J. A. (1998) Dev. Comp. Immunol. 22, 185-194.
27. Robey, F. A., and Liu, T. Y. (1981) J. Biol. Chem. 256, 969-975.
28. Seery, L. T., Schoenberg, D. R., Barbaux, S., Sharp, P. M., and Whitehead, A. S. (1993) Proc. R. Soc. London, Ser. B. 253, 263-270.
29. Tsui, C. C., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Barnes, C., and Worley, P. F. (1996) J. Neurosci. 16, 2463-2478.
30. Polentarutti, N., Bottazzi, B., Di Santo, E., Blasi, E., Agnello, D., Ghezzi, P., Introna, M., Bartfai, T., Richards, G., and Mantovani, A. (2000) J. Neuroimmunol. 106, 87-94.
31. Breviario, F., d'Aniello, E. M., Golay, J., Peri, G., Bottazzi, B., Bairoch, A., Saccone, S., Marzella, R., Predazzi, V., and Rocchi, M. (1992) J. Biol. Chem. 267, 22190-22197.
32. Noland, T. D., Friday, B. B., Maulit, M. T., and Gerton, G. L. (1994) J. Biol. Chem. 269, 32607-32614.
33. Reid, M. S., and Blobel, C. P. (1994) J. Biol. Chem. 269, 32615-32620.
34. Varani, S., Elvin, J. A., Yan, C. N., DeMayo, J., DeMayo, F. J., Horton, H. F., Byrne, M. C., and Matzuk, M. M. (2002) Mol. Endocrinol. 16, 1154-1167.
35. Ruibal, R., and Thomas, E. (1988) Copeia 1988, 591-604.
36. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Anal. Biochem. 150, 76-85.
37. Chomczynski, P., and Sacchi, N. (1987) Anal. Biochem. 162, 156-159.
38. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Moleular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Plainview, NY.
39. Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997) Protein Eng. 10, 1-6.
40. Wilkins, M. R., Gasteiger, E., Bairoch, A., Sanchez, J. C., Williams, K. L., Appel, R. D., and Hochstrasser, D. F. (1999) Methods Mol. Biol. 112, 531-552.
41. Shrive, A. K., Cheetham, G. M., Holden, D., Myles, D. A., Turnell, W. G., Volanakis, J. E., Pepys, M. B., Bloomer, A. C., and Greenhough, T. J. (1996) Nat. Struct. Biol. 3, 346-354.
42. Tennent, G. A., and Pepys, M. B. (1994) Biochem. Soc. Trans. 22, 74-79.
43. Buhi, W. C. (2002) Reproduction 123, 355-362.
44. Kinoshita, C. M., Gewurz, A. T., Siegel, J. N., Ying, S. C., Hugli, T. E., Coe, J. E., Gupta, R. K., Huckman, R., and Gewurz, H. (1992) Protein Sci. 1, 700-709.
45. Kinoshita, C. M., Ying, S. C., Hugli, T. E., Siegel, J. N., Potempa, L. A., Jiang, H., Houghten, R. A., and Gewurz, H. (1989) Biochemistry 28, 9840-9848.
46. Pinteric, L., Assimeh, S. N., Kells, D. I., and Painter, R. H. (1976) J. Immunol. 117, 79-83.
47. Osmand, A. P., Friedenson, B., Gewurz, H., Painter, R. H., Hofmann, T., and Shelton, E. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 739-743.
48. Hind, C. R. K., Collins, P. M., Renn, D., Cook, R. B., Caspi, D., Baltz, M. L., and Pepys, M. B. (1984) J. Exp. Med. 159, 1058-1069.
49. Del Pino, E. M. (1973) J. Exp. Zool. 185, 121-132.
50. Wolf, D. P., and Hedrick, J. L. (1971) Dev. Biol. 25, 348-359.