Purification of the stress protein αB-crystallin and its differentially phosphorylated forms

Journal of Immunological Methods

Volumn 221, Issue 1-2, 1998, Pages 159-168

  Van Noort, Johannes M ^a   Van Veelen, Peter ^b   Hopstaken, Frank ^a  

^a TNO   (Netherlands)

^b LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

B crystallin; Phosphorylation; Purification; Stress proteins

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN;

ARTICLE; COMPLEX FORMATION; DEAMINATION; GEL PERMEATION CHROMATOGRAPHY; IMMUNOGENICITY; MASS SPECTROMETRY; NONHUMAN; PHOTOOXIDATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PURIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, ION EXCHANGE; CRYSTALLINS; LENS, CRYSTALLINE; MASS SPECTROMETRY; PHOSPHORYLATION;

BOVINAE; RODENTIA;

EID: 0032444918     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(98)00182-3     Document Type: Article

References (32)

1. Atomi Y., Yamada S., Strohman R., Nonomura Y. Alpha B-crystallin in skeletal muscle: purification and localization. J. Biochem. 110:1991;812. (Tokyo).
2. Bajramović J.J., Lassmann H., van Noort J.M. Expression of alpha B-crystallin in glia cells during lesional development in multiple sclerosis. J. Neuroimmunol. 78:1997;143.
3. Carver J.A., Nicholls K.A., Aquilina J.A., Truscott R.J. Age-related changes in bovine alpha-crystallin and high-molecular-weight protein. Exp. Eye Res. 63:1996;639.
4. Chiesa R., Gawoniwicz-Kolks M.A., Kleiman N.J., Spector A. The phosphorylation sites of the B2 chain of bovine alpha-crystallin. Biochim. Biophys. Acta. 144:1987;1340.
5. De Jong W.W., Zweers A., Versteeg M., Nuy-Terwindt E.C. Primary structures of the alpha-crystallin A chains of twenty-eight mammalian species, chicken and frog. Eur. J. Biochem. 141:1984;131.
6. De Jong W.W., Lubsen N.H., Kraft H.J. Molecular evolution of the eye lens. Prog. Retinal Eye Res. 13:1994;391.
7. Dubin R.A., Wawrousek E.F., Piatigorsky J. Expression of the murine alpha B-crystallin gene is not restricted to the lens. Mol. Cell Biol. 9:1989;1083.
8. Finley E.L., Busman M., Dillon J., Crouch R.K., Schey K.L. Identification of photooxidation sites in bovine alpha-crystallin. Photochem. Photobiol. 66:1997;635.
9. Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K. Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens. Biochim. Biophys. Acta. 1204:1994;157.
10. Groenen P.J., van Dongen M.J., Voorter C.E., Bloemendal H., De Jong W.W. Age-dependent deamidation of alpha B-crystallin. FEBS Lett. 322:1993;69.
11. Head M.W., Corbin E., Goldman J.E. Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander's disease. Am. J. Pathol. 143:1993;1743.
12. Ingolia T.D., Craig E.A. Four small heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl. Acad. Sci. USA. 79:1982;2360.
13. Ito H., Okamoto K., Nakayama H., Isobe T., Kato K. Phosphorylation of alpha B-crystallin in response to various types of stress. J. Biol. Chem. 272:1997;29934.
14. Iwaki T., Kume-Iwaki A., Liem R.K., Goldman J.E. Alpha B-crystallin is expressed in non-lenticular tissue and accumulates in Alexander's disease brain. Cell. 57:1989;71.
15. Iwaki T., Kume-Iwaki A., Goldman J.E. Cellular distribution of alpha B-crystallin in non-lenticular tissues. J. Histochem. Cytochem. 38:1990;31.
16. Iwaki T., Wisniewski T., Iwaki A., Corbin E., Tomokane N., Tateishi J., Goldman J.E. Accumulation of alpha B-crystallin in central nervous system glia and neurons in pathologic conditions. Am. J. Pathol. 140:1992;345.
17. Kamei A., Iwase H., Masuda H. Cleavage of amino acid residue(s) from the N-terminal region of alpha A- and alpha B-crystallins in human crystallin lens during aging. Biochem. Biophys. Res. Commun. 231:1997;373.
18. Klemenz R., Frohli E., Steiger R.H., Schafer R., Aoyama A. Alpha B-crystallin is a small heat shock protein. Proc. Natl. Acad. Sci. USA. 88:1991;3652.
19. Lund A.L., Smith J.B., Smith D.L. Modification of the water-insoluble human lens alpha crystallins. Exp. Eye Res. 63:1996;661.
20. Mann E., McDermott M.J., Goldan J., Chiesa R., Spector A. Phosphorylation of alpha crystallin B in Alexander's disease brain. FEBS Lett. 294:1991;133.
21. Merck K.B., Groenen P.J., Voorter C.E., de Haard-Hoekman W.A., Horwitz J., Bloemendal H., de Jong W.W. Structural and functional similarities of bovine alpha-crystallin and mouse small heat shock proteins. A family of chaperones. J. Biol. Chem. 268:1993;1046.
22. Miesbauer L.R., Zhou X., Yang Z., Sun Y., Smith D.L., Smith J.B. Post-translational modification of water-soluble human lens crystalline from young adults. J. Biol. Chem. 269:1994;12494.
23. Muchowski P.J., Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein alpha B-crystallin. Proc. Natl. Acad. Sci. USA. 95:1998;1004.
24. Nagineni C.N., Bhat S.P. Alpha B-crystallin is expressed in kidney epithelial cell lines and not in fibroblasts. FEBS Lett. 249:1989;89.
25. Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W. Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry. 35:1996;3578.
26. Spector A., Chiesa R., Sredy J., Garner W. cAMP-dependent phosphorylation of bovine alpha-crystallin. Proc. Natl. Acad. Sci. USA. 82:1985;4712.
27. Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313:1992;307.
28. Sun T.X., Liang J.J.N. Intermolecular exchange and stabilization of recombinant human alpha A- and alpha B-crystallin. J. Biol. Chem. 273:1998;286.
29. Van Boeckel M.A., Hoenders H.J. In vivo glycation of bovine lens crystallins. Biochim. Biophys. Acta. 115:1992;99.
30. Van Noort J.M., Van Sechel A.C., Bajramović J.J., Polman C.H., Lassmann H., Ravid R. The small heat-shock protein alpha B-crystallin as candidate autoantigen in multiple sclerosis. Nature. 375:1995;798.
31. Van Stipdonk, M.J.B., Willems, A.A., Amor, S., Persoon-Deen, C., Travers, P.J., Boog, C.J.P., Van Noort, J.M., 1998. T cells discriminate between differentially phosphorylated forms of αB-crystallin, a major central nervous system myelin antigen. Int. Immunol., in press.
32. Voorter C.E.M., de Haard-Hoekman W.A., Roersma E.S., Meyer H., Bloemendal H., De Jong W.W. The in vivo phosphorylation sites of bovine α-crystallin. FEBS Lett. 259:1989;50.