Characterization of a mutant R11H αB-crystallin associated with human inherited cataract

Biological Chemistry

Volumn 391, Issue 12, 2010, Pages 1391-1400

  Chen, Qiang ^a,b   Yan, Ming ^a   Xiang, Feiyan ^a   Zhou, Xin ^a   Liu, Yuanyuan ^a   Zheng, Fang ^a  

^a WUHAN UNIVERSITY   (China)

^b National Institute for Communicable Disease Control and Prevention   (China)

Author keywords

Apoptosis; Cataract; Chaperone like activity; CRYAB; Subcellular distribution

Indexed keywords

ALPHA B CRYSTALLIN; ALPHA CRYSTALLIN; CHAPERONE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CATARACT; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DISEASE ASSOCIATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; MOLECULAR WEIGHT; MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; THERMOSTABILITY; WILD TYPE; CHEMICAL PHENOMENA; CHEMISTRY; CIRCULAR DICHROISM; GENETICS; METABOLISM; SITE DIRECTED MUTAGENESIS;

ALPHA-CRYSTALLIN B CHAIN; APOPTOSIS; CATARACT; CIRCULAR DICHROISM; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION;

EID: 79952523769     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.143     Document Type: Article

References (47)

1. Andley, U.P. (2007). Crystallins in the eye: function and pathology. Prog. Retin. Eye Res. 26, 78-98. (Pubitemid 44894995)
2. Andley, U.P., Song, Z., Wawrousek, E.F., Fleming, T.P., and Bassnett, S. (2000). Differential protective activity of aA- and αBcrystallin in lens epithelial cells. J. Biol. Chem. 275, 36823-36831. (Pubitemid 32002093)
3. Andley, U.P., Patel, H.C., and Xi, J.H. (2002). The R116C mutation in aA-crystallin diminishes its protective ability against stressinduced lens epithelial cell apoptosis. J. Biol. Chem. 277, 10178-10186. (Pubitemid 34968131)
4. Berengian, A.R., Bova, M.P., and McHaourab, H.S. (1997). Structure and function of the conserved domain in alphaA-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface. Biochemistry 36, 9951-9957. (Pubitemid 27357703)
5. Bhattacharyya, J., Padmanabha Udupa, E.G., Wang, J., and Sharma, K.K. (2006). Mini-αB-crystallin: a functional element of αBcrystallin with chaperone-like activity. Biochemistry 45, 3069-3076. (Pubitemid 43334555)
6. Biswas, A. and Das, K.P. (2004). Role of ATP on the interaction of a-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 279, 42648-42657. (Pubitemid 39372150)
7. Bova, M.P., Yaron, O., Huang, Q., Ding, L., Haley, D.A., Stewart, P.L., and Horwitz, J. (1999). Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. USA 96, 6137-6142. (Pubitemid 29256632)
8. Brady, J.P., Garland, D., Duglas-Tabor, Y., Robison, W.G. Jr., Groome, A., and Wawrousek, E.F. (1997). Targeted disruption of the mouse aA-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein αBcrystallin. Proc. Natl. Acad. Sci. USA 94, 884-889.
9. Brady, J.P., Garland, D.L., Green, D.E., Tamm, E.R., Giblin, F.J., and Wawrousek, E.F. (2001). AlphαB-crystallin in lens development and muscle integrity: a gene knockout approach. Invest. Ophthalmol. Vis. Sci. 42, 2924-2934. (Pubitemid 33035292)
10. Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C.M., and Stefani, M. (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511. (Pubitemid 34288846)
11. Chen, Q., Ma, J., Yan, M., Mothobi, M.E., Liu, Y., and Zheng, F. (2009). A novel mutation in CRYAB associated with autosomal dominant congenital nuclear cataract in a Chinese family. Mol. Vis. 15, 1359-1365.
12. Das, K.P. and Surewicz, W.K. (1995). Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of a-crystallin. FEBS Lett. 369, 321-325.
13. Delaye, M. and Tardieu, A. (1983). Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302, 415-417. (Pubitemid 13164324)
14. Eifert, C., Burgio, M.R., Bennett, P.M., Salerno, J.C., and Koretz, J.F. (2005). N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function. Biochim. Biophys. Acta 1748, 146-156. (Pubitemid 40354243)
15. Fu, L. and Liang, J.J. (2003). Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest. Ophthalmol. Vis. Sci. 44, 1155-1159. (Pubitemid 36297835)
16. Fu, B., Zhang, D., Weng, X., Zhang, M., Ma, H., Ma, Y., and Zhou, X. (2008). Cationic metal-corrole complexes: design, synthesis, and properties of guanine-quadruplex stabilizers. Chemistry 14, 9431-9441.
17. Graw, J., Klopp, N., Illig, T., Preising, M.N., and Lorenz, B. (2006). Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P. Graefes Arch. Clin. Exp. Ophthalmol. 244, 912-919. (Pubitemid 44184494)
18. Greenfield, N.J. (2006). Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1, 2527-2535.
19. Hansen, L., Yao, W., Eiberg, H., Kjaer, K.W., Baggesen, K., Hejtmancik, J.F., and Rosenberg, T. (2007). Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8. Invest. Ophthalmol. Vis. Sci. 48, 3937-3944. (Pubitemid 351261012)
20. Horwitz, J. (1992). Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89, 10449-10453.
21. Horwitz, J. (2003). Alpha-crystallin. Exp. Eye Res. 76, 145-153. (Pubitemid 36266698)
22. Horwitz, J., Bova, M., Huang, Q.L., Ding, L., Yaron, O., and Lowman, S. (1998a). Mutation of αB-crystallin: effects on chaperone-like activity. Int. J. Biol. Macromol. 22, 263-269. (Pubitemid 28276740)
23. Horwitz, J., Huang, Q.L., Ding, L., and Bova, M.P. (1998b). Lens a-crystallin: chaperone-like properties. Methods Enzymol. 290, 365-383.
24. Ingolia, T.D. and Craig, E.A. (1982). Four small Drosophila HSPs are related to each other and to mammalian crystallin. Proc. Natl. Acad. Sci. USA 79, 2360-2364. (Pubitemid 12161321)
25. Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993). Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520. (Pubitemid 23033534)
26. Koteiche, H.A. and McHaourab, H.S. (2006). Mechanism of a hereditary cataract phenotype. Mutations in aA-crystallin activate substrate binding. J. Biol. Chem. 281, 14273-14279. (Pubitemid 43848355)
27. Kumar, L.V.S., Ramakrishna, T., and Rao, C.M. (1999). Structural and functional consequences of the mutation of a conserved arginine residue in aA and αB-crystallins. J. Biol. Chem. 274, 24137-24141.
28. Kundu, M., Sen, P.C., and Das, K.P. (2007). Structure, stability, and chaperone function of aA-crystallin: role of N-terminal region. Biopolymers 86, 177-192. (Pubitemid 46910390)
29. Li, H., Li, C., Lu, Q., Su, T., Ke, T., Li, D.W., Yuan, M., Liu, J., Ren, X., Zhang, Z., et al. (2008). Cataract mutation P20S of αBcrystallin impairs chaperone activity of a crystallin and induces apoptosis of human lens epithelial cells. Biochim. Biophys. Acta 1782, 303-309.
30. Litt, M., Kramer, P., LaMorticella, D.M., Murphey, W., Lovrien, E.W., and Weleber, R.G. (1998). Autosomal dominant congenital cataract associated with a missense mutation in the human a crystallin gene CRYAA. Hum. Mol. Genet. 7, 471-474. (Pubitemid 28120638)
31. Liu, Y., Zhang, X., Luo, L., Wu, M., Zeng, R., Cheng, G., Hu, B., Liu, B., Liang, J.J., and Shang, F. (2006). A novel αB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest. Ophthalmol. Vis. Sci. 47, 1069-1075. (Pubitemid 46768341)
32. Mackay, D.S., Andley, U.P., and Shiels, A. (2003). Cell death triggered by a novel mutation in the aA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur. J. Hum. Genet. 11, 784-793. (Pubitemid 37337062)
33. Mafia, K., Gupta, R., Kirk, M., Wilson, L., Srivastava, O.P., and Barnes, S. (2008). UV-A-induced structural and functional changes in human lens deamidated αB-crystallin. Mol. Vis. 14, 234-248. (Pubitemid 351234338)
34. Markossian, K., Yudin, I., and Kurganov, B. (2009). Mechanism of suppression of protein aggregation by a-crystallin. Int. J. Mol. Sci. 10, 1314-1345.
35. Murugesan, R., Santhoshkumar, P., and Sharma, K.K. (2007). Cataract-causing aA-G98R mutant shows substrate-dependent chaperone activity. Mol. Vis. 13, 2301-2309. (Pubitemid 350303477)
36. Musci, G., Metz, G.D., Tsunematsu, H., and Berliner, L.J. (1985). 4,49-Bis w8-(phenylamino) naphthalene-1-sulfonatex binding to human thrombins: a sensitive exo site fluorescent affinity probe. Biochemistry 24, 2034-2039. (Pubitemid 15018534)
37. Perng, M.D., Muchowski, P.J., van Den IJssel, P., Wu, G.J., Hutcheson, A.M., Clark, J.I., and Quinlan, R.A. (1999). The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274, 33235-33243. (Pubitemid 129511621)
38. Raman, B. and Rao, C.M. (1994). Chaperone-like activity and quaternary structural of a-crystallin. J. Biol. Chem. 269, 27264-27268. (Pubitemid 24346544)
39. Reddy, G.B., Das, K.P., Petrash, J.M., and Surewicz, W.K. (2000). Temperature-dependent chaperone activity and structural properties of human aA- and αB-crystallins. J. Biol. Chem. 275, 4565-4570. (Pubitemid 30108838)
40. Santhiya, S.T., Soker, T., Klopp, N., Illig, T., Prakash, M.V., Selvaraj, B., Gopinath, P.M., and Graw, J. (2006). Identification of a novel putative cataract-causing allele in CRYAA (G98R) in an Indian family. Mol. Vis. 12, 768-773. (Pubitemid 44044578)
41. Safieh, L.A., Khan, A.O., and Alkuraya, F.S. (2009). Identification of a novel CRYAB mutation associated with autosomal recessive juvenile cataract in a Saudi family. Mol. Vis. 15, 980-984.
42. Sharma, K.K., Kaur, H., Kumar, G.S., and Kester, K. (1998). Interaction of 1,19-bi (4-anilino) naphthalene-5,59-disulfonic acid with a-crystallin. J. Biol Chem. 273, 8965-8970.
43. Shi, L., Palleros, D.R., and Fink, A.L. (1994). Protein conformational changes induced by 1,19-bis (4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 33, 7536-7546. (Pubitemid 24230577)
44. Shroff, N.P., Bera, S., Cherian-Shaw, M., and Abraham, E.C. (2001). Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin. Mol. Cell. Biochem. 220, 127-133. (Pubitemid 32519947)
45. Sreerama, N., Venyaminov, S.Y., and Woody, R.W. (1999). Estimation of the number of a-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380. (Pubitemid 29072437)
46. Treweek, T.M., Rekas, A., Lindner, R.A., Walker, M.J., Aquilina, J.A., Robinson, C.V., Horwitz, J., Perng, M.D., Quinlan, R.A., and Carver, J.A. (2005). R120G αB-crystallin promotes the unfolding of reduced a-lactalbumin and is inherently unstable. FEBS J. 272, 711-724. (Pubitemid 40208874)
47. Vicart, P., Caron, A., Guicheney, P., Li, Z., Prevost, M.C., Faure, A., Chateau, D., Chapon, F., Tome, F., Dupret, J.M., et al. (1998). A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20, 92-95. (Pubitemid 28410353)