Protein-protein interactions and lens transparency

Experimental Eye Research

Volumn 87, Issue 6, 2008, Pages 496-501

  Takemoto, Larry ^a   Sorensen, Christopher M ^a  

^a KANSAS STATE UNIVERSITY   (United States)

Author keywords

cataract; lens transparency

Indexed keywords

AMYLIN; CRYSTALLIN;

AGING; CATARACT; CATARACTOGENESIS; GENE MUTATION; HUMAN; IN VIVO STUDY; LIGHT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RADIATION SCATTERING; REVIEW;

AGING; BIOMEDICAL RESEARCH; CATARACT; CRYSTALLINS; HUMANS; LENS, CRYSTALLINE; PROTEIN BINDING;

EID: 56349133640     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2008.08.018     Document Type: Review

References (64)

1. Andley, U.P., Bai, F., Xi, J.-H., 2008. A knock in mouse model for the R120G mutation in alphaB-crystallin. ARVO abstract 5023.
2. Benedek G.B. Theory of transparency of the eye. Appl. Opt. 10 (1971) 459-473
3. Berry V., Francis P., Reddy A.A., Collyer D., Vithana E., MacKay I., Dawson G., Carey A., Moore A., Bhataacharya S.S., and Quinlan R.A. Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am. J. Hum. Genet. 69 (2001) 1141-1145
4. Bettelheim F.A., Ali S., White O., and Chylack L.T. Freezable and non-freezable water content of cataractous human lenses. Investig. Ophthalmol. Vis. Sci. 27 (1986) 122-128
5. Bettelheim F.A., Castoro J.A., White O., and Chylack L.T. Topographic correspondence between total and non-freezable water content and the appearance of cataract in human lens. Curr. Eye Res. 5 (1986) 925-932
6. Bettelheim F.A., and Chen A. Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins. Int. J. Biol. Macromol. 22 (1998) 247-252
7. Biswas A., and Das K.P. Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 279 (2004) 42648-42657
8. Bloemendal H. The verterbrate eye lens. Science 197 (1977) 127-138
9. Boyle D.L., Takemoto L., Brady J.P., and Wawrousek E.F. Morphological characterization of the alphaA- and alphaB- crystallin double knockout mouse lens. BMC Ophthalmol. 3 (2003) 1-11
10. Bron A.J., Vrensen G.F., Koretz J., Maraini G., and Harding J.J. The ageing lens. Ophthalmologica 214 (2000) 86-104
11. Brown Z., Ponce A., Lampi K., Hancock L., and Takemoto L. Differential binding of mutant (R116C) and wildtype alpha crystallin to actin. Curr. Eye Res. 32 (2007) 1051-1054
12. Bursell S.E., Baker R.S., Weiss J.N., Haughton J.F., and Rand L.I. Clinical photon correlation spectroscopy evaluation of human diabetic lenses. Exp. Eye Res. 49 (1989) 241-258
13. Carver J.A., Aquilina J.A., Cooper P.G., Williams G.A., and Truscott R.J. Alpha crystallin: molecular chaperone and protein surfactant. Biochim. Biophys. Acta 1205 (1994) 195-206
14. Clark J., and Steele J. Phase-separation inhibitors and prevention of selenite cataract. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 1720-1724
15. Clark J.I., Matsushima H., David L.L., and Clark J.M. Lens cytoskeleton and transparency: a model. Eye 13 (1999) 417-424
16. Cobb B.A., and Petrash M.J. Structural and functional changes in the alpha A crystallin R116C mutant in hereditary cataracts. Biochemistry 39 (2000) 15791-15798
17. Delaye M., and Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302 (1983) 415-417
18. Fu L., and Liang J.J.-N. Alteration of protein-protein interactions of congenital cataract crystallin mutants. Investig. Ophthalmol. Vis. Sci. 44 (2003) 1155-1159
19. Garner M.H., and Spector A. Selective oxidation of cysteine and methionine in normal and senile cataractous lenses. Proc. Natl. Acad. Sci. U.S.A. 77 (1980) 1274-1277
20. Graw J., Klopp N., Illig T., Preising M.N., and Lorenz B. 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 (2006) 912-919
21. Gupta R., and Srivastava O. Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin. Investig. Ophthalmol. Vis. Sci. 45 (2004) 206-214
22. Hains P.G., and Truscott R.J. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J. Proteome Res. 6 (2007) 3935-3953
23. Lampi K.L., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., and David L.L. Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. J. Biol. Chem. 272 (1997) 2268-2275
24. Lampi K.J., Oxford J.T., Bachinger H.P., Shearer T.R., David L.L., and Kapfer D.M. Deamidation of human betaB1 alters the elongated structure of the dimer. Exp. Eye Res. 72 (2001) 279-288
25. Li F., Zhu S., Wang S., Gao C., Huang S., Zhang M., and Ma X. Nonsense mutation in the CRYBB2 gene causing autosomal dominant progressive polymorphic congenital coronary cataracts. Mol. Vis. 14 (2008) 750-755
26. Li F., Wang S., Gao C., Liu S., Zhao B., Zhang M., Huang S., Zhu S., and Ma X. Mutation G61C in the CRYGD gene causing autosomal dominant congenital coralliform cataracts. Mol. Vis. 14 (2008) 378-386
27. Liu M., Ke T., Wang Z., Yang Q., Chang W., Jiang F., Tang Z., Li H., Ren X., Wang X., Li Q., Yang J., Liu J., and Wang Q.K. Identification of a CRYAB mutation associated with autosomal dominant posterior polar cataract in a Chinese family. Investig. Ophthalmol. Vis. Sci. 47 (2006) 3461-3466
28. Liu Y., Zhang X., Luo L., Wu M., Zeng R., Cheng G., Hu B., Liu B., Liang J.J., and Shang F. A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Investig. Ophthalmol. Vis. Sci. 47 (2006) 1069-1075
29. Mackay D.S., Boskovska O.B., Knopf H.L., Lampi K.J., and Shiels A. A nonsense mutatioin in CRYBB1 associated with autosomal dominant cataract linked to human chromosome 22q. Am. J. Hum. Genet. 71 (2002) 1216-1221
30. Mackay D.S., Andley U.P., and Shiels A. Cell death triggered by a novel mutation in the alpha-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. 2003. Eur. J. Hum. Genet. 11 (2003) 784-793
31. McManus J.J., Lomakin A., Ogun O., Pande A., Basan M., Pande J., and Benedek G. Altered phase diagram due to a single point mutation in human gammaD-crystallin. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 16856-16861
32. Mendez-Alcaraz J.M., and Klein R. Depletion forces in colloidal mixtures. Phys. Rev. E, Part B 61 (2000) 4095-4099
33. Messina-Baas O.M., Gonzalez-Huerta L.M., and Cuevas-Covarubias S.A. Two affected siblings with nuclear cataract associated with a novel missense mutation in the CRYGD gene. Mol. Vis. 12 (2006) 995-1000
34. Metlapally S., Costello M.J., Gilliland K.O., Ramamurthy B., Krishna P.V., Balasubramanian D., and Johnsen S. Analysis of nuclear fiber cell cytoplasmic texture in advanced cataractous lenses from Indian subjects using Debye-Bueche theory. Exp. Eye Res. 86 (2008) 424-444
35. Murugesan R., Santhoshkumar P., and Sharma K. Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity. Mol. Vis. 13 (2007) 2301-2309
36. Nilsson M.R., Driscoll M., and Raleigh D. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implication for the study of amyloid formation. Prot. Sci. 11 (2002) 342-349
37. Pande A., Pande J., Asherie N., Lomakin A., Ogun O., King J.A., Lubsen N.H., Walton D., and Benedek G.B. Molecular basis of a progressive juvenile-onset hereditary cataract. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 1993-1998
38. Pande A., Pande J., Asherie N., Lomakin A., Ogun O., and Benedek G.B. Crystal cataracts: human genetic cataract caused by protein crystallization. Proc. Nat. Acad. Sci. U.S.A. 98 (2001) 6116-6120
39. Perng M.D., Muchowski P.J., Ijssel P., Wu G.J., Hutcheson A.M., Clark J.I., and Quinlan R.A. The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274 (2004) 33235-33243
40. Peterson J., Radke G., and Takemoto L. Interaction of lens alpha and gamma crystallins during aging of the bovine lens. Exp. Eye Res. 81 (2005) 680-689
41. Ponce A., and Takemoto L. Screening of crystallin-crystallin interactions using microequilibrium dialysis. Mol. Vis. 11 (2005) 752-757
42. Qin K., Yang D.S., Yang Y., Chishti M.A., Meng L.J., Kretzschmar H.A., Yip C.M., Fraser P.E., and Westaway D. Copper (II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. J. Biol. Chem. 275 (2000) 19121-19131
43. Reddy M.A., Bateman O.A., Chakarova C., Ferris J., Berry V., Lomas E., Sarra R., Smith M.A., Moore A.T., Bhattacharya S.S., and Slingsby C. Hum. Mol. Genet. 13 (2004) 945-953
44. Santhiya S.T., Manohar M.S., Rawlley D., Vijayalakshmi P., Namperumalsamy P., Gopinath P.M., Loster J., and Graw J. Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts. J. Med. Genet. 39 (2002) 352-358
45. Simpanya M.F., Ansari R.R., Suh K.I., Leverenz V.R., and Giblin F.J. Aggregation of lens crystallins in an in vivo hyperbaric oxygen guinea pig model of nuclear cataract: dynamic light-scattering and HPLC analysis. Investig. Ophthalmol. Vis. Sci. 46 (2005) 4641-4651
46. Song S., Hanson M.J., Liu B.-F., Chylack L.T., and Liang J.J.-N. Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching. Mol. Vis. 14 (2008) 1282-1287
47. Stradner A., Foffi G., Dorsaz N., Thurston G., and Schurtenberger R. New insight into cataract formation: enhanced stability through mutual attraction. Phys. Rev. Lett. 99 (2007) 198103-1-198103-4
48. 13C-NMR off-resonance rotating frame spin-lattice relaxation studies of bovine lens gamma-crystallin self association: effect of macromolecular crowding. Biochim. Biophys. Acta 1246 (1995) 82-90
49. Sun H., Ma Z., Li Y., Liu B., Ding X., Gao Y., Ma W., Tang X., Li X., and Shen Y. Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans. J. Med. Genet. 42 (2005) 706-710
50. Talla V., Narayanan C., Srinivasan N., and Balasubramanian D. Mutation causing self-aggregation in human gammaC-crystallin leading to congenital cataract. Investig. Ophthalmol. Vis. Sci. 47 (2006) 5212-5217
51. Takemoto L.J. Oxidation of cysteine residues from alpha-A crystallin during cataractogenesis of the human lens. Biochem. Biophys. Res. Commun. 223 (1996) 216-220
52. Takemoto L.J. BetaA3/A1 crystallin from human cataractous lens contains an intramolecular disulfide bond. Curr. Eye Res. 16 (1997) 719-724
53. Takemoto L.J. Disulfide bond formation of cysteine-37 and cysteine-66 of betaB2 crystallin during cataractogenesis of the human lens. Exp. Eye Res. 64 (1997) 609-614
54. Takemoto L., and Boyle D. Increased deamidation of asparagine during human senile cataractogenesis. Mol. Vis. 6 (2000) 164-168
55. Takemoto L.J., and Ponce A. Decreased association of aged alpha-crystallins with gamma crystallins. Exp. Eye Res. 83 (2006) 793-797
56. Takemoto L., Ponce A., and Sorensen C.M. Age-dependent association of gamma crystallins with aged alpha-crystallins from old bovine lens. Mol. Vis. 14 (2008) 970-974
57. Tardieu A., Veretout F., Krop B., and Slingsby C. Protein interactions in the calf eye lens: interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive. Eur. J. Biophys. 21 (1992) 1-12
58. Thurston G.M., Pande J., Ogun O., and Benedek G.B. Static and quasielastic light scattering and phase separation of concentrated ternary mixtures of bovine alpha and gammaB crystallins. Investig. Ophthalmol. Vis. Sci. 40 (1999) S299
59. 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. R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. FEBS J. 272 (2005) 711-724
60. Trokel S. The physical basis for transparency of the crystalline lens. Investig. Ophthalmol. Vis. Sci. 1 (1962) 493-501
61. Vaezy S., Clark J.I., and Clark J. Quantitative analysis of the lens cell microstructure in selenite cataract using a two-dimensional Fourier analysis. Exp. Eye Res. 60 (1995) 245-255
62. Watanabe A., Won-Kyoung H., Dohmae N., Takio K., Morishima-Kawashima M., and Ihara Y. Molecular aging of tau: disulfide independent aggregation and nonenzymatic degradation in vitro and in vivo. J. Neurochem. 90 (2004) 1302-1311
63. Willoughby C.E., Shafigq A., Ferrini W., Chan L.L., Billingsley G., Priston M., Mok C., Chandna A., Kaye S., and Heon E. CRYBB1 mutation associated with congenital cataract and microcornea. Mol. Vis. 11 (2005) 587-593
64. Wilmarth P.A., Tanner S., Dasari S., Nagalla S.R., Riviere M.A., Bafna V., Pevzner P.A., and David L.L. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystalline insolubility?. J. Proteome Res. 5 (2006) 2554-2566