Modulation of α-crystallin chaperone activity in diabetic rat lens by curcumin

Molecular Vision

Volumn 11, Issue , 2005, Pages 561-568

  Kumar, P Anil ^a   Suryanarayana, P ^a   Reddy, P Yadagiri ^a   Reddy, G Bhanuprakash ^a  

^a NATIONAL INSTITUTE OF NUTRITION   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; CURCUMIN; STREPTOZOCIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; CATARACT; CATARACTOGENESIS; CONTROLLED STUDY; DIABETES MELLITUS; DIET SUPPLEMENTATION; DISEASE COURSE; DOSE RESPONSE; GEL FILTRATION; HYDROPHOBICITY; HYPERGLYCEMIA; LENS; LIGHT SCATTERING; MALE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAT; SLIT LAMP; SPECTROSCOPY; STREPTOZOCIN DIABETES;

ALPHA-CRYSTALLINS; ANIMALS; ANTIOXIDANTS; BLOOD GLUCOSE; BODY WEIGHT; CATARACT; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CURCUMIN; DIABETES MELLITUS, EXPERIMENTAL; DIET; HYPERGLYCEMIA; LENS, CRYSTALLINE; MALE; MOLECULAR CHAPERONES; RATS; SPECTROMETRY, FLUORESCENCE;

EID: 26244442494     PISSN: 10900535     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur J Biochem 1994; 225:1-19.
2. Horwitz J. Alpha-crystallin. Exp Eye Res 2003; 76:145-53.
3. Ganea E. Chaperone-like activity of alpha-crystallin and other small heat shock proteins. Curr Protein Pept Sci 2001; 2:205-25.
4. Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. J Biol Chem 2000; 275:4565-70.
5. Reddy GB, Reddy PY, Suryanarayana P. alphaA- and alphaB-crystallins protect glucose-6-phosphate dehydrogenase against UVB irradiation-induced inactivation. Biochem Biophys Res Commun 2001; 282:712-6.
6. Hook DW, Harding JJ. Molecular chaperones protect catalase against thermal stress. Eur J Biochem 1997; 247:380-5.
7. Bhat SP. Crystallins, genes and cataract. Prog Drug Res 2003; 60:205-62.
8. Bai F, Xi JH, Wawrousek EF, Fleming TP, Andley UP. Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice. J Biol Chem 2003; 278:36876-86.
9. Boyle DL, Takemoto L, Brady JP, Wawrousek EF. Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. BMC Ophthalmol 2003; 3:3.
10. Brady JP, Garland D, Duglas-Tabor Y, Robison WG Jr, Groome A, Wawrousek EF. Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin. Proc Natl Acad Sci U S A 1997; 94:884-9.
11. Thampi P, Hassan A, Smith JB, Abraham EC. Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 2002; 43:3265-72.
12. Hanson SR, Hasan A, Smith DL, Smith JB. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp Eye Res 2000; 71:195-207.
13. van Boekel MA, Hoenders HJ. Glycation of crystallins in lenses from aging and diabetic individuals. FEBS Lett 1992; 314:1-4.
14. Derham BK, Harding JJ. Effects of modifications of alpha-crystallin on its chaperone and other properties. Biochem J 2002; 364:711-7.
15. Cherian M, Abraham EC. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem Biophys Res Commun 1995; 208:675-9.
16. Kumar MS, Reddy PY, Kumar PA, Surolia I, Reddy GB. Effect of dicarbonyl-induced browning on alpha-crystallin chaperonelike activity: physiological significance and caveats of in vitro aggregation assays. Biochem J 2004; 379:273-82.
17. Thampi P, Abraham EC. Influence of the C-terminal residues on oligomerization of alpha A-crystallin. Biochemistry 2003; 42:11857-63.
18. Derham BK, Harding JJ. Effect of aging on the chaperone-like function of human alpha-crystallin assessed by three methods. Biochem J 1997; 328:763-8.
19. Horwitz J, Emmons T, Takemoto L. The ability of lens alpha crystallin to protect against heat-induced aggregation is agedependent. Curr Eye Res 1992; 11:817-22.
20. Harding, J. Cataract: biochemistry, epidemiology, and pharmacology. 1st ed. London: Chapman and Hall; 1991.
21. Nirmalan PK, Robin AL, Katz J, Tielsch JM, Thulasiraj RD, Krishnadas R, Ramakrishnan R. Risk factors for age related cataract in a rural population of southern India: the Aravind Comprehensive Eye Study. Br J Ophthalmol 2004; 88:989-94.
22. Ughade SN, Zodpey SP, Khanolkar VA. Risk factors for cataract: a case control study. Indian J Ophthalmol 1998; 46:221-7.
23. International Diabetes Federation (2001) Diabetes Atlas 2000. Brussels: International Diabetic Foundation (www.idf.org).
24. Thampi P, Zarina S, Abraham EC. alpha-Crystallin chaperone function in diabetic rat and human lenses. Mol Cell Biochem 2002; 229:113-8.
25. Cherian M, Abraham EC. Diabetes affects alpha-crystallin chaperone function. Biochem Biophys Res Commun 1995; 212:184-9.
26. Huang FY, Ho Y, Shaw TS, Chuang SA. Functional and structural studies of alpha-crystallin from galactosemic rat lenses. Biochem Biophys Res Commun 2000; 273:197-202.
27. Suryanarayana P, Krishnaswamy K, Reddy GB. Effect of curcumin on galactose-induced cataractogenesis in rats. Mol Vis 2003; 9:223-30.
28. Suryanarayana P, Saraswat M, Mrudula T, Krishna TP, Krishnaswamy K, Reddy GB. Curcumin and turmeric delay streptozotocin-induced diabetic cataract in rats. Invest Ophthalmol Vis Sci 2005; 46:2092-9.
29. Reeves PG. Components of the AIN-93 diets as improvements in the AIN-76A diet. J Nutr 1997; 127:838S-841S.
30. Reddy GB, Reddy PY, Vijayalakshmi A, Kumar MS, Suryanarayana P, Sesikeran B. Effect of long-term dietary manipulation on the aggregation of rat lens crystallins: role of alpha-crystallin chaperone function. Mol Vis 2002; 8:298-305.
31. Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett 1995; 369:321-5.
32. Raman B, Rao CM. Chaperone-like activity and temperature-induced structural changes of alpha-crystallin. J Biol Chem 1997; 272:23559-64.
33. Sharma KK, Kaur H, Kumar GS, Kester K. Interaction of 1,1′-bi (4-anilino)naphthalene-5,5′-disulfonic acid with alpha-crystallin. J Biol Chem 1998; 273:8965-70.
34. Kumar MS, Kapoor M, Sinha S, Reddy GB. Insights into hydrophobicity and the chaperone-like function of alphaA- and alphaB-crystallins: An isothermal titrationcalorimetric study. J Biol Chem 2005; 280:21726-30.
35. Pradeepa R, Mohan V. The changing scenario of the diabetes epidemic: implications for India. Indian J Med Res 2002; 116:121-32.
36. Kyselova Z, Stefek M, Bauer V. Pharmacological prevention of diabetic cataract. J Diabetes Complications 2004; 18:129-40.
37. Spector A. Review: Oxidative stress and disease. J Ocul Pharmacol Ther 2000; 16:193-201.
38. Mares JA. High-dose antioxidant supplementation and cataract risk. Nutr Rev 2004; 62:28-32.
39. Kador PF, Kinoshita JH, Sharpless NE. Aldose reductase inhibitors: a potential new class of agents for the pharmacological control of certain diabetic complications. J Med Chem 1985; 28:841-9.
40. Clark JI, Huang QL. Modulation of the chaperone-like activity of bovine alpha-crystallin. Proc Natl Acad Sci U S A 1996; 93:15185-9.
41. Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao ChM. Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride. Protein Sci 2003; 12:1262-70.
42. Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao ChM. Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin. Mol Vis 2005; 11:249-55.
43. Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen PP, Kayed R, Glabe CG, Frautschy SA, Cole GM. Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 2005; 280:5892-901.
44. Horwitz J, Huang QL, Ding L, Bova MP. Lens alpha-crystallin: chaperone-like properties. Methods Enzymol 1998; 290:365-83.