αb-Crystallin selectively targets intermediate filament proteins during thermal stress

Investigative Ophthalmology and Visual Science

Volumn 40, Issue 5, 1999, Pages 951-958

  Muchowski, Paul J ^a   Valdez, Melissa M ^a   Clark, John I ^a,b  

^a UNIVERSITY OF WASHINGTON   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA CRYSTALLIN; ALPHA TUBULIN; AMYLOSE; BETA CRYSTALLIN; CHAPERONE; CYTOSKELETON PROTEIN; FILENSIN; HEAT SHOCK PROTEIN; HYBRID PROTEIN; INTERMEDIATE FILAMENT PROTEIN; LENS PROTEIN; MALTOSE BINDING PROTEIN; SPECTRIN; CRYSTALLIN; EYE PROTEIN; MALTOSE; PHAKININ; VIMENTIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CATARACT; CATTLE; CELL FREE SYSTEM; CELL PROTECTION; CONTROLLED STUDY; HEAT STRESS; IMMUNOPRECIPITATION; INTERMEDIATE FILAMENT; LENS EPITHELIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN IMMOBILIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; ANIMAL; HEAT SHOCK RESPONSE; HUMAN; LENS; METABOLISM; PHYSIOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; WESTERN BLOTTING;

ANIMALS; BLOTTING, WESTERN; CATTLE; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EYE PROTEINS; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HUMANS; INTERMEDIATE FILAMENT PROTEINS; LENS, CRYSTALLINE; MALTOSE; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; VIMENTIN;

EID: 0032587169     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (53)

1. de Jong WW, Leunissen JAM, Voorter CEM. Evolution of the α-crystallin/small heat-shock protein family. Mol Biol Evol. 1993;10:103-126.
2. Groenen PJTA, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone α-crystallin. Eur J Biochem. 1994;225:1-19.
3. Wistow GJ, Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem. 1988;55:479-504.
4. Bhat SP, Nagineni CN. αB subunit of lens specific protein α-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun. 1989;158:319-325.
5. Bhat SP, Horwitz J, Srinivasan A, Ding L. αB-crystallin exists as an independent protein in the heart and in the lens. Eur J Biochem. 1991;202:775-781.
6. Dubin RA, Wawrousek EF, Piatigorsky J. Expression of the murine αB-crystallin gene is not restricted to the lens. Mol Cell Biol. 1989;9:1083-1091.
7. Iwaki T, Kume-Iwaki A, Liem RKH, Goldman JE. αB-Crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell. 1989;57:71-78.
8. Kato K, Shinohara H, Kurobe N, Goto S, Inaguma Y, Ohshima K. Immunoreactive αA-crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim Biophys Acta. 1991;1080:173-180.
9. Kato K, Shinohara H, Goto S, Inaguma Y, Morishita R, Asano T. Copurification of small heat shock protein with αB-crystallin from human skeletal muscle. J Biol Chem. 1992;267:7718-7725.
10. Lee DC, Kim RY, Wistow GJ. Avian αB-Crystallin: non-lens expression and sequence similarities with both small (Hsp27) and large (Hsp70) heat shock proteins. J Mol Biol. 1993;232:1221-1226.
11. Longoni S, Lattonen S, Bullock G, Chiesi M. Cardiac α-crystallin. Mol Cell Biochem. 1990;97:113-120.
12. Nagineni CN, Bhat SP. αB-crystallin is expressed in kidney epithelial cell lines and not in fibroblasts. FEBS Lett. 1989;249:89-94.
13. Srinivasan AN, Nagineni CN, Bhat SP. αA-crystallin is expressed in non-ocular tissues. J Biol Chem. 1992;267:23337-23441.
14. Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci USA. 1982;79:2360-2364.
15. Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem. 1993;268:1517-1520.
16. Merck KB, Groenen PJ, Voorter CE, et al. Structural and functional similarities of bovine α-crystallin and mouse small heat-shock protein. A family of chaperones. J Biol Chem. 1993;268:1046-1052.
17. Horwitz J. α-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992;89:10449-10453.
18. Aoyama A, Frohli K, Schafer R, Klemenz R. αB-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection. Mol Cell Biol. 1993;13:1824-1835.
19. Rao PV, Horwitz J, Zigler JS Jr. Chaperone-like activity of α-crystallin. The effect of NADPH on its interaction with zeta-crystallin. J Biol Chem. 1994;269:13266-13272.
20. Rao PV, Huang QL, Horwitz J, Zigler JS Jr. Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta. 1995;1245:439-447.
21. Wang K, Spector A. The chaperone activity of bovine α-crystallin. Interaction with other crystalline in native and denatured states. J Biol Chem. 1994;269:13601-13608.
22. Wang K, Spector A. α-crystallin can act as a chaperone under conditions of oxidative stress. Invest Ophthalmol Vis Sci. 1995; 36:311-321.
23. Ganea E, Harding JJ. Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by α-crystallin, a chaperone-like protein. Biochem Biophys Res Commun. 1996;222:626-631.
24. Hook DWA, Harding JJ. α-Crystallin acting as a molecular chaperone protects catalase against steroid-induced inactivation. FEBS Lett. 1996;382:281-284.
25. Plater ML, Goode D, Crabbe MJC. Effects of site-directed mutations on the chaperone-like activity of αB-crystallin. J Biol Chem. 1996; 271:28558-28566.
26. Muchowski PJ, Bassuk JA, Lubsen NH, Clark JI. Human αB-crystallin. Small heat shock protein and molecular chaperone. J Biol Chem. 1997;272:2578-2582.
27. Muchowski PJ, Clark JI. ATP-enhanced molecular chaperone functions of the small heat shock protein human αB crystallin. Proc Natl Acad Sci USA. 1998;95:1004-1009.
28. Sun TX, Das BK, Liang JJN. Conformational and functional differences between recombinant human lens αA-and αB-crystallin J Biol Chem. 1997;272:6220-6225.
29. Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin FEBS Lett. 1995;369:521-325.
30. Carter JM, Hutcheson AM, Quinlan RA. In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with α-crystallin but not with vimentin. Exp Eye Res. 1995;60:181-192.
31. Djabali K, de Nechaud B, Landon F, Portier MM. αB-Crystallin interacts with intermediate filaments in response to stress. J Cell Sci. 1997;110:2759-2769.
32. Nicholl ID, Quinlan RA. Chaperone activity of α-crystallins modulates intermediate filament assembly EMBO J. 1994;13:945-953.
33. Wang K, Spector A. α-Crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation-dependent manner. Eur J Biochem. 1996;242:56-66.
34. Iwaki T, Iwaki A, Tateishi J, Goldman JE. Sense and anti-sense modification of glial αB-crystallin production results in alterations of stress fiber formation and thermoresistance. J Cell Biol. 1994; 125:1385-1393.
35. Wisniewski T, Goldman JE. αB-Crystallin is associated with intermediate filaments in astrocytonia cells, Neurochem Res. 1998;23: 385-392.
36. Clark JI. Development and maintenance of lens transparency. In: Albert DM, Jakobiec FA, eds. Principles and Practice of Ophthalmology. Philadelphia: WB Saunders; 1994:114-123.
37. Benedek GB. Theory of transparency of the eye. Appl Opt. 1971; 10:459-473.
38. Spector A. The search for a solution to senile cataract. Invest Ophthalmol Vis Sci. 1984;25:130-146.
39. Matsushima H, David LL, Hiraoka T, Clark JI. Loss of cytoskeletal proteins and lens cell opacification in the selenite cataract model. Exp Eye Res. 1997;64:387-395.
40. Bova MP, Ding LL, Horwitz J, Fung BKK. Subunit exchange of αA-crystallin. J Biol Chem. 1997;272:29511-29517.
41. Sun TX, Liang JJN. Intermolecular exchange and stabilization of recombinant human αA-and αB-crystallin. J Biol Chem. 1998;273: 286-290.
42. Buchner J. Supervising the fold: functional principles of molecular chaperones. FASEB J. 1996;10:10-19.
43. Alcala J, Maisel H. Biochemistry of lens plasma membrane and cytoskeleton. In: Maisel H, ed. The Ocular Lens. New York: Marcel Dekker; 1985:169-222.
44. Capetanaki Y, Smith S, Heath JP. Over-expression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation. J Cell Biol. 1989;109:1653-1664.
45. Tumminia SJ, Jonak GJ, Focht RJ, Cheng YSE, Russell P. Cataractogenesis in transgenic mice containing the HIV-1 protease linked to the lens αa-crystallin promoter. J Biol Chem. 1996;271:425-431.
46. Welch WJ, Suhan JP. Morphological study of the mammalian stress response: characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat-shock treatment. J Cell Biol. 1985;101:1198-1211.
47. Renkawek K, de Jong WW, Merck KB, Frenken CW, van Workum FP, Bosman GJ. αB-crystallin is present in reactive glia in Creutzfeldt-Jakob disease. Acta Neuropathol (Berl). 1992;83: 324-327.
48. Renkawek K, Voorter CE, Bosman GJ, van Workum FP, de Jong WW. Expression of αB-crystallin in Alzheimer's disease. Acta Neuropathol (Berl). 1994;87:155-160.
49. Shinohara H, Inaguma Y, Goto S, Inagaki T, Kato K. αB-Crystallin and Hsp28 are enhanced in the cerebral cortex of patients with Alzheimer's disease. J Neurol Sci. 1993;119:203-208.
50. van Noort JM, van Sechel AC, Bajramovic JJ, et al. The small heat-shock protein αB-crystallin as a candidate autoantigen in multiple sclerosis. Nature. 1995;375:798-801.
51. Chiesi M, Longoni S, Limbruno U. Cardiac α-crystallin: Involvement during heart ischemia. Mol Cell Biochem. 1990;97:129-136.
52. Gopalakrishnan S, Takemoto L. Binding of actin to lens α-crystallin. Curr Eye Res. 1992;11:929-933.
53. Gu J, Emerman M, Sandemeyer S. sHsp suppression of Vpr-induced cytoskeletal defects in budding yeast. Mol Cell Biol. 1997;17:4033-4042.