Heat shock protein 27 expression in human proximal tubule cells exposed to lethal and sublethal concentrations of CdCl2

Environmental Health Perspectives

Volumn 107, Issue 7, 1999, Pages 545-552

  Somji, Seema ^a   Sens, Donald A ^a   Garrett, Scott H ^a   Sens, Mary Ann ^a   Todd, John H ^a,b  

^a WEST VIRGINIA UNIVERSITY   (United States)

^b WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

Cadmium; Gene expression; Heart shock; Heavy metals; Hsp 27; Proximal tubule; Sodium arsenite

Indexed keywords

CADMIUM CHLORIDE; HEAT SHOCK PROTEIN 27; MESSENGER RNA;

ARTICLE; CELL CULTURE; CONTROLLED STUDY; HEAT STRESS; HUMAN; HUMAN CELL; KIDNEY PROXIMAL TUBULE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; STRESS;

EUKARYOTA;

EID: 0032797963     PISSN: 00916765     EISSN: None     Source Type: Journal    
DOI: 10.1289/ehp.99107545     Document Type: Article

References (39)

1. Bernard A, Roels H, Hubermont G, Buchet JP, Masson PL, Lauwerys R. Characterization of the proteinuria in Cd exposed workers. Int Arch Occup Environ Health 38:19-30 (1976).
2. Kido T, Honda R, Tsuritani I, Yamada H, Ishizaki M, Yamada Y, Nogawa K. Progress of renal dysfunction in inhabitants environmentally exposed to cadmium. Arch Environ Health 43:213-217 (1988).
3. Piscator M. Proteinuria in chronic cadmium poisoning. Arch Environ Health 5:325-328 (1962).
4. Lauwerys R, Buchet JP, Roels H, Brouwers J, Stanescu D. Epidemiological survey of workers exposed to cadmium: effect of lung, kidney and several biological indices. Arch Environ Health 28:145-148 (1974).
5. Gonich HC, Indraprasit S, Rosen VJ, Neustein H, Van de Velde R, Raghavan SRV. Effect of cadmium on renal tubular function, the ATP-Na-ATPase transport system and renal tubular ultrastructure. Mineral Electrol Metab 3:21-35 (1980).
6. Kinter LB, Short BG. Anatomy and physiology of the kidney. In: Toxicology of the Kidney (Hook JB, Goldstein RS, ads). New York:Raven Press, 1993;1-36.
7. Bosco E, Porta N, Diezi J. Renal handling of cadmium: a study by tubular microinjections. Arch Toxicol 7:371-373 (1986).
8. Detrisac CJ, Sens MA, Garvin AJ, Spicer SS, Sens DA. Tissue culture of human kidney epithelial cells of proximal tubule origin. Kidney Int 25:383-390 (1984).
9. Todd JH, McMartin K, Sens DA. Enzymatic isolation and serum-free culture of human renal cells retaining properties of proximal tubule cells. In: Methods in Molecular Medicine. Human Cell Culture Protocols (Jones GE, ed). Totowa, NJ:Humana Press, 1996;431-436.
10. Sens DA, Detrisac CJ, Sens MA, Rossi MR, Wenger SL, Todd JH. Tissue culture of human renal epithelial cells using a defined serum-free growth formulation. Exper Nephrol (in press).
11. Hazen-Martin DJ, Sens DA, Blackburn JG, Sens MA. Cadmium nephrotoxicity in human proximal tubule cell cultures. In Vitro Cell Dev Biol 25:784-790 (1989).
12. Hazen-Martin DJ, Sens DA, Blackburn JG, Flath MC, Sens MA. An electrophysiological and freeze fracture assessment of cadmium nephrotoxicity in vitro. In Vitro Cell Dev Biol 25:791-799 (1989).
13. Hazen-Martin DJ, Todd JH, Sens MA, Khan W, Bylander JE, Smyth BJ, Sens DA. Electrical and freeze-fracture analysis of the effects of ionic cadmium on the cell membrane of human proximal tubule cells. Environ Health Perspect 101:510-516 (1993).
14. Hoey JG, Garrett SH, Sens MA, Todd JH, Sens DA. Expression of MT-3 mRNA in human kidney, proximal tubule cell cultures, and renal cell carcinoma. Toxicol Lett 92:149-160 (1997).
15. 2+ induces metallothionein protein accumulation, but not metallothionein isoform 2 mRNA. Environ Health Perspect 106:587-595 (1998).
16. Garrett SH, Somji S, Todd JH, Sens, MA, Sens DA. Differential expression of human metallothionein isoform I mRNAs in human proximal tubule cells exposed to metals. Environ Health Perspect 106:825-832 (1998).
17. Aufricht C, Ardito T, Thulin G, Kashgarian M, Sieger NJ, Van Why SK. Heat-shock protein 25 induction and redistribution during actin reorganization after renal ischemia. Am J Physiol 274:F215-F222 (1998).
18. Schober A, Müller E, Thurau K, Beck FX. The response of heat shock proteins 25 and 72 to ischaemia in different kidney zones. Pfluegers Arch Eur J Physiol 434:292-299 (1997).
19. Schober A, Burger-Kentischer A, Müller E, Beck FX. Effect of ischemia on localization of heat shock protein 25 in kidney. Kidney Int 54:S174-S176 (1998).
20. Welch W. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 72:1063-1081 (1992).
21. Georgopoulos C, Welch WJ. Role of the major heat shock proteins as molecular chaperones. Annu Rev Cell Biol 9:601-634 (1993).
22. Ciocca DR, Oesterreich S, Chamness GC, McGuire WL, Fuqua SAW. Biological and clinical implications of heat shock protein 27000 (Hsp 27): a review. J Natl Cancer Inst 85:1558-1570 (1993).
23. Huot J, Houle F, Spitz DR, Landry J. Hsp 27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res 56:273-279 (1996).
24. Lavoie J, Gingras-Breton G, Tanguay RM, Landry J. Induction of Chinese hamster hsp 27 gene expression in mouse cells confers resistance to heat shock. Hsp 27 stabilization of microfilament organization. J Biol Chem 268:3420-3429 (1993).
25. Lavoie JN, Hickey E, Weber LA, Landry J. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J Biol Chem 268:24210-24214 (1993).
26. Landry J, Chretien P, Lambert J, Hickey E, Weber LA. Heat shock resistance conferred by expression of the human hsp 27 gene in rodent cells. J Cell Biol 109:7-15 (1989).
27. Huot J, Roy G, Lambert H, Chretien P, Landry J. Increased survival after treatment with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res 51:5245-5252 (1991).
28. Lavoie JN, Lambert H, Hickey E, Weber LA, Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 15:505-516 (1995).
29. Kampinga HH, Luppes JG, Konings AW. Heat-induced nuclear protein binding and its relation to thermal cytotoxicity. Int J Hyperthermia 3:459-465 (1987).
30. Mehlen P, Preville X, Chareyron P, Briolay J, Klemenz R, Arrigo A-P. Constitutive expression of human hsp 27, Drosophila hsp 27, or human αβ-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity by stably transfected murine L929 fibroblasts. J Immunol 154:363-374 (1995).
31. Miron T, Vancompernolle K, Vanderkerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol 114:256-261 (1991).
32. Arrigo A-P, Landry J. Expression and function of the low-molecular-weight heat shock proteins. In: The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto R, Tissieres A, Georgopoulos C, eds). New York:Cold Spring Harbor Laboratory Press, 1994;335-373.
33. Arrigo A-P. Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. Cell 379:19-26 (1998).
34. Mehlen P, Schulze-Osthoff K, Arrigo A-P. Small stress proteins as novel regulators of apoptosis. J Biol Chem 271:16510-16514 (1996).
35. Samali A, Cotter TG. Heat shock proteins increase resistance to apoptosis. Exp Cell Res 223:163-170 (1996).
36. Molitoris BA. Putting the actin cytoskeleton into perspective: pathophysiology of ischemic alterations. Am J Physiol 272:F430-F433 (1997).
37. Boonstra JG, Van Der Voude FJ, Wever PC, Laterveer JC, Daha MR, Van Kooten C. Expression and function of Fas (CD95) on human renal tubular epithelial cells. J Am Soc Nephrol 8:1517-1524 (1997).
38. Sens D. Personal communication.
39. Wu W, Welsh MJ. Expression of the 25-kDa heat shock protein (HSP 27) correlates with resistance to the toxicity of cadmium chloride, mercuric chloride, cis-platinum (II)-diamine dichloride, or sodium arsenite in mouse embryonic stem cells transfected with sense or antisense hsp 27 cDNA. Toxicol Appl Pharmacol 141:330-339 (1996).