HSP72 inhibits smad3 activation and nuclear translocation in renal epithelial-to-mesenchymal transition

Journal of the American Society of Nephrology

Volumn 21, Issue 4, 2010, Pages 598-609

  Zhou, Yi ^a   Mao, Haiping ^a   Li, Shu ^a   Cao, Shirong ^a   Li, Zhijian ^a   Zhuang, Shougang ^b   Fan, Jinjin ^a   Dong, Xiuqing ^a   Borkan, Steven C ^c   Wang, Yihan ^d   Yu, Xueqing ^a  

^a SUN YAT SEN UNIVERSITY   (China)

^b BROWN UNIVERSITY   (United States)

^c BOSTON MEDICAL CENTER   (United States)

^d Laboratory for Kidney Pathology Inc ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 72; SMAD PROTEIN; SMAD2 PROTEIN; SMAD3 PROTEIN; TEPRENONE; TRANSFORMING GROWTH FACTOR BETA1;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; KIDNEY EPITHELIUM; KIDNEY INTERSTITIUM; KIDNEY TUBULE CELL; MALE; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; RAT; URETER OBSTRUCTION;

EID: 77950605687     PISSN: 10466673     EISSN: 15333450     Source Type: Journal    
DOI: 10.1681/ASN.2009050552     Document Type: Article

References (34)

1. Massague J, Blain SW, Lo RS: TGFbeta signaling in growth control, cancer, and heritable disorders. Cell 103: 295-309, 2000
2. Blobe GC, Schiemann WP, Lodish HF: Role of transforming growth factor beta in human disease. N Engl J Med 342: 1350-1358, 2000
3. Macias-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL: MADR2 is a substrate of the TGFbeta receptor and its phosphor-ylation is required for nuclear accumulation and signaling. Cell 87: 1215-1224, 1996
4. Chen HB, Rud JG, Lin K, Xu L: Nuclear targeting of transforming growth factor-beta-activated Smad complexes. J Biol Chem 280: 21329-21336, 2005
5. Ross S, Hill CS: How the Smads regulate transcription. Int J Biochem Cell Biol 40: 383-408, 2008
6. Hill CS: Nucleocytoplasmic shuttling of Smad proteins. Cell Res 19: 36-46, 2009
7. Zeisberg M, Kalluri R: The role of epithelial-to-mesenchymal transition in renal fibrosis. J Mol Med 82: 175-181, 2004
8. Hartl FU: Molecular chaperones in cellular protein folding. Nature 381: 571-579, 1996
9. Bukau B, Horwich AL: The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366, 1998
10. Mao H, Li Z, Zhou Y, Li Z, Zhuang S, An X, Zhang B, Chen W, Nie J, Wang Z, Borkan SC, Wang Y, Yu X: HSP72 attenuates renal tubular cell apoptosis and interstitial fibrosis in obstructive nephropathy. Am J Physiol Renal Physiol 295: F202-F214, 2008
11. Ruchalski K, Mao H, Li Z, Wang Z, Gillers S, Wang Y, Mosser DD, Gabai V, Schwartz JH, Borkan SC: Distinct hsp70 domains mediate apopto-sis-inducing factor release and nuclear accumulation. J Biol Chem 281: 7873-7880, 2006
12. Knowlton AA: Mutation of amino acids 246-251 alters nuclear accumulation of human heat shock protein (HSP) 72 with stress, but does not reduce viability. J Mol Cell Cardiol 31: 523-532, 1999
13. Knowlton AA: Mutation of amino acids 566-572 (KKKVLDK) inhibits nuclear accumulation of heat shock protein 72 after heat shock. J Mol Cell Cardiol 33: 49-55, 2001
14. Chow AM, Steel R, Anderson RL: Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis. Cell Stress Chaperones 14: 253-263, 2009
15. Mosser DD, Caron AW, Bourget L, Meriin AB, Sherman MY, Morimoto RI, Massie B: The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol Cell Biol 20: 7146-7159, 2000
16. Stege GJ, Li L, Kampinga HH, Konings AW, Li GC: Importance of the ATP-binding domain and nucleolar localization domain of HSP72 in the protection of nuclear proteins against heat-induced aggregation. Exp Cell Res 214: 279-284, 1994
17. Tang D, Kang R, Xiao W, Jiang L, Liu M, Shi Y, Wang K, Wang H, Xiao X: Nuclear heat shock protein 72 as a negative regulator of oxidative stress (hydrogen peroxide)-induced HMGB1 cytoplasmic translocation and release. J Immunol 178: 7376-7384, 2007
18. Voss MR, Gupta S, Stice JP, Baumgarten G, Lu L, Tristan JM, Knowlton AA: Effect of mutation of amino acids 246-251 (KRKHKK) in HSP72 on protein synthesis and recovery from hypoxic injury. Am J Physiol Heart Circ Physiol 289: H2519-H2525, 2005
19. Shi Y, Thomas JO: The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol Cell Biol 12: 2186-2192, 1992
20. Beckmann RP, Mizzen LE, Welch WJ: Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248: 850-854, 1990
21. Healy DA, Daly PJ, Docherty NG, Murphy M, Fitzpatrick JM, Watson RW: Heat shock-induced protection of renal proximal tubular epithelial cells from cold storage and rewarming injury. J Am Soc Nephrol 17: 805-812, 2006
22. Margarit SM, Sondermann H, Hall BE, Nagar B, Hoelz A, Pirruccello M, Bar-Sagi D, Kuriyan J: Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112: 685-695, 2003
23. Lanneau D, Brunet M, Frisan E, Solary E, Fontenay M, Garrido C: Heat shock proteins: Essential proteins for apoptosis regulation. J Cell Mol Med 12: 743-761, 2008
24. Beck FX, Neuhofer W, Muller E: Molecular chaperones in the kidney: Distribution, putative roles, and regulation. Am J Physiol Renal Physiol 279: F203-F215, 2000
25. Chung J, Nguyen AK, Henstridge DC, Holmes AG, Chan MH, Mesa JL, Lancaster GI, Southgate RJ, Bruce CR, Duffy SJ, Horvath I, Mestril R, Watt MJ, Hooper PL, Kingwell BA, Vigh L, Hevener A, Febbraio MA: HSP72 protects against obesity-induced insulin resistance. Proc Natl Acad Sci USA 105: 1739-1744, 2008
26. Ogawa F, Shimizu K, Hara T, Muroi E, Hasegawa M, Takehara K, Sato S: Serum levels of heat shock protein 70, a biomarker of cellular stress, are elevated in patients with systemic sclerosis: Association with fibro-sis and vascular damage. Clin Exp Rheumatol 26: 659-662, 2008
27. Yaglom JA, Gabai VL, Sherman MY: High levels of heat shock protein Hsp72 in cancer cells suppress default senescence pathways. Cancer Res 67: 2373-2381, 2007
28. Bidmon B, Endemann M, Arbeiter K, Ruffingshofer D, Regele H, Herkner K, Eickelberg O, Aufricht C: Overexpression of HSP-72 confers cytoprotection in experimental peritoneal dialysis. Kidney Int 66: 2300-2307, 2004
29. Wakisaka O, Takahashi N, Shinohara T, Ooie T, Nakagawa M, Yonemochi H, Hara M, Shimada T, Saikawa T, Yoshimatsu H: Hyper-thermia treatment prevents angiotensin II-mediated atrial fibrosis and fibrillation via induction of heat-shock protein 72. J Mol Cell Cardiol 43: 616-626, 2007
30. Hagiwara S, Iwasaka H, Matsumoto S, Noguchi T, Yoshioka H: Association between heat stress protein 70 induction and decreased pulmonary fibrosis in an animal model of acute lung injury. Lung 185: 287-293, 2007
31. Xu J, Lamouille S, Derynck R: TGF-beta-induced epithelial to mesen-chymal transition. Cell Res 19: 156-172, 2009
32. Kee HJ, Eom GH, Joung H, Shin S, Kim JR, Cho YK, Choe N, Sim BW, Jo D, Jeong MH, Kim KK, Seo JS, Kook H: Activation of histone deacetylase 2 by inducible heat shock protein 70 in cardiac hypertrophy. Circ Res 103: 1259-1269, 2008
33. Cizkova D, Rosocha J, Vanicky I, Radonak J, Galik J, Cizek M: Induction of mesenchymal stem cells leads to HSP72 synthesis and higher resistance to oxidative stress. Neurochem Res 31: 1011-1020, 2006
34. Johnson JD, Fleshner M: Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72. J Leukoc Biol 79: 425-434, 2006