Inhibition of histone deacetylase 2 mitigates profibrotic TGF-β1 responses in fibroblasts derived from Peyronie's plaque

Asian Journal of Andrology

Volumn 15, Issue 5, 2013, Pages 640-645

  Ryu, Ji Kan ^a   Kim, Woo Jean ^a   Choi, Min Ji ^a   Park, Jin Mi ^a   Song, Kang Moon ^a   Kwon, Mi Hye ^a   Das, Nando Dulal ^a   Kwon, Ki Dong ^a   Batbold, Dulguun ^a   Yin, Guo Nan ^a   Suh, Jun Kyu ^a  

^a Inha University School of Medicine   (South Korea)

Author keywords

Cell culture; Fibrosis; Histone deacetylase; Peyronie's disease; Transforming growth factor beta

Indexed keywords

ALPHA SMOOTH MUSCLE ACTIN; COLLAGEN TYPE 1; COLLAGEN TYPE 4; FIBRONECTIN; HISTONE DEACETYLASE 2; PLASMINOGEN ACTIVATOR INHIBITOR 1; SCLEROPROTEIN; SMAD2 PROTEIN; SMAD3 PROTEIN; SMALL INTERFERING RNA; TRANSFORMING GROWTH FACTOR BETA1;

ARTICLE; CELL NUCLEUS; CELL TRANSDIFFERENTIATION; DEACETYLATION; ENZYME INHIBITION; EPIGENETIC REPRESSION; EXTRACELLULAR MATRIX; FIBROBLAST; GENE SILENCING; GENETIC TRANSFECTION; HISTONE ACETYLATION; HUMAN; HUMAN CELL; IMMUNOCYTOCHEMISTRY; MALE; MYOFIBROBLAST; PEYRONIE DISEASE; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; RNA INTERFERENCE; TUNICA ALBUGINEA; WESTERN BLOTTING;

CELL TRANSDIFFERENTIATION; CELLS, CULTURED; FIBROBLASTS; GENE KNOCKDOWN TECHNIQUES; HISTONE DEACETYLASE 2; HUMANS; MALE; PENILE INDURATION; RNA, SMALL INTERFERING; SMAD2 PROTEIN; SMAD3 PROTEIN; TRANSFORMING GROWTH FACTOR BETA1;

EID: 84883484788     PISSN: 1008682X     EISSN: 17457262     Source Type: Journal    
DOI: 10.1038/aja.2013.61     Document Type: Article

References (25)

1. Hellstrom WJ, Bivalacqua TJ. Peyronie's disease: Etiology, medical, and surgical therapy. J Androl 2000; 21: 347-54
2. Gholami SS, Gonzalez-Cadavid NF, Lin CS, Rajfer J, Lue TF. Peyronie's disease: A review. J Urol 2003; 169: 1234-41
3. Hauck EW, Diemer T, Schmelz HU, Weidner W. A critical analysis of nonsurgical treatment of Peyronie's disease. Eur Urol 2006; 49: 987-97
4. Kadioglu A, Akman T, Sanli O, Gurkan L, Cakan M et al. Surgical treatment of Peyronie's disease: A critical analysis. Eur Urol 2006; 50: 235-48
5. Gonzalez-Cadavid NF, Magee TR, Ferrini M, Qian A, Vernet D et al. Gene expression in Peyronie's disease. Int J Impot Res 2002; 14: 361-74
6. El-Sakka AI, Hassoba HM, Pillarisetty RJ, Dahiya R, Lue TF. Peyronie's disease is associated with an increase in transforming growth factor-beta protein expression. J Urol 1997; 158: 1391-4
7. Haag SM, Hauck EW, Szardening-Kirchner C, Diemer T, Cha ES et al. Alterations in the transforming growth factor (TGF)-beta pathway as a potential factor in the pathogenesis of Peyronie's disease. Eur Urol 2007; 51: 255-61
8. Piao S, Choi MJ, Tumurbaatar M, Kim WJ, Jin HR et al. Transforming growth factor (TGF)-b type I receptor kinase (ALK5) inhibitor alleviates profibrotic TGF-b1 responses in fibroblasts derived from Peyronie's plaque. J Sex Med 2010; 7: 3385-95
9. Ryu JK, Piao S, Shin HY, Choi MJ, Zhang LW et al. IN-1130, a novel transforming growth factor-beta type I receptor kinase (activin receptor-like kinase 5) inhibitor, promotes regression of fibrotic plaque and corrects penile curvature in a rat model of Peyronie's disease. J Sex Med 2009; 6: 1284-96
10. Pang M, Zhuang S. Histone deacetylase: A potential therapeutic target for fibrotic disorders. J Pharmacol Exp Ther 2010; 335: 266-72
11. McKinsey TA. Targeting inflammation in heart failure with histone deacetylase inhibitors. Mol Med 2011; 17: 434-41
12. Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J Mol Biol 2004; 338: 17-31
13. Hodges SJ, Yoo JJ, Mishra N, Atala A. The effect of epigenetic therapy on congenital neurogenic bladders-A pilot study. Urology 2010; 75: 868-72
14. Qin L, Han YP. Epigenetic repression of matrix metalloproteinases in myofibroblastic hepatic stellate cells through histone deacetylases 4: Implication in tissue fibrosis. Am J Pathol 2010; 177: 1915-28
15. Rombouts K, Niki T, Greenwel P, Vandermonde A, Wielant A et al. Trichostatin A, a histone deacetylase inhibitor, suppresses collagen synthesis and prevents TGF-beta1-induced fibrogenesis in skin fibroblasts. Exp Cell Res 2002; 278: 184-97
16. Noh H, Oh EY, Seo JY, Yu MR, Kim YO et al. Histone deacetylase-2 is a key regulator of diabetes-And transforming growth factor-beta1-induced renal injury. Am J Physiol Renal Physiol 2009; 297: F729-39
17. Hoodless PA, Haerry T, Abdollah S, Stapleton M, O'Connor MB et al. MADR1, a MADrelated protein that functions in BMP2 signaling pathways. Cell 1996; 85: 489-500
18. Marumo T, Hishikawa K, Yoshikawa M, Hirahashi J, Kawachi S et al. Histone deacetylase modulates the pro-inflammatory and fibrotic changes in tubulointerstitial injury. Am J Physiol Renal Physiol 2009; 298: F133-41
19. Ghosh AK, Varga J. The transcriptional coactivator and acetyltransferase p300 in fibroblast biology and fibrosis. J Cell Physiol 2007; 213: 663-71
20. Huber LC, Distler JH, Moritz F, Hemmatazad H, Hauser T et al. Trichostatin A prevents the accumulation of extracellular matrix in a mouse model of bleomycin-induced skin fibrosis. Arthritis Rheum 2007; 56: 2755-64
21. Hemmatazad H, Rodrigues HM, Maurer B, Brentano F, Pileckyte M et al. Histone deacetylase 7, a potential target for the antifibrotic treatment of systemic sclerosis. Arthritis Rheum 2009; 60: 1519-29
22. Glenisson W, Castronovo V, Waltregny D. Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation. Biochim Biophys Acta 2007; 1773: 1572-82
23. Guo W, Shan B, Klingsberg RC, Qin X, Lasky JA. Abrogation of TGFbeta1-induced fibroblast-myofibroblast differentiation by histone deacetylase inhibition. Am J Physiol Lung Cell Mol Physiol 2009; 297: L864-70
24. Pang M, Kothapally J, Mao H, Tolbert E, Ponnusamy M et al. Inhibition of histone deacetylase activity attenuates renal fibroblast activation and interstitial fibrosis in obstructive nephropathy. Am J Physiol Renal Physiol 2009; 297: F996-1005
25. Macías-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L et al. MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 1996; 87: 1215-24