Oxidative stress and steroid resistance in asthma and COPD: pharmacological manipulation of HDAC-2 as a therapeutic strategy

Bibliography

• ADCOCK IM, LANE SJ: Corticosteroid-insensitive asthma: molecular mechanisms. J. Endocrinol. (2003) 178:347-355.
   PubMed Web of Science ®Google Scholar
• ITO K, CHUNG KF, ADCOCK IM: Update on glucocorticoid action and resistance. J. Allergy Clin. Immunol. (2006) 117:522-543.
   PubMed Web of Science ®Google Scholar
• ALSAEEDI A, SIN DD, MCALISTER FA: The effects of inhaled corticosteroids in chronic obstructive pulmonary disease: a systematic review of randomized placebo-controlled trials. Am. J. Med. (2002) 113:59-65.
   PubMed Web of Science ®Google Scholar
• HOGG JC, CHU F, UTOKAPARCH S et al.: The nature of small-airway obstruction in chronic obstructive pulmonary disease. N. Engl. J. Med. (2004) 350:2645-2653.
   PubMed Web of Science ®Google Scholar
• CHAKRABORTI S, CHAKRABORTI T: Oxidant-mediated activation of mitogen- activated protein kinases and nuclear transcription factors in the cardiovascular system: a brief overview. Cell. Signal. (1998) 10:675-683.
   PubMed Web of Science ®Google Scholar
• HADDAD JJ: Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors. Cell. Signal. (2002) 14:879-897.
   PubMed Web of Science ®Google Scholar
• MOSSMAN BT, LOUNSBURY KM, REDDY SP: Oxidants and signalling by mitogen-activated protein kinases in lung epithelium. Am. J. Respir. Cell Mol. Biol. (2006) 34:666-669.
   PubMed Web of Science ®Google Scholar
• CHURCH DF, PRYOR WA: Free-radical chemistry of cigarette smoke and its toxicological implications. Environ. Health Perspect. (1985) 64:111-126.
   PubMed Web of Science ®Google Scholar
• TATUM AJ, SHAPIRO GG: The effects of outdoor air pollution and tobacco smoke on asthma. Immunol. Allergy. Clin. North Am. (2005) 25:15-30.
   PubMed Web of Science ®Google Scholar
• MORRISON D, RAHMAN I, LANNAN S, MACNEE W: Epithelial permeability, inflammation, and oxidant stress in the air spaces of smokers. Am. J. Respir. Crit. Care Med. (1999) 159:473-479.
   PubMed Web of Science ®Google Scholar
• RAHMAN I: Oxidative stress in pathogenesis of chronic obstructive pulmonary disease: cellular and molecular mechanisms. Cell. Biochem. Biophys. (2005) 43:167-188.
   PubMed Web of Science ®Google Scholar
• DOORN JA, PETERSEN DR: Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Chem. Res. Toxicol. (2002) 15:1445-1450.
   PubMed Web of Science ®Google Scholar
• GUTTERIDGE JMC, HALLIWELL B: Free radicals and antioxidants in the year 2000: a historical look to the future. Ann. NY. Acad. Sci (2000) 899:136-147.
   PubMed Web of Science ®Google Scholar
• HADDAD JJ: Redox and oxidant-mediated regulation of apoptosis signalling pathways: immuno-pharmaco-redox conception of oxidative siege versus cell death commitment. Int. Immunopharmacol. (2004) 4:475-493.
   PubMed Web of Science ®Google Scholar
• VAN DER VAART H, POSTMA DS, TIMENS W, TEN HACKEN NHT: Acute effects of cigarette smoke on inflammation and oxidative stress: a review. Thorax (2004) 59:713-721.
   PubMed Web of Science ®Google Scholar
• KIRKHAM PA, SPOONER G, RAHMAN I, ROSSI AG: Macrophage phagocytosis of apoptotic neutrophils is compromised by matrix proteins modified by cigarette smoke and lipid peroxidation products. Biochem. Biophys. Res. Commun. (2004) 318:32-37.
   PubMed Web of Science ®Google Scholar
• UCHIDA K, SHIRAISHI M, NAITO Y et al.: Activation of stress signalling pathways by the end product of lipid peroxidation. 4-Hydroxy-2-nonenal is a potential inducer of intracellular peroxide production. J. Biol. Chem. (1999) 274:2234-2242.
   PubMed Web of Science ®Google Scholar
• RAHMAN I, MACNEE W: Oxidative stress and regulation of glutathione in lung inflammation. Eur. Respir. J. (2000) 16:534-554.
   PubMed Web of Science ®Google Scholar
• GUYTON KZ, LIU Y, GOROSPE M, XU Q, HOLBROOK NJ: Activation of mitogen-activated protein kinase by H2O2. J. Biol. Chem. (1996) 271:4138-4142.
   PubMed Web of Science ®Google Scholar
• BARTHEL A, KLOTZ LO: Phosphoinositide 3-kinase signalling in the cellular response to oxidative stress. Biol. Chem. (2005) 386:207-216.
   PubMed Web of Science ®Google Scholar
• RAHMAN I, MACNEE W: Role of transcription factors in inflammatory lung diseases. Thorax (1998) 53:601-612.
   PubMed Web of Science ®Google Scholar
• MARWICK JA, KIRKHAM PA, STEVENSON CS et al.: Cigarette smoke alters chromatin remodeling and induces pro-inflammatory genes in rat lungs. Am. J. Respir. Cell Mol. Biol. (2004) 31:633-642.
   PubMed Web of Science ®Google Scholar
• BARNES PJ, SHAPIRO SD, PAUWELS RA: Chronic obstructive pulmonary disease: molecular and cellular mechanisms. Eur. Respir. J. (2003) 22:672-688.
   PubMed Web of Science ®Google Scholar
• BARNES PJ: Mediators of chronic obstructive pulmonary disease. Pharmacol. Rev. (2004) 56:515-548.
   PubMed Web of Science ®Google Scholar
• CHUNG KF: Cytokines as targets in chronic obstructive pulmonary disease. Curr. Drug Targets (2006) 7:675-681.
   PubMed Web of Science ®Google Scholar
• BARNES PJ: Inhaled corticosteroids are not beneficial in chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. (2000) 161:342-344.
   PubMedGoogle Scholar
• RAHMAN I, MACNEE W: Role of oxidants/antioxidants in smoking-induced lung diseases. Free Rad. Biol. Med. (1996) 21:669-681.
   PubMed Web of Science ®Google Scholar
• CARAMORI G, PAPI A: Oxidants and asthma. Thorax (2004) 59:170-173.
   PubMed Web of Science ®Google Scholar
• CHALMERS GW, MACLEOD KJ, LITTLE SA et al.: Influence of cigarette smoking on inhaled corticosteroid treatment in mild asthma. Thorax (2002) 57:226-230.
   PubMed Web of Science ®Google Scholar
• ADCOCK IM, ITO K: Steroid resistance in asthma: a major problem requiring novel solutions or a non-issue? Curr. Opin. Pharmacol. (2004) 4:257-262.
   PubMed Web of Science ®Google Scholar
• LEUNG DYM, BLOOM JW: Update on glucocorticoid action and resistance. J. Allergy Clin. Immunol. (2003) 111:3-22.
   PubMed Web of Science ®Google Scholar
• HAYASHI R, WADA H, ITO K, ADCOCK IM: Effects of glucocorticoids on gene transcription. Eur. J. Pharmacol. (2004) 500:51-62.
   PubMed Web of Science ®Google Scholar
• GRUNSTEIN M: Histone acetylation in chromatin structure and transcription. Nature (1997) 389:349-352.
   PubMed Web of Science ®Google Scholar
• STRUHL K: Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. (1998) 12:599-606.
   PubMed Web of Science ®Google Scholar
• CHEUNG P, ALLIS CD, SASSONE-CORSI P: Signalling to chromatin through histone modifications. Cell (2000) 103:263-271.
   PubMed Web of Science ®Google Scholar
• MUEGGE K: Preparing the target for the bullet. Nat. Immunol. (2002) 3:16-17.
   Google Scholar
• JENUWEIN T, ALLIS CD: Translating the histone code. Science (2001) 293:1074-1080.
   PubMed Web of Science ®Google Scholar
• MELLOR J: It takes a PHD to read the histone code. Cell (2006) 126:22-24.
   PubMed Web of Science ®Google Scholar
• PAZIN MJ, KADONAGA JT: What’s up and down with histone deacetylation and transcription? Cell (1997) 89:325-328.
   PubMed Web of Science ®Google Scholar
• JOHNSON CA, TURNER BM: Histone deacetylases: complex transducers of nuclear signals. Sem. Cell Dev. Biol. (1999) 10:179-188.
   PubMed Web of Science ®Google Scholar
• FINNIN MS, DONIGIAN JR, COHEN A et al.: Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature (1999) 401:188-193.
   PubMed Web of Science ®Google Scholar
• DE RUIJTER AJ, VAN GENNIP AH, CARON HN, KEMP S, VAN KUILENBURG AB: Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. (2003) 370:737-749.
   PubMed Web of Science ®Google Scholar
• SEALY L, CHALKLEY R: DNA associated with hyperacetylated histone is preferentially digested by DNase I. Nucleic Acid Res. (1978) 5:1863-1876.
   PubMed Web of Science ®Google Scholar
• VIDALI G, BOFFA LC, BRADBURY EM, ALLFREY VG: Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences. Proc. Natl. Acad. Sci. USA (1978) 75:2239-2243.
   PubMed Web of Science ®Google Scholar
• HEBBES TR, THORNE AW, CRANE-ROBINSON C: A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. (1988) 7:1395-1402.
   PubMed Web of Science ®Google Scholar
• HASSIG CA, FLEISCHER TC, BILLIN AN, SCHREIBER SL, AYER DE: Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell (1997) 89:341-347.
   PubMed Web of Science ®Google Scholar
• LAHERTY CD, YANG WM, SUN JM et al.: Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell (1997) 89:349-356.
   PubMed Web of Science ®Google Scholar
• TONG JK, HASSIG CA, SCHNITZLER GR, KINGSTON RE, SCHREIBER SL: Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature (1998) 395:917-921.
   PubMed Web of Science ®Google Scholar
• ZHANG Y, LEROY G, SEELIG HP, LANE WS, REINBERG D: The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell (1998) 95:279-289.
   PubMed Web of Science ®Google Scholar
• YOU A, TONG JK, GROZINGER CM, SCHREIBER SL: CoREST is an integral component of the Co. Proc. Natl. Acad. Sci. USA (2001) 98:1454-1458.
   PubMed Web of Science ®Google Scholar
• CRESS WD, SETO E: Histone deacetylases, transcriptional control, and cancer. J. Cell Physol. (2000) 184:1-16.
   PubMed Web of Science ®Google Scholar
• HUI NG H, BIRD A: Histone deacetylases: silencers for hire. Trends Biochem. Sci. (2000) 25:121-126.
   Google Scholar
• ITO K, LIM S, CARAMORI G et al.: Cigarette smoking reduces histone deacetylase 2 expression, enhances cytokine expression, and inhibits glucocorticoid actions in alveolar macrophages. FASEB J. (2001) 15:1110-1112.
   PubMedGoogle Scholar
• ITO K, ITO M, ELLIOTT WM et al.: Decreased histone deacetylase activity in chronic obstructive pulmonary disease. N. Engl. J. Med. (2005) 352:1967-1976.
   PubMed Web of Science ®Google Scholar
• ITO K, CARAMORI G, LIM S et al.: Expression and activity of histone deacetylases in human asthmatic airways. Am. J. Respir. Crit. Care Med. (2002) 166:392-396.
   PubMed Web of Science ®Google Scholar
• COSIO BG, MANN B, ITO K et al.: Histone acetylase and deacetylase activity in alveolar macrophages and blood mononocytes in asthma. Am. J. Respir. Crit. Care Med. (2004) 170:141-147.
   PubMed Web of Science ®Google Scholar
• HEW M, BHAVSAR P, TORREGO A et al.: Relative corticosteroid insensitivity of peripheral blood mononuclear cells in severe asthma. Am. J. Respir. Crit. Care Med. (2006) 174:134-141.
   PubMed Web of Science ®Google Scholar
• UCHIDA K, KANEMATSU M, SAKAI K et al.: Protein-bound acrolein: potential markers for oxidative stress. Proc. Natl. Acad. Sci. USA (1998) 95:4882-4887.
   PubMed Web of Science ®Google Scholar
• ISCHIROPOULOS H: Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun. (2003) 305:776-783.
   PubMed Web of Science ®Google Scholar
• ITO K, HANAZAWA T, TOMITA K, BARNES PJ, ADCOCK IM: Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration. Biochem. Biophys. Res. Commun. (2004) 315:240-245.
   PubMed Web of Science ®Google Scholar
• YANG SR, CHIDA AS, BAUTER MR et al.: Cigarette smoke induces pro-inflammatory cytokine release by activation of NF-κB and post-translational modifications of histone deacetylase in macrophages. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) 291:L46-L57.
   PubMed Web of Science ®Google Scholar
• KARIN M: New twists in gene regulation by glucocorticoid receptor: is DNA binding dispensable? Cell (1998) 93:487-490.
   PubMed Web of Science ®Google Scholar
• YAN K, KUDO A, HIRANO H et al.: Subcellular localization of glucocorticoid receptor protein in the human kidney glomerulus. Kidney Int. (1999) 56:65-73.
   PubMedGoogle Scholar
• ITO K, YAMAMURA S, ESSILFIE-QUAYE S et al.: Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-κB suppression. J. Exp. Med. (2006) 203:7-13.
   PubMed Web of Science ®Google Scholar
• WANG JC, DERYNCK MK, NONAKA DF et al.: Chromatin immunoprecipitation (ChIP) scanning identifies primary glucocorticoid receptor target genes. Proc. Natl. Acad. Sci. USA (2004) 101:15603-15608.
   PubMed Web of Science ®Google Scholar
• SCHAAF MJM, LEWIS-TUFFIN LJ, CIDLOWSKI JA: Ligand-selective targeting of the glucocorticoid receptor to nuclear subdomains is associated with decreased receptor mobility. Mol. Endocrinol. (2005) 19:1501-1515.
   PubMedGoogle Scholar
• SCHACKE H, DOCKE WD, ASADULLAH K: Mechanisms involved in the side effects of glucocorticoids. Pharmacol. Ther. (2002) 96:23-43.
   PubMed Web of Science ®Google Scholar
• GLASS CK, OGAWA S: Combinatorial roles of nuclear receptors in inflammation and immunity. Nat. Rev. Immunol. (2006) 6:44-55.
   PubMed Web of Science ®Google Scholar
• BARNES PJ, KARIN M: Nuclear factor-κB – a pivotal transcription factor in chronic inflammatory diseases. N. Engl. J. Med. (1997) 336:1066-1071.
   PubMed Web of Science ®Google Scholar
• ROSENFELD MG, GLASS CK: Coregulator codes of transcriptional regulation by nuclear receptors. J. Biol. Chem. (2001) 276:36865-36868.
   PubMed Web of Science ®Google Scholar
• ITO K, BARNES PJ, ADCOCK IM: Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1β-induced histone H4 acetylation on lysines 8 and 12. Mol. Cell. Biol. (2000) 20:6891-6903.
   PubMed Web of Science ®Google Scholar
• SACCANI S, NATOLI G: Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes. Genes Dev. (2002) 16:2219-2224.
   PubMed Web of Science ®Google Scholar
• KAGOSHIMA M, WILCKE T, ITO K et al.: Glucocorticoid-mediated transrepression is regulated by histone acetylation and DNA methylation. Eur. J. Pharmacol (2001) 429:327-334.
   PubMed Web of Science ®Google Scholar
• RIDER LG, HIRASAWA N, SANTINI F, BEAVEN MA: Activation of the mitogen-activated protein kinase cascade is suppressed by low concentrations of dexamethasone in mast cells. J. Immunol. (1996) 157:2374-2380.
   PubMedGoogle Scholar
• SWANTEK JL, COBB MH, GEPPERT TD: Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumour necrosis factor α (TNF-α) translation: glucocorticoids inhibit TNF-α translation by blocking JNK/SAPK. Mol. Cell. Biol. (1997) 17:6274-6282.
   PubMed Web of Science ®Google Scholar
• CAELLES C, GONZALEZ-SANCHO JM, MUNOZ A: Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway. Genes Dev. (1997) 11:3351-3364.
   PubMed Web of Science ®Google Scholar
• HIRASAWA N, SATO Y, FUJITA Y, MUE S, OHUCHI K: Inhibition by dexamethasone of antigen-induced c-Jun N-terminal kinase activation in rat basophilic leukaemia cells. J. Immunol. (1998) 161:4939-4943.
   PubMedGoogle Scholar
• LASA M, BROOK M, SAKLATVALA J, CLARK AR: Dexamethasone destabilizes COX-2 mRNA by inhibiting mitogen-activated protein kinase p38. Mol. Cell. Biol. (2001) 21:771-780.
   PubMed Web of Science ®Google Scholar
• KASSEL O, SANCONO A, KRATZSCHMAR J et al.: Glucocorticoids inhibit MAPK via increased expression and decreased degradation of MKP-1. EMBO J. (2001) 20:7108-7116.
   PubMed Web of Science ®Google Scholar
• LASA M, ABRAHAM SM, BOUCHERON C, SAKLATVALA J, CLARK AR: Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38. Mol. Cell. Biol. (2002) 22:7802-7811.
   PubMed Web of Science ®Google Scholar
• NISSEN RM, YAMAMOTO KR: The glucocorticoid receptor inhibits NFκB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. (2000) 14:2314-2329.
   PubMed Web of Science ®Google Scholar
• LUECKE HF, YAMAMOTO KR: The glucocorticoid receptor blocks P-TEFb recruitment by NFκB to effect promoter-specific transcriptional repression. Genes Dev. (2005) 19:1116-1127.
   PubMed Web of Science ®Google Scholar
• BILODEAU S, VALLETTE-KASIC S, GAUTHIER Y et al.: Role of Brg1 and HDAC2 in GR trans-repression of the pituitary POMC gene and misexpression in Cushing disease. Genes Dev. (2006) 20:2871-2886.
   PubMed Web of Science ®Google Scholar
• ADCOCK IM, ITO K: Glucocorticoid pathways in chronic obstructive pulmonary disease therapy. Proc. Am. Thorac. Soc. (2005) 2:313-319.
   PubMedGoogle Scholar
• ITO K, LIM S, CARAMORI G et al.: A molecular mechanism of action of theophylline: Induction of histone deacetylase activity to decrease inflammatory gene expression. Proc. Natl. Acad. Sci. USA (2002) 99:8921-8926.
   PubMed Web of Science ®Google Scholar
• UKENA D, HARNEST U, SAKALAUSKAS R et al.: Comparison of addition of theophylline to inhaled steroid with doubling of the dose of inhaled steroid in asthma. Eur. Respir. J. (1997) 10:2754-2760.
   PubMed Web of Science ®Google Scholar
• EVANS DJ, TAYLOR DA, ZETTERSTROM O et al.: A comparison of low-dose inhaled budesonide plus theophylline and high-dose inhaled budesonide for moderate asthma. N. Engl. J. Med. (1997) 337:1412-1418.
   PubMed Web of Science ®Google Scholar
• KIDNEY J, DOMINGUEZ M, TAYLOR PM et al.: Immunomodulation by theophylline in asthma. Demonstration by withdrawal of therapy. Am. J. Respir. Crit. Care Med. (1995) 151:1907-1914.
   PubMedGoogle Scholar
• PFLUM MK, TONG JK, LANE WS, SCHREIBER SL: Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. (2001) 276:47733-47741.
   PubMed Web of Science ®Google Scholar
• TSAI SC, SETO E: Regulation of histone deacetylase 2 by protein kinase CK2. J. Biol. Chem. (2002) 277:31826-31833.
   PubMed Web of Science ®Google Scholar
• CHANG S, BEZPROZVANNAYA S, LI S, OLSON EN: An expression screen reveals modulators of class II histone deacetylase phosphorylation. Proc. Natl. Acad. Sci. USA (2005) 102:8120-8125.
   PubMed Web of Science ®Google Scholar
• KRAMER OH, ZHU P, OSTENDORFF HP et al.: The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2. EMBO J. (2003) 22:3411-3420.
   PubMed Web of Science ®Google Scholar
• TOURNIER C, WHITMARSH AJ, CAVANAGH J, BARRETT T, DAVIS RJ: Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase. Proc. Natl. Acad. Sci. USA (1997) 94:7337-7342.
   PubMed Web of Science ®Google Scholar
• SZATMARY Z, GARABEDIAN MJ, VILCEK J: Inhibition of glucocorticoid receptor-mediated transcriptional activation by p38 mitogen-activated protein (MAP) kinase. J. Biol. Chem. (2004) 279:43708-43715.
   PubMed Web of Science ®Google Scholar
• SOUSA AR, LANE SJ, SOH C, LEE TH: In vivo resistance to corticosteroids in bronchial asthma is associated with enhanced phosyphorylation of JUN N-terminal kinase and failure of prednisolone to inhibit JUN N-terminal kinase phosphorylation. J. Allergy Clin. Immunol. (1999) 104:565-574.
   PubMed Web of Science ®Google Scholar
• LOKE TK, MALLETT KH, RATOFF J et al.: Systemic glucocorticoid reduces bronchial mucosal activation of activator protein 1 components in glucocorticoid-sensitive but not glucocorticoid-resistant asthmatic patients. J. Allergy Clin. Immunol. (2006) 118:368-375.
   PubMed Web of Science ®Google Scholar
• IRUSEN E, MATTHEWS JG, TAKAHASHI A et al.: p38 Mitogen-activated protein kinase-induced glucocorticoid receptor phosphorylation reduces its activity: Role in steroid-insensitive asthma. J. Allergy Clin. Immunol. (2002) 109:649-657.
   PubMed Web of Science ®Google Scholar
• TSITOURA DC, ROTHMAN PB: Enhancement of MEK/ERK signalling promotes glucocorticoid resistance in CD4+ T cells. J. Clin. Invest. (2004) 113:619-627.
   PubMed Web of Science ®Google Scholar
• LI LB, GOLEVA E, HALL CF, OU LS, LEUNG DYM: Superantigen-induced corticosteroid resistance of human T cells occurs through activation of the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (MEK-ERK) pathway. J. Allergy Clin. Immunol. (2004) 114:1059-1069.
   PubMed Web of Science ®Google Scholar
• BARNES PJ: How corticosteroids control inflammation: Quintiles Prize Lecture 2005. Br. J. Pharmacol. (2006) 148:245-254.
   PubMed Web of Science ®Google Scholar
• COSIO BG, TSAPROUNI L, ITO K et al.: Theophylline restores histone deacetylase activity and steroid responses in COPD macrophages. J. Exp. Med. (2004) 200:689-695.
   PubMed Web of Science ®Google Scholar
• KIRKHAM PA, MEJA K, MARWICK JA: Pharmacological induction of HDAC activity restores steroid function in macrophages subject to oxidative stress. Eur. Respir. J. (2005) 26:214s-214s.
   Google Scholar
• KIRKHAM PA, MEJA K, BAUTER MR, RAHMAN I: Curcumin restores glucocorticoid function and inhibits cigarette smoke-mediated IL-8 release in oxidant stressed monocytic U937 cells. Eur. Respir. J. (2005) 26:215s-215s.
   Google Scholar
• FOUKAS LC, DANIELE N, KTORI C et al.: Direct effects of caffeine and theophylline on p110δ and other phosphoinositide 3-kinases. Differential effects on lipid kinase and protein kinase activities. J. Biol. Chem. (2002) 277:37124-37130.
   PubMed Web of Science ®Google Scholar
• IWATA K, TOMITA K, SANO H et al.: Trichostatin A, a histone deacetylase inhibitor, downregulates interleukin-12 transcription in SV-40-transformed lung epithelial cells. Cell. Immunol. (2002) 218:26-33.
   PubMedGoogle Scholar
• GLOZAK MA, SENGUPTA N, ZHANG X, SETO E: Acetylation and deacetylation of non-histone proteins. Gene (2005) 363:15-23.
   PubMed Web of Science ®Google Scholar
• ADCOCK IM: Histone deacetylase inhibitors as novel anti-inflammatory agents. Curr. Opin. Investig. Drugs (2006) 7:966-973.
   Google Scholar
• CHUNG YL, LEE MY, WANG AJ, YAO LF: A therapeutic strategy uses histone deacetylase inhibitors to modulate the expression of genes involved in the pathogenesis of rheumatoid arthritis. Mol. Ther. (2003) 8:707-717.
   PubMed Web of Science ®Google Scholar
• CHOI JH, OH SW, KANG MS et al.: Trichostatin A attenuates airway inflammation in mouse asthma model. Clin. Exp. Allergy (2005) 35:89-96.
   PubMed Web of Science ®Google Scholar
• MORADEI O, MAROUN CR, PAQUIN I, VAISBURG A: Histone deacetylase inhibitors: latest developments, trends and prospects. Curr. Med. Chem. Anti-Cancer Agents (2005) 5:529-560.
   PubMedGoogle Scholar
• SPEARS M, MCSHARRY C, THOMSON NC: Peroxisome proliferator-activated receptor-γ agonists as potential anti-inflammatory agents in asthma and chronic obstructive pulmonary disease. Clin. Exp. Allergy (2006) 36:1494-1504.
   PubMed Web of Science ®Google Scholar
• ANNICOTTE JS, IANKOVA I, MIARD S et al.: Peroxisome proliferator-activated receptor γ regulates E-cadherin expression and inhibits growth and invasion of prostate cancer. Mol. Cell. Biol. (2006) 26:7561-7574.
   PubMed Web of Science ®Google Scholar
• CHANG TH, SZABO E: Enhanced growth inhibition by combination differentiation therapy with ligands of peroxisome proliferator-activated receptor-γ and inhibitors of histone deacetylase in adenocarcinoma of the lung. Clin. Cancer Res. (2002) 8:1206-1212.
   PubMed Web of Science ®Google Scholar
• HRZENJAK A, MOINFAR F, KREMSER ML et al.: Valproate inhibition of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells. Mol. Cancer Ther. (2006) 5:2203-2210.
   PubMed Web of Science ®Google Scholar
• GIANNINI R, CAVALLINI A: Expression analysis of a subset of coregulators and three nuclear receptors in human colorectal carcinoma. Anti-Cancer Res. (2005) 25:4287-4292.
   PubMed Web of Science ®Google Scholar
• ZHU P, MARTIN E, MENGWASSER J et al.: Induction of HDAC2 expression upon loss of APC in colorectal tumourigenesis. Cancer Cell (2004) 5:455-463.
   PubMed Web of Science ®Google Scholar
• SONG JAEH, NOH JH, LEE JH et al.: Increased expression of histone deacetylase 2 is found in human gastric cancer. APMIS (2005) 113:264-268.
   PubMed Web of Science ®Google Scholar
• ROPERO S, FRAGA MF, BALLESTAR E et al.: A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition. Nat. Genet. (2006) 38:566-569.
   PubMed Web of Science ®Google Scholar