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Herve M Blottiere - One of the best experts on this subject based on the ideXlab platform.
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butyrAte And TrichostAtin A effects on the proliferAtion differentiAtion of humAn intestinAl epitheliAl cells induction of cyclin d3 And p21 expression
Gut, 2000Co-Authors: Samila Siavoshian, Jeanpierre Segain, M Kornprobst, C Bonnet, C Cherbut, J P Galmiche, Herve M BlottiereAbstract:BACKGROUND—Sodium butyrAte, A product of colonic bActeriAl fermentAtion, is Able to inhibit cell proliferAtion And to stimulAte cell differentiAtion of colonic epitheliAl cell lines. It hAs been proposed thAt these cellulAr effects could be linked to its Ability to cAuse hyperAcetylAtion of histone through the inhibition of histone deAcetylAse. AIM—To AnAlyse the moleculAr mechAnisms of butyrAte Action on cell proliferAtion/differentiAtion And to compAre them with those of TrichostAtin A, A well known inhibitor of histone deAcetylAse. METHODS—HT-29 cells were grown in the Absence or presence of butyrAte or TrichostAtin A. Cell proliferAtion And cell cycle distribution were studied After DNA stAining by crystAl violet And propidium iodide respectively. Cell cycle regulAtory proteins were studied by western blot And reverse trAnscription-polymerAse chAin reAction. Cell differentiAtion wAs followed by meAsuring brush border enzyme Activities. Histone AcetylAtion wAs studied by Acid/ureA/Triton AcrylAmide gel electrophoresis. RESULTS—ButyrAte blocked cells mAinly in the G1 phAse of the cell cycle, whereAs TrichostAtin A wAs inhibitory in both G1 And G2 phAses. ButyrAte inhibited the mRNA expression of cyclin D1 without Affecting its protein expression And stimulAted the protein expression of cyclin D3 without Affecting its mRNA expression. TrichostAtin A showed similAr effects on cyclin D1 And D3. ButyrAte And TrichostAtin A stimulAted p21 expression both At the mRNA And protein levels, whereAs their effects on the expression of cyclin dependent kinAses were slightly different. Moreover, butyrAte strongly stimulAted the Activity of AlkAline phosphAtAse And dipeptidyl peptidAse IV, whereAs TrichostAtin A hAd no effect. FinAlly, A six hour exposure to butyrAte or TrichostAtin A induced histone H4 hyperAcetylAtion. At 15 And 24 hours, histone H4 remAined hyperAcetylAted in the presence of butyrAte, whereAs it returned to control levels in the presence of TrichostAtin A. CONCLUSIONS—The dAtA mAy explAin how butyrAte Acts on cell proliferAtion/differentiAtion, And they show thAt TrichostAtin A does not reproduce every effect of butyrAte, mAinly becAuse of its shorter hAlf life. Keywords: butyrAte; cyclin D; p21; TrichostAtin A; colonic epitheliAl cells; histone AcetylAtion
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ButyrAte And TrichostAtin A effects on the proliferAtion/differentiAtion of humAn intestinAl epitheliAl cells: induction of cyclin D3 And p21 expression
Gut, 2000Co-Authors: Samila Siavoshian, Jeanpierre Segain, C Bonnet, C Cherbut, Kornprobst M, Galmiche Jp, Herve M BlottiereAbstract:BACKGROUND—Sodium butyrAte, A product of colonic bActeriAl fermentAtion, is Able to inhibit cell proliferAtion And to stimulAte cell differentiAtion of colonic epitheliAl cell lines. It hAs been proposed thAt these cellulAr effects could be linked to its Ability to cAuse hyperAcetylAtion of histone through the inhibition of histone deAcetylAse. AIM—To AnAlyse the moleculAr mechAnisms of butyrAte Action on cell proliferAtion/differentiAtion And to compAre them with those of TrichostAtin A, A well known inhibitor of histone deAcetylAse. METHODS—HT-29 cells were grown in the Absence or presence of butyrAte or TrichostAtin A. Cell proliferAtion And cell cycle distribution were studied After DNA stAining by crystAl violet And propidium iodide respectively. Cell cycle regulAtory proteins were studied by western blot And reverse trAnscription-polymerAse chAin reAction. Cell differentiAtion wAs followed by meAsuring brush border enzyme Activities. Histone AcetylAtion wAs studied by Acid/ureA/Triton AcrylAmide gel electrophoresis. RESULTS—ButyrAte blocked cells mAinly in the G1 phAse of the cell cycle, whereAs TrichostAtin A wAs inhibitory in both G1 And G2 phAses. ButyrAte inhibited the mRNA expression of cyclin D1 without Affecting its protein expression And stimulAted the protein expression of cyclin D3 without Affecting its mRNA expression. TrichostAtin A showed similAr effects on cyclin D1 And D3. ButyrAte And TrichostAtin A stimulAted p21 expression both At the mRNA And protein levels, whereAs their effects on the expression of cyclin dependent kinAses were slightly different. Moreover, butyrAte strongly stimulAted the Activity of AlkAline phosphAtAse And dipeptidyl peptidAse IV, whereAs TrichostAtin A hAd no effect. FinAlly, A six hour exposure to butyrAte or TrichostAtin A induced histone H4 hyperAcetylAtion. At 15 And 24 hours, histone H4 remAined hyperAcetylAted in the presence of butyrAte, whereAs it returned to control levels in the presence of TrichostAtin A. CONCLUSIONS—The dAtA mAy explAin how butyrAte Acts on cell proliferAtion/differentiAtion, And they show thAt TrichostAtin A does not reproduce every effect of butyrAte, mAinly becAuse of its shorter hAlf life. Keywords: butyrAte; cyclin D; p21; TrichostAtin A; colonic epitheliAl cells; histone AcetylAtion
Jun Lu - One of the best experts on this subject based on the ideXlab platform.
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vitAmin d stimulAtes Apoptosis in gAstric cAncer cells in synergy with TrichostAtin A sodium butyrAte induced And 5 AzA 2 deoxycytidine induced pten upregulAtion
FEBS Journal, 2010Co-Authors: Ammar F Matloob, Baiqu Huang, Juan Du, Zhixiong Dong, Jing Zhao, Yu Feng, Yun Zhong, Jun LuAbstract:Previous studies hAve shown An AnticAncer effect of vitAmin D, but the mechAnisms underlying this Action hAve not been fully explored. Here we show thAt 1,25-dihydroxyvitAmin D3 (VD3, the Active form of vitAmin D) significAntly promoted Apoptosis in the undifferentiAted gAstric cAncer cell line HGC-27, And this wAs AccompAnied by A concurrent increAse in phosphAtAse And tensin homolog deleted on chromosome 10 (PTEN) expression on VD3 treAtment. In contrAst, knockdown of PTEN expression by stAble trAnsfection of PTEN smAll interfering RNA greAtly decreAsed the Apoptosis rAte. We further demonstrAted thAt VD3 induced PTEN expression through vitAmin D receptor. In Addition, our evidence showed thAt vitAmin D receptor, Egr-1 And p300 induced PTEN expression in A synergistic fAshion. Furthermore, we found thAt the histone deAcetylAse inhibitors TrichostAtin A And sodium butyrAte And the methylAtion inhibitor 5-AzA-2′-deoxycytidine plAyed importAnt roles in vitAmin D-induced Apoptosis through PTEN upregulAtion. The dAtA presented in this Article suggest potentiAl benefits of vitAmin D in gAstric cAncer therApies in AssociAtion with the use of TrichostAtin A/sodium butyrAte And 5-AzA-2′-deoxycytidine. Structured digitAl AbstrAct • MINT-7306489, MINT-7306501, MINT-7306512: P300 (uniprotkb:Q09472) physicAlly interActs (MI:0914) with VDR (uniprotkb:P11473) And EGR1 (uniprotkb:P18146) by Anti bAit coimmunoprecipitAtion (MI:0006)
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TrichostAtin A Extends the LifespAn of DrosophilA melAnogAster by ElevAting hsp22 Expression
Acta Biochimica et Biophysica Sinica, 2004Co-Authors: Jun Lu, Yanmei Zhao, Zhi-gen Yuan, Xiaoxue Li, Baiqu HuangAbstract:The level of AcetylAtion of histones in nucleosomes is relAted to the longevity of yeAst And AnimAls. However, the mechAnisms by which AcetylAtion And deAcetylAtion Affect longevity remAin uncleAr. In present study, we investigAted the influence of histone AcetylAtion modificAtion on the expression of hsp22 gene And the lifespAn in DrosophilA melAnogAster using histone deAcetylAse (HDAC) inhibitor TrichostAtin A (TSA). The results showed thAt TSA could extend the lifespAn of DrosophilA melAnogAster. Furthermore, TSA significAntly promoted the hsp22 gene trAnscription, And Affected the chromAtin morphology At the locus of hsp22 gene Along the polytene chromosome. Present dAtA implicAte thAt TSA mAy Affect the lifespAn of DrosophilA through chAnging the level of histone AcetylAtion And influencing the expression of hsp22 gene thAt is relAted to Aging.
Samila Siavoshian - One of the best experts on this subject based on the ideXlab platform.
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butyrAte And TrichostAtin A effects on the proliferAtion differentiAtion of humAn intestinAl epitheliAl cells induction of cyclin d3 And p21 expression
Gut, 2000Co-Authors: Samila Siavoshian, Jeanpierre Segain, M Kornprobst, C Bonnet, C Cherbut, J P Galmiche, Herve M BlottiereAbstract:BACKGROUND—Sodium butyrAte, A product of colonic bActeriAl fermentAtion, is Able to inhibit cell proliferAtion And to stimulAte cell differentiAtion of colonic epitheliAl cell lines. It hAs been proposed thAt these cellulAr effects could be linked to its Ability to cAuse hyperAcetylAtion of histone through the inhibition of histone deAcetylAse. AIM—To AnAlyse the moleculAr mechAnisms of butyrAte Action on cell proliferAtion/differentiAtion And to compAre them with those of TrichostAtin A, A well known inhibitor of histone deAcetylAse. METHODS—HT-29 cells were grown in the Absence or presence of butyrAte or TrichostAtin A. Cell proliferAtion And cell cycle distribution were studied After DNA stAining by crystAl violet And propidium iodide respectively. Cell cycle regulAtory proteins were studied by western blot And reverse trAnscription-polymerAse chAin reAction. Cell differentiAtion wAs followed by meAsuring brush border enzyme Activities. Histone AcetylAtion wAs studied by Acid/ureA/Triton AcrylAmide gel electrophoresis. RESULTS—ButyrAte blocked cells mAinly in the G1 phAse of the cell cycle, whereAs TrichostAtin A wAs inhibitory in both G1 And G2 phAses. ButyrAte inhibited the mRNA expression of cyclin D1 without Affecting its protein expression And stimulAted the protein expression of cyclin D3 without Affecting its mRNA expression. TrichostAtin A showed similAr effects on cyclin D1 And D3. ButyrAte And TrichostAtin A stimulAted p21 expression both At the mRNA And protein levels, whereAs their effects on the expression of cyclin dependent kinAses were slightly different. Moreover, butyrAte strongly stimulAted the Activity of AlkAline phosphAtAse And dipeptidyl peptidAse IV, whereAs TrichostAtin A hAd no effect. FinAlly, A six hour exposure to butyrAte or TrichostAtin A induced histone H4 hyperAcetylAtion. At 15 And 24 hours, histone H4 remAined hyperAcetylAted in the presence of butyrAte, whereAs it returned to control levels in the presence of TrichostAtin A. CONCLUSIONS—The dAtA mAy explAin how butyrAte Acts on cell proliferAtion/differentiAtion, And they show thAt TrichostAtin A does not reproduce every effect of butyrAte, mAinly becAuse of its shorter hAlf life. Keywords: butyrAte; cyclin D; p21; TrichostAtin A; colonic epitheliAl cells; histone AcetylAtion
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ButyrAte And TrichostAtin A effects on the proliferAtion/differentiAtion of humAn intestinAl epitheliAl cells: induction of cyclin D3 And p21 expression
Gut, 2000Co-Authors: Samila Siavoshian, Jeanpierre Segain, C Bonnet, C Cherbut, Kornprobst M, Galmiche Jp, Herve M BlottiereAbstract:BACKGROUND—Sodium butyrAte, A product of colonic bActeriAl fermentAtion, is Able to inhibit cell proliferAtion And to stimulAte cell differentiAtion of colonic epitheliAl cell lines. It hAs been proposed thAt these cellulAr effects could be linked to its Ability to cAuse hyperAcetylAtion of histone through the inhibition of histone deAcetylAse. AIM—To AnAlyse the moleculAr mechAnisms of butyrAte Action on cell proliferAtion/differentiAtion And to compAre them with those of TrichostAtin A, A well known inhibitor of histone deAcetylAse. METHODS—HT-29 cells were grown in the Absence or presence of butyrAte or TrichostAtin A. Cell proliferAtion And cell cycle distribution were studied After DNA stAining by crystAl violet And propidium iodide respectively. Cell cycle regulAtory proteins were studied by western blot And reverse trAnscription-polymerAse chAin reAction. Cell differentiAtion wAs followed by meAsuring brush border enzyme Activities. Histone AcetylAtion wAs studied by Acid/ureA/Triton AcrylAmide gel electrophoresis. RESULTS—ButyrAte blocked cells mAinly in the G1 phAse of the cell cycle, whereAs TrichostAtin A wAs inhibitory in both G1 And G2 phAses. ButyrAte inhibited the mRNA expression of cyclin D1 without Affecting its protein expression And stimulAted the protein expression of cyclin D3 without Affecting its mRNA expression. TrichostAtin A showed similAr effects on cyclin D1 And D3. ButyrAte And TrichostAtin A stimulAted p21 expression both At the mRNA And protein levels, whereAs their effects on the expression of cyclin dependent kinAses were slightly different. Moreover, butyrAte strongly stimulAted the Activity of AlkAline phosphAtAse And dipeptidyl peptidAse IV, whereAs TrichostAtin A hAd no effect. FinAlly, A six hour exposure to butyrAte or TrichostAtin A induced histone H4 hyperAcetylAtion. At 15 And 24 hours, histone H4 remAined hyperAcetylAted in the presence of butyrAte, whereAs it returned to control levels in the presence of TrichostAtin A. CONCLUSIONS—The dAtA mAy explAin how butyrAte Acts on cell proliferAtion/differentiAtion, And they show thAt TrichostAtin A does not reproduce every effect of butyrAte, mAinly becAuse of its shorter hAlf life. Keywords: butyrAte; cyclin D; p21; TrichostAtin A; colonic epitheliAl cells; histone AcetylAtion
Teruhiko Beppu - One of the best experts on this subject based on the ideXlab platform.
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TrichostAtin A And trApoxin novel chemicAl probes for the role of histone AcetylAtion in chromAtin structure And function
BioEssays, 1995Co-Authors: Minoru Yoshida, Sueharu Horinouchi, Teruhiko BeppuAbstract:Reversible AcetylAtion At the ϵ-Amino group of lysines locAted At the conserved domAin of core histones is supposed to plAy An importAnt role in the regulAtion of chromAtin structure And its trAnscriptionAl Activity. One promising strAtegy for AnAlyzing the precise function of histone AcetylAtion is to block the Activities of AcetylAting or deAcetylAting enzymes by specific inhibitors. Recently, two microbiAl metAbolites, TrichostAtin A And trApoxin, were found to be potent inhibitors of histone deAcetylAses. TrichostAtin A reversibly inhibits the mAmmAliAn histone deAcetylAse, whereAs trApoxin cAuses inhibition through irreversible binding to the enzyme. The histone deAcetylAse from A TrichostAtin A-resistAnt cell line is resistAnt to TrichostAtin A, indicAting thAt the enzyme is the primAry tArget. Both of the Agents induce A vAriety of biologicAl responses of cells such As induction of differentiAtion And cell cycle Arrest. TrichostAtin A And trApoxin Are useful in AnAlyzing the role of histone AcetylAtion in chromAtin structure And function As well As in determining the genes whose Activities Are regulAted by histone AcetylAtion.
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structurAl specificity for biologicAl Activity of TrichostAtin A A specific inhibitor of mAmmAliAn cell cycle with potent differentiAtion inducing Activity in friend leukemiA cells
The Journal of Antibiotics, 1990Co-Authors: Minoru Yoshida, Yutaka Hoshikawa, Koshi Koseki, Kenji Mori, Teruhiko BeppuAbstract:BiologicAl Activities of four chemicAlly synthesized TrichostAtin-relAted compounds, (R)-TrichostAtin A, (S)-trichostAtm A, (R)-trichostAtic Acid, And (S)-trichostAtic Acid, were investigAted. AssAys of differentiAtion-inducing Activity in Friend leukemiA cells And G2-Arresting Activity in the cell cycle of normAl rAt fibroblAst cells were used As monitoring systems for compAring the bioActivities of these compounds. The results cleArly showed thAt both of the enAntiomers of trichostAtic Acid hAd no Activity in both the AssAy systems. In the cAse of (S)-TrichostAtin A, the Antipode of nAturAlly occurring TrichostAtin A, 50% effective concentrAtions were determined to be 50-70-fold higher thAn those of (R)-TrichostAtin A. The relAtionship between this rAtio And the vAlue of enAntiomeric excess strongly suggests thAt (S)-TrichostAtin A is Also biologicAlly inActive. These results indicAte thAt the Absolute configurAtion And the presence of the hydroxAmAte group of TrichostAtin A Are essentiAl for its biologicAl Activity.
Yungjue Bang - One of the best experts on this subject based on the ideXlab platform.
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the histone deAcetylAse inhibitor TrichostAtin A sensitizes estrogen receptor α negAtive breAst cAncer cells to tAmoxifen
Oncogene, 2004Co-Authors: Eun Ryoung Jang, Gajin Jeong, Yungjue BangAbstract:The histone deAcetylAse inhibitor TrichostAtin A sensitizes estrogen receptor α -negAtive breAst cAncer cells to tAmoxifen
