Ignet

Gene Information

Gene symbol: HDAC9

Gene name: histone deacetylase 9

HGNC ID: 14065

Synonyms: KIAA0744, HDAC, MITR, HD7, HDAC7B

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	BCL6	1 hits
3	CD97	1 hits
4	CREB1	1 hits
5	CREBBP	1 hits
6	EGF	1 hits
7	EGFR	1 hits
8	EP300	1 hits
9	FAS	1 hits
10	GATA3	1 hits
11	GCG	1 hits
12	GIP	1 hits
13	GORASP1	1 hits
14	GSK3B	1 hits
15	HDAC1	1 hits
16	HDAC2	1 hits
17	HDAC3	1 hits
18	HDAC4	1 hits
19	HDAC5	1 hits
20	HDAC8	1 hits
21	HIST4H4	1 hits
22	IFNGR2	1 hits
23	IGF1R	1 hits
24	IL4	1 hits
25	IL6R	1 hits
26	INS	1 hits
27	JMJD2C	1 hits
28	KCNB1	1 hits
29	MAPK14	1 hits
30	MARVELD2	1 hits
31	MYEF2	1 hits
32	MYST2	1 hits
33	NCOR1	1 hits
34	NCOR2	1 hits
35	NFKB1	1 hits
36	NR3C1	1 hits
37	PCAF	1 hits
38	PDPK1	1 hits
39	PDX1	1 hits
40	PPARG	1 hits
41	PPARGC1A	1 hits
42	PRKAR2A	1 hits
43	PRKCZ	1 hits
44	PSMD4	1 hits
45	PTEN	1 hits
46	RC3H1	1 hits
47	RPS27A	1 hits
48	RPS6KA5	1 hits
49	RUNX1T1	1 hits
50	SIRT1	1 hits
51	SLC2A4	1 hits
52	TGFA	1 hits
53	TMPRSS11D	1 hits
54	TNF	1 hits
55	TNFRSF10B	1 hits
56	TRIB3	1 hits

Related Sentences

#	PMID	Sentence
1	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
2	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
3	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
4	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
5	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
6	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
7	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
8	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
9	12482846	Selective estrogen receptor modulators (SERMs) show differential effects upon ERalpha activation function 1 (AF-1).
10	12482846	Tamoxifen allows strong ERalpha AF-1 activity, whereas raloxifene allows less and ICI 182,780 (ICI) allows none.
11	12482846	Here, we show that blockade of corepressor histone de-acetylase (HDAC) activity reverses the differential inhibitory effect of SERMs upon AF-1 activity in MCF-7 cells.
12	12482846	This suggests that differential SERM repression of AF-1 involves HDAC-dependent corepressors.
13	12482846	An ERalpha mutation (537X) that increases N-CoR binding in the presence of all SERMs blocks AF-1 activity.
14	12482846	An ERalpha mutation (L379R) that decreases N-CoR binding increases AF-1 activity in the presence of ICI and raloxifene and reverses the effect of the 537X mutation.
15	12482846	The 537X and L379R mutations also alter the ligand preference of ERalpha action at AP-1 sites and C3 complement, an action that also involves AF-1.
16	12482846	Selective estrogen receptor modulators (SERMs) show differential effects upon ERalpha activation function 1 (AF-1).
17	12482846	Tamoxifen allows strong ERalpha AF-1 activity, whereas raloxifene allows less and ICI 182,780 (ICI) allows none.
18	12482846	Here, we show that blockade of corepressor histone de-acetylase (HDAC) activity reverses the differential inhibitory effect of SERMs upon AF-1 activity in MCF-7 cells.
19	12482846	This suggests that differential SERM repression of AF-1 involves HDAC-dependent corepressors.
20	12482846	An ERalpha mutation (537X) that increases N-CoR binding in the presence of all SERMs blocks AF-1 activity.
21	12482846	An ERalpha mutation (L379R) that decreases N-CoR binding increases AF-1 activity in the presence of ICI and raloxifene and reverses the effect of the 537X mutation.
22	12482846	The 537X and L379R mutations also alter the ligand preference of ERalpha action at AP-1 sites and C3 complement, an action that also involves AF-1.
23	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
24	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
25	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
26	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
27	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
28	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
29	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
30	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
31	14976218	Its effects are optimized by various coactivators including histone acetyltransferases (HATs) such as CBP/p300 and p/CAF.
32	14976218	We therefore carried out chromatin immunoprecipitation (ChIP) assays in monocytes to identify 1) chromatin factors bound to the promoters of tumor necrosis factor-alpha (TNF-alpha) and related NF-kappaB-regulated genes under HG or diabetic conditions, 2) specific lysine (Lys (K)) residues on histone H3 (HH3) and HH4 acetylated in this process.
33	14976218	HG treatment of THP-1 monocytes increased the transcriptional activity of NF-kappaB p65, which was augmented by CBP/p300 and p/CAF.
34	14976218	ChIP assays showed that HG increased the recruitment of NF-kappaB p65, CPB, and p/CAF to the TNF-alpha and COX-2 promoters.
35	14976218	Interestingly, ChIP assays also demonstrated concomitant acetylation of HH3 at Lys(9) and Lys(14), and HH4 at Lys(5), Lys(8), and Lys(12) at the TNF-alpha and COX-2 promoters.
36	14976218	Overexpression of histone deacetylase (HDAC) isoforms inhibited p65-mediated TNF-alpha transcription.
37	14976218	Finally, we demonstrated increased HH3 acetylation at TNF-alpha and COX-2 promoters in human blood monocytes from type 1 and type 2 diabetic subjects relative to nondiabetic.
38	15111488	Overexpression of GLUT4 in skeletal muscle enhances whole-body insulin action.
39	15111488	Exercise increases GLUT4 gene and protein expression, and a binding site for the myocyte enhancer factor 2 (MEF-2) is required on the GLUT4 promoter for this response.
40	15111488	In various cell systems, MEF-2 regulation is a balance between transcriptional repression by histone deacetylases (HDACs) and transcriptional activation by the nuclear factor of activated T-cells (NFAT), peroxisome proliferator-activated receptor-gamma coactivator 1 (PGC-1), and the p38 mitogen-activated protein kinase.
41	15111488	After exercise, HDAC5 was dissociated from MEF-2 and exported from the nucleus, whereas nuclear PGC-1 was associated with MEF-2.
42	15111488	Exercise increased total and nuclear p38 phosphorylation and association with MEF-2, without changes in total or nuclear p38 protein abundance.
43	15111488	This result was associated with p38 sequence-specific phosphorylation of MEF-2 and an increase in GLUT4 mRNA.
44	15111488	From these data, it appears that HDAC5, PGC-1, and p38 regulate MEF-2 and could be potential targets for modulating GLUT4 expression.
45	15156183	The 8;21 translocation produces a fusion between the ETO gene and that encoding the myeloid transcription factor AML1.
46	15156183	The AML1-ETO fusion substitutes the majority of the ETO protein for the coregulator recruitment domains of AML1.
47	15156183	Importantly, the proteins interacting with ETO are different from those of wild-type AML1, suggesting that altered coregulator recruitment underlies the oncogenic properties of AML1-ETO.
48	15156183	The list of corepressors capable of binding ETO includes histone deacetylases (HDACs) and components of distinct HDAC core complexes.
49	18385463	Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring.
50	18385463	We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities.
51	18385463	In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities.
52	18385463	Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver.
53	18385463	In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity.
54	18385463	These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation.
55	18385463	Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring.
56	18385463	We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities.
57	18385463	In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities.
58	18385463	Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver.
59	18385463	In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity.
60	18385463	These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation.
61	18464933	The fetal IUGR state was characterized by loss of USF-1 binding at the proximal promoter of Pdx1, recruitment of the histone deacetylase 1 (HDAC1) and the corepressor Sin3A, and deacetylation of histones H3 and H4.
62	18464933	During the neonatal period, these epigenetic changes and the reduction in Pdx1 expression could be reversed by HDAC inhibition.
63	19275684	The enzymes which regulate this modification are described as histone acetyltransferases or HATs, and histone deacetylases or HDACs [1].
64	19553350	Histone deacetylase-2 is a key regulator of diabetes- and transforming growth factor-beta1-induced renal injury.
65	19553350	This study examined the effect of HDAC inhibition on renal fibrosis induced by diabetes or transforming growth factor (TGF)-beta1 and determined the role of reactive oxygen species (ROS) as mediators of HDAC activation.
66	19553350	Among the six HDACs tested (HDAC-1 through -5 and HDAC-8), HDAC-2 activity significantly increased in the kidneys of STZ-induced diabetic rats and db/db mice and TGF-beta1-treated NRK52-E cells.
67	19553350	Levels of mRNA expression of fibronectin and alpha-smooth muscle actin were decreased, whereas E-cadherin mRNA was increased when HDAC-2 was knocked down using RNA interference in NRK52-E cells.
68	19553350	Histone deacetylase-2 is a key regulator of diabetes- and transforming growth factor-beta1-induced renal injury.
69	19553350	This study examined the effect of HDAC inhibition on renal fibrosis induced by diabetes or transforming growth factor (TGF)-beta1 and determined the role of reactive oxygen species (ROS) as mediators of HDAC activation.
70	19553350	Among the six HDACs tested (HDAC-1 through -5 and HDAC-8), HDAC-2 activity significantly increased in the kidneys of STZ-induced diabetic rats and db/db mice and TGF-beta1-treated NRK52-E cells.
71	19553350	Levels of mRNA expression of fibronectin and alpha-smooth muscle actin were decreased, whereas E-cadherin mRNA was increased when HDAC-2 was knocked down using RNA interference in NRK52-E cells.
72	19793100	It has been shown that HDAC4 and 5 co-operatively regulate a number of genes involved in various aspects of metabolism.
73	19793100	The HDACs are also regulated by ubiquitin-mediated proteasomal degradation, although the exact mediators of this process have not been identified. 5.
74	19793100	Together, these data show that HDAC4 and 5 are critical regulators of metabolic gene expression and that understanding their regulation could provide a number of points of intervention for therapies designed to treat metabolic diseases, such as insulin resistance, obesity and Type 2 diabetes.
75	20141611	We report that three novel compounds (THS-73-44, THS-72-5 and THS-78-5) significantly inhibited HDAC activity and increased the acetylation of histone H4 in isolated beta-cells.
76	20175943	Also, EGCG decreased NF-kappaB activity and increased HDAC activity and HDAC-2 expression in Tregs (P < 0.05) in both groups.
77	20175943	IL-10 production and number by suppressing the NF-kappaB signalling pathway via inducing epigenetic changes.
78	20564224	Activities of histone deacetylase (HDAC) and histone acetyltransferase (HAT), and histone acetylation were quantified.
79	20564224	Hyperglycemia activated HDAC and increased HDAC1, 2, and 8 gene expressions in the retina and its capillary cells.
80	20564224	Termination of hyperglycemia failed to provide any benefits to diabetes-induced changes in retinal HDAC and HAT, and histone H3 remained subnormal.
81	20564224	Activities of histone deacetylase (HDAC) and histone acetyltransferase (HAT), and histone acetylation were quantified.
82	20564224	Hyperglycemia activated HDAC and increased HDAC1, 2, and 8 gene expressions in the retina and its capillary cells.
83	20564224	Termination of hyperglycemia failed to provide any benefits to diabetes-induced changes in retinal HDAC and HAT, and histone H3 remained subnormal.
84	20564224	Activities of histone deacetylase (HDAC) and histone acetyltransferase (HAT), and histone acetylation were quantified.
85	20564224	Hyperglycemia activated HDAC and increased HDAC1, 2, and 8 gene expressions in the retina and its capillary cells.
86	20564224	Termination of hyperglycemia failed to provide any benefits to diabetes-induced changes in retinal HDAC and HAT, and histone H3 remained subnormal.
87	20633551	High levels of glucose induce apoptosis in cardiomyocyte via epigenetic regulation of the insulin-like growth factor receptor.
88	20633551	We investigate whether HG-induced repression of insulin-like growth factor 1 receptor (IGF-1R) mediated by epigenetic modifications is one potential mechanism.
89	20633551	We found that HG resulted in decreased IGF-1 receptor (IGF-1R) mRNA levels, and IGF-1R protein when compared with H9C2 rat cardiomyocyte cells incubated in normal glucose.
90	20633551	The effects of HG on reduced expression of IGF-1R and increased apoptosis were blocked by silencing p53 with small interference RNA but not by non-targeting scrambled siRNA.
91	20633551	Moreover, HG negatively regulated IGF-1R promoter activity as determined by ChIP analysis, which was dependent on p53 since siRNA-p53 attenuated the effects of HG on IGF-1R promoter activity.
92	20633551	HG also increased the association of p53 with histone deacetylase 1 (HDAC1), and decreased the association of acetylated histone-4 with the IGF-1R promoter.
93	20633551	Furthermore, HDAC inhibitor relieved the repression of IGF-1R following HG state.
94	20633551	These results suggest that HG-induced repression of IGF-1R is mediated by the association of p53 with the IGF-1R promoter, and by the subsequent enhanced recruitment of chromatin-modifying proteins, such as HDAC1, to the IGF-1R promoter-p53 complex.
95	20633551	In conclusion, our data demonstrate that HG decreases expression of IGF-1R and decreases the association of acetylated histone-4 with the IGF-1R promoter.
96	21274504	Both common forms of diabetes have an inflammatory pathogenesis in which immune and metabolic factors converge on interleukin-1β as a key mediator of insulin resistance and β-cell failure.
97	21274504	In addition to improving insulin resistance and preventing β-cell inflammatory damage, there is evidence of genetic association between diabetes and histone deacetylases (HDACs); and HDAC inhibitors (HDACi) promote β-cell development, proliferation, differentiation and function and positively affect late diabetic microvascular complications.
98	21389970	As EGF signaling is altered by the acetylation status of histone proteins, we measured the effects of the histone deacetylase (HDAC) inhibitor, vorinostat, in mediating renal enlargement in diabetes focusing on the EGF-EGF receptor (EGFR) axis.
99	21389970	Attenuating effects of HDAC inhibition, although multifactorial, are likely to be mediated in part through downregulation of the EGFR.
100	21389970	As EGF signaling is altered by the acetylation status of histone proteins, we measured the effects of the histone deacetylase (HDAC) inhibitor, vorinostat, in mediating renal enlargement in diabetes focusing on the EGF-EGF receptor (EGFR) axis.
101	21389970	Attenuating effects of HDAC inhibition, although multifactorial, are likely to be mediated in part through downregulation of the EGFR.
102	21565617	We show here that in liver, class IIa HDACs (HDAC4, 5, and 7) are phosphorylated and excluded from the nucleus by AMPK family kinases.
103	21565617	In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors.
104	21637537	Trichostatin A, a HDAC inhibitor, reduces the repressive effect of JMJD2C.
105	21637537	In summary, we herein describe JMJD2C-mediated reduction of PPARgamma transcriptional activation as well as preadipocyte differentiation.
106	21708950	HDAC9 deficiency also resulted in increased GATA3 and roquin and decreased BCL6 gene expression.
107	21708950	HDAC9 deficiency was associated with increased site-specific lysine histone acetylation at H3 (H3K9, H3K14, and H3K18) globally that was localized to IL-4, roquin, and peroxisome proliferator-activated receptor-γ promoters with increased gene expression, respectively.
108	21708950	HDAC9 deficiency also resulted in increased GATA3 and roquin and decreased BCL6 gene expression.
109	21708950	HDAC9 deficiency was associated with increased site-specific lysine histone acetylation at H3 (H3K9, H3K14, and H3K18) globally that was localized to IL-4, roquin, and peroxisome proliferator-activated receptor-γ promoters with increased gene expression, respectively.
110	21818121	Glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) are the major incretin hormones that exert insulinotropic and anti-apoptotic actions on pancreatic β-cells.
111	21818121	Overexpression of Kv2.1 in INS-1 β-cells potentiated apoptosis in response to mitochondrial and ER stress and, conversely, co-stimulation with GIP/GLP-1 uncoupled this potentiation, suppressing apoptosis.
112	21818121	In parallel, incretins promoted phosphorylation and acetylation of Kv2.1 via pathways involving protein kinase A (PKA)/mitogen- and stress-activated kinase-1 (MSK-1) and histone acetyltransferase (HAT)/histone deacetylase (HDAC).
113	21818121	Further studies demonstrated that acetylation of Kv2.1 was mediated by incretin actions on nuclear/cytoplasmic shuttling of CREB binding protein (CBP) and its interaction with Kv2.1.
114	21818121	Regulation of β-cell survival by GIP and GLP-1 therefore involves post-translational modifications (PTMs) of Kv channels by PKA/MSK-1 and HAT/HDAC.
115	21818121	Glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) are the major incretin hormones that exert insulinotropic and anti-apoptotic actions on pancreatic β-cells.
116	21818121	Overexpression of Kv2.1 in INS-1 β-cells potentiated apoptosis in response to mitochondrial and ER stress and, conversely, co-stimulation with GIP/GLP-1 uncoupled this potentiation, suppressing apoptosis.
117	21818121	In parallel, incretins promoted phosphorylation and acetylation of Kv2.1 via pathways involving protein kinase A (PKA)/mitogen- and stress-activated kinase-1 (MSK-1) and histone acetyltransferase (HAT)/histone deacetylase (HDAC).
118	21818121	Further studies demonstrated that acetylation of Kv2.1 was mediated by incretin actions on nuclear/cytoplasmic shuttling of CREB binding protein (CBP) and its interaction with Kv2.1.
119	21818121	Regulation of β-cell survival by GIP and GLP-1 therefore involves post-translational modifications (PTMs) of Kv channels by PKA/MSK-1 and HAT/HDAC.
120	21953612	Specific control of pancreatic endocrine β- and δ-cell mass by class IIa histone deacetylases HDAC4, HDAC5, and HDAC9.
121	22020928	To further increase the collaborative effect, the histone deacetylase (HDAC) inhibitor valproic acid (VPA), a known potentiator for PPARγ function, was added to the combinatorial treatment, robustly inducing apoptosis mediated by highly expressed death receptors, including Fas/CD95 and DR5.
122	22086720	Sirtuin 1 (SIRT1): the misunderstood HDAC.
123	22086720	Many of the sirtuin isoforms also deacetylate nonhistone substrates, such as p53 (SIRT1) and α-tubulin (SIRT2).
124	22210316	In the current study, we investigated the importance of histone deacetylase (HDAC)6 for glucocorticoid receptor-mediated effects on glucose metabolism and its potential as a therapeutic target for the prevention of glucocorticoid-induced diabetes.
125	22210316	Dexamethasone-induced hepatic glucose output and glucocorticoid receptor translocation were analyzed in wild-type (wt) and HDAC6-deficient (HDAC6KO) mice.
126	22210316	The effect of the specific HDAC6 inhibitor tubacin was analyzed in vitro. wt and HDAC6KO mice were subjected to 3 weeks' dexamethasone treatment before analysis of glucose and insulin tolerance.
127	22210316	This study demonstrates that HDAC6 is an essential regulator of hepatic glucocorticoid-stimulated gluconeogenesis and impairment of whole-body glucose metabolism through modification of glucocorticoid receptor nuclear translocation.
128	22403301	Insulin-mediated glucose uptake is highly sensitive to the levels of the facilitative glucose transporter protein, GLUT4.
129	22403301	Repression of GLUT4 expression is correlated with insulin resistance in adipose tissue.
130	22403301	We have shown that differentiation-dependent GLUT4 transcription was under control of class II histone deacetylases (HDACs).
131	22403301	Chromatin immunoprecipitation experiments showed the association of HDAC4/5 with the GLUT4 promoter in vivo and in vitro in response to elevated cAMP.
132	22403301	Knockdown of HDACs by small interfering RNA in cultured adipocytes prevented the cAMP-dependent decrease in GLUT4 transcription.
133	22403301	HDAC4/5 recruitment to the GLUT4 promoter was dependent on the GLUT4 liver X receptor (LXR) binding site.
134	22403301	Insulin-mediated glucose uptake is highly sensitive to the levels of the facilitative glucose transporter protein, GLUT4.
135	22403301	Repression of GLUT4 expression is correlated with insulin resistance in adipose tissue.
136	22403301	We have shown that differentiation-dependent GLUT4 transcription was under control of class II histone deacetylases (HDACs).
137	22403301	Chromatin immunoprecipitation experiments showed the association of HDAC4/5 with the GLUT4 promoter in vivo and in vitro in response to elevated cAMP.
138	22403301	Knockdown of HDACs by small interfering RNA in cultured adipocytes prevented the cAMP-dependent decrease in GLUT4 transcription.
139	22403301	HDAC4/5 recruitment to the GLUT4 promoter was dependent on the GLUT4 liver X receptor (LXR) binding site.
140	22427718	Histone deacetylase (HDAC) inhibitor is emphasized as a new class of insulin sensitizer here.
141	22427718	Regulators of SIRT1, CREB, NO, p38, ERK and Cdk5 are discussed in the activation of PPARγ.
142	22638581	This oxidative stress causes the accumulation of reactive oxygen species (ROS) and depletion of reduced glutathione (GSH) that together inhibited histone deacetylases (HDACs) activity, reduced protein levels of HDAC2 and increased acetylation in miR-466h-5p promoter region, which led to the activation of this miRNA.
143	22648458	Acetylation of retinal histones in diabetes increases inflammatory proteins: effects of minocycline and manipulation of histone acetyltransferase (HAT) and histone deacetylase (HDAC).
144	22733364	Co-location of HDAC2 and insulin signaling components in the adult mouse hippocampus.
145	22733364	However, the recent studies indicated that HDAC2, a member of HDACs family, played a role in insulin signaling pathway and synaptic plasticity.
146	22733364	Here, we are concerned about whether HDAC2 was co-located with insulin signaling components in postsynaptic glutamatergic neurons (PSGNs) of the adult mouse hippocampus using double immunofluorescence staining.
147	22733364	The results displayed that HDAC2 was present in PSGNs marked by N-methyl-D-aspartate receptor subunit 2B, in which major components of insulin signaling pathway such as insulin receptor alpha and beta and insulin receptor substrate-1 were also involved.
148	22733364	Accordingly, we speculate that the interaction of HDAC2 and insulin signaling system in PSGNs observed in the present study may serve as a potential mechanism in memory formation.
149	22733364	We hope this could provide a valuable basis for understanding the roles of HDAC2 and insulin on cognitive impairment of diabetes mellitus, involved Alzheimer's disease, which is also called type 3 diabetes recently.
150	23235480	Involvement of p300/CBP and epigenetic histone acetylation in TGF-β1-mediated gene transcription in mesangial cells.
151	23235480	Transforming growth factor-β1 (TGF-β1)-induced expression of plasminogen activator inhibitor-1 (PAI-1) and p21 in renal mesangial cells (MCs) plays a major role in glomerulosclerosis and hypertrophy, key events in the pathogenesis of diabetic nephropathy.
152	23235480	We evaluated the roles of histone acetylation, specific HATs, and HDACs in TGF-β1-induced gene expression in rat mesangial cells (RMCs) and in glomeruli from diabetic mice.
153	23235480	Overexpression of HATs CREB binding protein (CBP) or p300, but not p300/CBP-activating factor, significantly enhanced TGF-β1-induced PAI-1 and p21 mRNA levels as well as transactivation of their promoters in RMCs.
154	23235480	Conversely, they were significantly attenuated by HAT domain mutants of CBP and p300 or overexpression of HDAC-1 and HDAC-5.
155	23235480	Chromatin immunoprecipitation assays showed that TGF-β1 treatment led to a time-dependent enrichment of histone H3-lysine9/14-acetylation (H3K9/14Ac) and p300/CBP occupancies around Smad and Sp1 binding sites at the PAI-1 and p21 promoters.
156	23235480	TGF-β1 also enhanced the interaction of p300 with Smad2/3 and Sp1 and increased Smad2/3 acetylation.
157	23235480	High glucose-treated RMCs exhibited increased PAI-1 and p21 levels, and promoter H3K9/14Ac, which were blocked by TGF-β1 antibodies.
158	23235480	Furthermore, increased PAI-1 and p21 expression was associated with elevated promoter H3K9/14Ac levels in glomeruli from diabetic mice.
159	23235480	Thus TGF-β1-induced PAI-1 and p21 expression involves interaction of p300/CBP with Smads and Sp1, and increased promoter access via p300/CBP-induced H3K9/14Ac.
160	23363995	Dietary components, such as butyrate, sulforaphane, and curcumin, have been shown to affect HAT and HDAC activity, and their health benefits are attributed, at least in part, to epigenetic modifications.
161	23363995	The goal of this review is to highlight the roles of diets and food components in epigenetic modifications through the regulation of HATs and HDACs for disease prevention.
162	23363995	Dietary components, such as butyrate, sulforaphane, and curcumin, have been shown to affect HAT and HDAC activity, and their health benefits are attributed, at least in part, to epigenetic modifications.
163	23363995	The goal of this review is to highlight the roles of diets and food components in epigenetic modifications through the regulation of HATs and HDACs for disease prevention.
164	23771909	The three most significantly upregulated of this group, interleukin 6 receptor (IL6R), histone deacetylase 9 (HDAC9) and CD97 molecule (CD97), were significantly correlated with insulin resistance.
165	23832395	We found that STZ-induced diabetes resulted in decreased hippocampal expression of genes involved in epigenetic regulation and synaptic plasticity, for example, histone deacetylases and glycogen synthase kinase 3 beta (HDACs and GSK3β).
166	23832395	We also found increased expression of genes involved in signalling cascades related to cell growth, cell survival and energy metabolism, such as neurotropic tyrosine kinase receptor type 2, apolipoprotein E, and protein tyrosine phosphatase receptor type (Ntrk2, APOE, PTPRT).
167	23951179	In obesity, high levels of tumor necrosis factor α (TNFα) stimulate lipolysis in adipocytes, leading to hyperlipidemia and insulin resistance.
168	23951179	Previous studies have revealed that in macrophages, the insulin-sensitizing effect of PPARγ may involve suppression of proinflammatory gene expression by recruiting the corepressor complex that contains corepressors and histone deacetylases (HDACs).
169	23951179	Finally, extracellular signal-related kinase 1/2 (ERK1/2) mediated TNFα-induced lipolysis, and TZDs suppressed TNFα-induced ERK phosphorylation.