Ignet

Gene Information

Gene symbol: ACO1

Gene name: aconitase 1, soluble

HGNC ID: 117

Synonyms: IRP1, IREBP

Related Genes

#	Gene Symbol	Number of hits
1	ACO2	1 hits
2	AKT1	1 hits
3	FXN	1 hits
4	IGFBP1	1 hits
5	IGFBP3	1 hits
6	INS	1 hits

Related Sentences

#	PMID	Sentence
1	15753094	Recently, we have identified the insulin-response element-binding protein-1 (IRE-BP1) as a transcription factor that appears to mediate insulin action on multiple target genes.
2	15753094	To examine the possibility that IRE-BP1 is an insulin-responsive glucoregulatory factor involved in the metabolic actions of insulin, we investigated the effect of adenoviral overexpression of hepatic IRE-BP1 on the glycemic control of insulin-resistant diabetic rats.
3	15753094	The insulin mimetic effects of IRE-BP1 were also confirmed in L6 myocytes; stable constitutive expressions of IRE-BP1 enhanced glucose transporter expression, glucose uptake, and glycogen accumulation in these cells.
4	15753094	Understanding IRE-BP1 action should constitute a useful probe into the mechanisms of metabolic regulation and an important target to develop therapeutic agents that mimic or enhance insulin action.
5	15753094	Recently, we have identified the insulin-response element-binding protein-1 (IRE-BP1) as a transcription factor that appears to mediate insulin action on multiple target genes.
6	15753094	To examine the possibility that IRE-BP1 is an insulin-responsive glucoregulatory factor involved in the metabolic actions of insulin, we investigated the effect of adenoviral overexpression of hepatic IRE-BP1 on the glycemic control of insulin-resistant diabetic rats.
7	15753094	The insulin mimetic effects of IRE-BP1 were also confirmed in L6 myocytes; stable constitutive expressions of IRE-BP1 enhanced glucose transporter expression, glucose uptake, and glycogen accumulation in these cells.
8	15753094	Understanding IRE-BP1 action should constitute a useful probe into the mechanisms of metabolic regulation and an important target to develop therapeutic agents that mimic or enhance insulin action.
9	15753094	Recently, we have identified the insulin-response element-binding protein-1 (IRE-BP1) as a transcription factor that appears to mediate insulin action on multiple target genes.
10	15753094	To examine the possibility that IRE-BP1 is an insulin-responsive glucoregulatory factor involved in the metabolic actions of insulin, we investigated the effect of adenoviral overexpression of hepatic IRE-BP1 on the glycemic control of insulin-resistant diabetic rats.
11	15753094	The insulin mimetic effects of IRE-BP1 were also confirmed in L6 myocytes; stable constitutive expressions of IRE-BP1 enhanced glucose transporter expression, glucose uptake, and glycogen accumulation in these cells.
12	15753094	Understanding IRE-BP1 action should constitute a useful probe into the mechanisms of metabolic regulation and an important target to develop therapeutic agents that mimic or enhance insulin action.
13	15753094	Recently, we have identified the insulin-response element-binding protein-1 (IRE-BP1) as a transcription factor that appears to mediate insulin action on multiple target genes.
14	15753094	To examine the possibility that IRE-BP1 is an insulin-responsive glucoregulatory factor involved in the metabolic actions of insulin, we investigated the effect of adenoviral overexpression of hepatic IRE-BP1 on the glycemic control of insulin-resistant diabetic rats.
15	15753094	The insulin mimetic effects of IRE-BP1 were also confirmed in L6 myocytes; stable constitutive expressions of IRE-BP1 enhanced glucose transporter expression, glucose uptake, and glycogen accumulation in these cells.
16	15753094	Understanding IRE-BP1 action should constitute a useful probe into the mechanisms of metabolic regulation and an important target to develop therapeutic agents that mimic or enhance insulin action.
17	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
18	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
19	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
20	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
21	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
22	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
23	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
24	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
25	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
26	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
27	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
28	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
29	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
30	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
31	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
32	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
33	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
34	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
35	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
36	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
37	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
38	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
39	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
40	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
41	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
42	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
43	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
44	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
45	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
46	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
47	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
48	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
49	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
50	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
51	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
52	18566119	We recently identified insulin response element-binding protein-1 (IRE-BP1) as a transcription factor that binds and transactivates multiple insulin-responsive genes, but the regulation of IRE-BP1 in vivo is largely unknown.
53	18566119	In this study, we show that IRE-BP1 interacts with the insulin response sequence of the IGF-I, IGFBP-1, and IGFBP-3 genes using chromatin immunoprecipitation assay.
54	18566119	Furthermore, activation by IRE-BP1 is sequence specific and mimics that of the insulin effect on gene transcription.
55	18566119	Tissue expression of IRE-BP1 is 50- to 200-fold higher in classical insulin target compared with nontarget tissues in lean animals, with a significantly reduced level of expression in the skeletal muscle and adipose tissue in obese and diabetic animals.
56	18566119	Cytoplasmic sequestration appears to be related to inhibition of insulin-mediated phosphatidylinositol-3 kinase signaling.
57	18566119	Therefore, in diabetes and obesity, the mechanisms involved in reducing the transactivation of the insulin response sequence by IRE-BP1 include decreased gene transcription and nuclear exclusion to prevent DNA binding.
58	18566119	Our study supports the notion that IRE-BP1 may be relevant to the action of insulin in vivo and may play a role in the development of insulin resistance and diabetes.
59	19213832	Recent evidence supports the idea that insulin signaling through the insulin receptor substrate/phosphatidyl-inositol 3-kinase/Akt pathway is involved in the maintenance of beta-cell mass and function.
60	19213832	We previously identified the insulin-response element binding protein-1 (IRE-BP1) as an effector of insulin-induced Akt signaling in the liver, and showed that the 50-kDa carboxyl fragment confers the transcriptional activity of this factor.
61	19213832	To test whether IRE-BP1 modulates beta-cell function and insulin secretion, we used the rat insulin II promoter to drive expression of the carboxyl fragment in beta-cells.
62	19213832	Our findings suggest that increased gene transcription mediated through IRE-BP1 may contribute to beta-cell dysfunction in insulin resistance, and allow for the hypothesis that IRE-BP1 plays a role in the pathophysiology of type 2 diabetes.
63	19213832	Recent evidence supports the idea that insulin signaling through the insulin receptor substrate/phosphatidyl-inositol 3-kinase/Akt pathway is involved in the maintenance of beta-cell mass and function.
64	19213832	We previously identified the insulin-response element binding protein-1 (IRE-BP1) as an effector of insulin-induced Akt signaling in the liver, and showed that the 50-kDa carboxyl fragment confers the transcriptional activity of this factor.
65	19213832	To test whether IRE-BP1 modulates beta-cell function and insulin secretion, we used the rat insulin II promoter to drive expression of the carboxyl fragment in beta-cells.
66	19213832	Our findings suggest that increased gene transcription mediated through IRE-BP1 may contribute to beta-cell dysfunction in insulin resistance, and allow for the hypothesis that IRE-BP1 plays a role in the pathophysiology of type 2 diabetes.
67	19213832	Recent evidence supports the idea that insulin signaling through the insulin receptor substrate/phosphatidyl-inositol 3-kinase/Akt pathway is involved in the maintenance of beta-cell mass and function.
68	19213832	We previously identified the insulin-response element binding protein-1 (IRE-BP1) as an effector of insulin-induced Akt signaling in the liver, and showed that the 50-kDa carboxyl fragment confers the transcriptional activity of this factor.
69	19213832	To test whether IRE-BP1 modulates beta-cell function and insulin secretion, we used the rat insulin II promoter to drive expression of the carboxyl fragment in beta-cells.
70	19213832	Our findings suggest that increased gene transcription mediated through IRE-BP1 may contribute to beta-cell dysfunction in insulin resistance, and allow for the hypothesis that IRE-BP1 plays a role in the pathophysiology of type 2 diabetes.
71	20053667	Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin.
72	20053667	We demonstrate that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1), a bifunctional protein alternating between an enzymatic and a RNA-binding function through the 'iron-sulfur switch' mechanism.
73	20053667	Importantly, we found that the cytosolic aconitase defect and consequent IRP1 activation occurring in FRDA cells are reversed by the action of extramitochondrial frataxin.
74	20053667	These results provide new insight into the control of cytosolic aconitase/IRP1 switch and expand current knowledge about the molecular pathogenesis of FRDA.
75	20053667	Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin.
76	20053667	We demonstrate that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1), a bifunctional protein alternating between an enzymatic and a RNA-binding function through the 'iron-sulfur switch' mechanism.
77	20053667	Importantly, we found that the cytosolic aconitase defect and consequent IRP1 activation occurring in FRDA cells are reversed by the action of extramitochondrial frataxin.
78	20053667	These results provide new insight into the control of cytosolic aconitase/IRP1 switch and expand current knowledge about the molecular pathogenesis of FRDA.
79	20053667	Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin.
80	20053667	We demonstrate that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1), a bifunctional protein alternating between an enzymatic and a RNA-binding function through the 'iron-sulfur switch' mechanism.
81	20053667	Importantly, we found that the cytosolic aconitase defect and consequent IRP1 activation occurring in FRDA cells are reversed by the action of extramitochondrial frataxin.
82	20053667	These results provide new insight into the control of cytosolic aconitase/IRP1 switch and expand current knowledge about the molecular pathogenesis of FRDA.
83	20053667	Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin.
84	20053667	We demonstrate that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1), a bifunctional protein alternating between an enzymatic and a RNA-binding function through the 'iron-sulfur switch' mechanism.
85	20053667	Importantly, we found that the cytosolic aconitase defect and consequent IRP1 activation occurring in FRDA cells are reversed by the action of extramitochondrial frataxin.
86	20053667	These results provide new insight into the control of cytosolic aconitase/IRP1 switch and expand current knowledge about the molecular pathogenesis of FRDA.