Ignet

Gene Information

Gene symbol: CYP4A11

Gene name: cytochrome P450, family 4, subfamily A, polypeptide 11

HGNC ID: 2642

Synonyms: CYP4AII

Related Genes

#	Gene Symbol	Number of hits
1	ABCA1	1 hits
2	ABCG1	1 hits
3	ACOX1	1 hits
4	CYP2B6	1 hits
5	CYP2E1	1 hits
6	FASN	1 hits
7	HMGA1	1 hits
8	INS	1 hits
9	NR1H3	1 hits
10	PPARA	1 hits
11	TBXAS1	1 hits
12	UCP1	1 hits

Related Sentences

#	PMID	Sentence
1	8274152	Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity.
2	8274152	Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2.
3	8274152	Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney.
4	8274152	These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2.
5	8274152	Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity.
6	8274152	Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2.
7	8274152	Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney.
8	8274152	These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2.
9	8274152	Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity.
10	8274152	Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2.
11	8274152	Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney.
12	8274152	These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2.
13	8274152	Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity.
14	8274152	Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2.
15	8274152	Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney.
16	8274152	These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2.
17	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
18	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
19	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
20	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
21	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
22	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
23	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
24	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
25	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
26	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
27	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
28	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
29	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
30	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
31	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
32	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
33	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
34	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
35	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
36	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
37	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
38	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
39	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
40	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
41	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
42	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
43	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
44	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
45	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
46	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
47	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
48	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
49	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
50	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
51	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
52	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
53	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
54	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
55	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
56	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
57	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
58	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
59	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
60	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
61	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
62	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
63	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
64	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
65	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
66	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
67	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
68	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
69	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
70	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
71	15056802	Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes.
72	15056802	CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting.
73	15056802	Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11.
74	15056802	Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control).
75	15056802	In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein.
76	15056802	Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1.
77	15056802	Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content.
78	15056802	Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes.
79	15056802	The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses.
80	20300478	PPAR/RXR Regulation of Fatty Acid Metabolism and Fatty Acid omega-Hydroxylase (CYP4) Isozymes: Implications for Prevention of Lipotoxicity in Fatty Liver Disease.
81	20300478	How steatosis increases PPARalpha activated gene expression of fatty acid transport proteins, peroxisomal and mitochondrial fatty acid beta-oxidation and omega-oxidation of fatty acids genes regardless of whether dietary fatty acids are polyunsaturated (PUFA), monounsaturated (MUFA), or saturated (SFA) may be determined by the interplay of PPARs and HNF4alpha with the fatty acid transport proteins L-FABP and ACBP.
82	20300478	In hepatic steatosis and steatohepatitis, the omega-oxidation cytochrome P450 CYP4A gene expression is increased even with reduced hepatic levels of PPARalpha.
83	20300478	This strongly implies that CYP4A fatty acid omega-hydroxylase P450s may play an important role in the development of steatohepatitis.
84	20300478	PPAR/RXR Regulation of Fatty Acid Metabolism and Fatty Acid omega-Hydroxylase (CYP4) Isozymes: Implications for Prevention of Lipotoxicity in Fatty Liver Disease.
85	20300478	How steatosis increases PPARalpha activated gene expression of fatty acid transport proteins, peroxisomal and mitochondrial fatty acid beta-oxidation and omega-oxidation of fatty acids genes regardless of whether dietary fatty acids are polyunsaturated (PUFA), monounsaturated (MUFA), or saturated (SFA) may be determined by the interplay of PPARs and HNF4alpha with the fatty acid transport proteins L-FABP and ACBP.
86	20300478	In hepatic steatosis and steatohepatitis, the omega-oxidation cytochrome P450 CYP4A gene expression is increased even with reduced hepatic levels of PPARalpha.
87	20300478	This strongly implies that CYP4A fatty acid omega-hydroxylase P450s may play an important role in the development of steatohepatitis.
88	20811644	Transcriptional regulation of human and rat hepatic lipid metabolism by the grapefruit flavonoid naringenin: role of PPARalpha, PPARgamma and LXRalpha.
89	20811644	Here, we demonstrate that naringenin regulates the activity of nuclear receptors PPARalpha, PPARgamma, and LXRalpha.
90	20811644	We show it activates the ligand-binding domain of both PPARalpha and PPARgamma, while inhibiting LXRalpha in GAL4-fusion reporters.
91	20811644	Using TR-FRET, we show that naringenin is a partial agonist of LXRalpha, inhibiting its association with Trap220 co-activator in the presence of TO901317.
92	20811644	In addition, naringenin induces the expression of PPARalpha co-activator, PGC1alpha.
93	20811644	The flavonoid activates PPAR response element (PPRE) while suppressing LXRalpha response element (LXRE) in human hepatocytes, translating into the induction of PPAR-regulated fatty acid oxidation genes such as CYP4A11, ACOX, UCP1 and ApoAI, and inhibition of LXRalpha-regulated lipogenesis genes, such as FAS, ABCA1, ABCG1, and HMGR.
94	21326303	Variants of the human CYP4A11, which belongs to the cytochrome P450, family 4, have been reported to be associated with hypertension in general populations.