Ignet

Gene Information

Gene symbol: ACSL4

Gene name: acyl-CoA synthetase long-chain family member 4

HGNC ID: 3571

Synonyms: ACS4, LACS4

Related Genes

#	Gene Symbol	Number of hits
1	ACACA	1 hits
2	ACSL1	1 hits
3	ACSL5	1 hits
4	ACSS2	1 hits
5	CD36	1 hits
6	CHKA	1 hits
7	PPARG	1 hits

Related Sentences

#	PMID	Sentence
1	12147264	Although ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, mitochondria, and peroxisomes, the study had used an antibody raised against the full-length ACS1 protein which cross-reacts with other isoforms, probably because all ACS family members contain highly conserved amino acid sequences.
2	12147264	Therefore, we examined the subcellular location of ACS1, ACS4, and ACS5 in rat liver to determine which isoform was present in peroxisomes, whether the ACSs were intrinsic membrane proteins, and which ACS isoforms were up-regulated by PPAR alpha ligands.
3	12147264	Non-cross-reacting ACS1, ACS4, and ACS5 peptide antibodies showed that ACS4 was the only ACS isoform present in peroxisomes isolated from livers of gemfibrozil-treated rats.
4	12147264	ACS1 was present in endoplasmic reticulum fractions and ACS5 was present in mitochondrial fractions.
5	12147264	Incubation with troglitazone, a specific inhibitor of ACS4, decreased ACS activity in the MAM fractions 30-45% and in the peroxisomal fractions about 30%.
6	12147264	Treatment with GW9578 increased ACS4 mRNA abundance 40% and ACS1 mRNA 25%.
7	12147264	We also determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
8	12147264	Although ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, mitochondria, and peroxisomes, the study had used an antibody raised against the full-length ACS1 protein which cross-reacts with other isoforms, probably because all ACS family members contain highly conserved amino acid sequences.
9	12147264	Therefore, we examined the subcellular location of ACS1, ACS4, and ACS5 in rat liver to determine which isoform was present in peroxisomes, whether the ACSs were intrinsic membrane proteins, and which ACS isoforms were up-regulated by PPAR alpha ligands.
10	12147264	Non-cross-reacting ACS1, ACS4, and ACS5 peptide antibodies showed that ACS4 was the only ACS isoform present in peroxisomes isolated from livers of gemfibrozil-treated rats.
11	12147264	ACS1 was present in endoplasmic reticulum fractions and ACS5 was present in mitochondrial fractions.
12	12147264	Incubation with troglitazone, a specific inhibitor of ACS4, decreased ACS activity in the MAM fractions 30-45% and in the peroxisomal fractions about 30%.
13	12147264	Treatment with GW9578 increased ACS4 mRNA abundance 40% and ACS1 mRNA 25%.
14	12147264	We also determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
15	12147264	Although ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, mitochondria, and peroxisomes, the study had used an antibody raised against the full-length ACS1 protein which cross-reacts with other isoforms, probably because all ACS family members contain highly conserved amino acid sequences.
16	12147264	Therefore, we examined the subcellular location of ACS1, ACS4, and ACS5 in rat liver to determine which isoform was present in peroxisomes, whether the ACSs were intrinsic membrane proteins, and which ACS isoforms were up-regulated by PPAR alpha ligands.
17	12147264	Non-cross-reacting ACS1, ACS4, and ACS5 peptide antibodies showed that ACS4 was the only ACS isoform present in peroxisomes isolated from livers of gemfibrozil-treated rats.
18	12147264	ACS1 was present in endoplasmic reticulum fractions and ACS5 was present in mitochondrial fractions.
19	12147264	Incubation with troglitazone, a specific inhibitor of ACS4, decreased ACS activity in the MAM fractions 30-45% and in the peroxisomal fractions about 30%.
20	12147264	Treatment with GW9578 increased ACS4 mRNA abundance 40% and ACS1 mRNA 25%.
21	12147264	We also determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
22	12147264	Although ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, mitochondria, and peroxisomes, the study had used an antibody raised against the full-length ACS1 protein which cross-reacts with other isoforms, probably because all ACS family members contain highly conserved amino acid sequences.
23	12147264	Therefore, we examined the subcellular location of ACS1, ACS4, and ACS5 in rat liver to determine which isoform was present in peroxisomes, whether the ACSs were intrinsic membrane proteins, and which ACS isoforms were up-regulated by PPAR alpha ligands.
24	12147264	Non-cross-reacting ACS1, ACS4, and ACS5 peptide antibodies showed that ACS4 was the only ACS isoform present in peroxisomes isolated from livers of gemfibrozil-treated rats.
25	12147264	ACS1 was present in endoplasmic reticulum fractions and ACS5 was present in mitochondrial fractions.
26	12147264	Incubation with troglitazone, a specific inhibitor of ACS4, decreased ACS activity in the MAM fractions 30-45% and in the peroxisomal fractions about 30%.
27	12147264	Treatment with GW9578 increased ACS4 mRNA abundance 40% and ACS1 mRNA 25%.
28	12147264	We also determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
29	12147264	Although ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, mitochondria, and peroxisomes, the study had used an antibody raised against the full-length ACS1 protein which cross-reacts with other isoforms, probably because all ACS family members contain highly conserved amino acid sequences.
30	12147264	Therefore, we examined the subcellular location of ACS1, ACS4, and ACS5 in rat liver to determine which isoform was present in peroxisomes, whether the ACSs were intrinsic membrane proteins, and which ACS isoforms were up-regulated by PPAR alpha ligands.
31	12147264	Non-cross-reacting ACS1, ACS4, and ACS5 peptide antibodies showed that ACS4 was the only ACS isoform present in peroxisomes isolated from livers of gemfibrozil-treated rats.
32	12147264	ACS1 was present in endoplasmic reticulum fractions and ACS5 was present in mitochondrial fractions.
33	12147264	Incubation with troglitazone, a specific inhibitor of ACS4, decreased ACS activity in the MAM fractions 30-45% and in the peroxisomal fractions about 30%.
34	12147264	Treatment with GW9578 increased ACS4 mRNA abundance 40% and ACS1 mRNA 25%.
35	12147264	We also determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
36	17259370	In addition to peroxisome proliferator-activated receptor (PPAR)-gamma, rosiglitazone can affect other targets, such as directly inhibiting recombinant long-chain acyl-CoA synthetase (ACSL)-4 activity.
37	17259370	Thus, rosiglitazone inhibits ACSL activity and fatty acid partitioning in human and murine SMCs and in human macrophages through a PPAR-gamma-independent mechanism likely to be mediated by ACSL4 inhibition.
38	20094041	Although germ-line deletion of c-Jun NH(2)-terminal kinase (JNK) improves overall insulin sensitivity in mice, those studies could not reveal the underlying molecular mechanism and the tissue site(s) in which reduced JNK activity elicits the observed phenotype.
39	20094041	Given its importance in nonesterified fatty acids (NEFA) and glucose utilization, we hypothesized that the insulin-sensitive phenotype associated with Jnk deletion originates from loss of JNK function in skeletal muscle.
40	20094041	We show for the first time that cellular JNK2- and JNK1/JNK2-deficiency divert glucose from oxidation to glycogenesis due to increased glycogen synthase (GS) activity and induction of Pdk4.
41	20094041	We further show that JNK2- and JNK1/JNK2-deficiency profoundly increase cellular NEFA oxidation, and their conversion to phospholipids and triglyceride.
42	20094041	The increased NEFA utilization was coupled to increased expressions of selective NEFA handling genes including Cd36, Acsl4, and Chka, and enhanced palmitic acid (PA)-dependent suppression of acetyl-CoA carboxylase (Acc).
43	20094041	In JNK-intact cells, PA inhibited insulin signaling and glycogenesis.
44	20094041	Although silencing Jnk1 and/or Jnk2 prevented PA-induced inhibition of insulin signaling, it did not completely block decreased insulin-mediated glycogenesis, thus indicating JNK-independent pathways in the suppression of glycogenesis by PA.
45	20094041	Muscle-specific inhibition of JNK2 (or total JNK) improves the capacity of NEFA utilization and glycogenesis, and is a potential therapeutic target for improving systemic insulin sensitivity in type 2 diabetes (T2D).