PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17905647-5 2007 The ACC/malonyl-CoA/CPT-I system can therefore represent a coordinate control by which CLA may exert effects on the partitioning of fatty acids between esterification and oxidation. Fatty Acids 132-143 carnitine palmitoyltransferase 1B Rattus norvegicus 20-25 10486258-8 1999 Since it has been reported that the intracellular accumulation of lipids following the inhibition of CPT-I by etomoxir leads to a PPARalpha-mediated metabolic response that increases the expression of genes involved in alternate fatty acid oxidation pathways, these results seem to implicate UCP-3 in this protective metabolic response. Fatty Acids 229-239 carnitine palmitoyltransferase 1B Rattus norvegicus 101-106 16357012-12 2006 We further suggest that decreased CPTI M-CoA sensitivity and increased mitochondrial FAT/CD36 protein are both important for increasing whole body fatty acid oxidation during prolonged exercise. Fatty Acids 147-157 carnitine palmitoyltransferase 1B Rattus norvegicus 34-38 15254779-1 2004 Hepatic mitochondrial outer membrane carnitine palmitoyltransferase I (CPT I) and mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (HMG-CoA synthase) enzymes play a key role in regulation of fatty acid oxidation and in ketogenic pathways, respectively. Fatty Acids 196-206 carnitine palmitoyltransferase 1B Rattus norvegicus 37-69 15254779-1 2004 Hepatic mitochondrial outer membrane carnitine palmitoyltransferase I (CPT I) and mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (HMG-CoA synthase) enzymes play a key role in regulation of fatty acid oxidation and in ketogenic pathways, respectively. Fatty Acids 196-206 carnitine palmitoyltransferase 1B Rattus norvegicus 71-76 10861226-1 2000 Carnitine palmitoyltransferase I (CPT I) catalyses the initial step of fatty acid import into the mitochondrial matrix, the site of beta-oxidation, and its inhibition by malonyl-CoA is a primary control point for this process. Fatty Acids 71-81 carnitine palmitoyltransferase 1B Rattus norvegicus 0-32 10861226-1 2000 Carnitine palmitoyltransferase I (CPT I) catalyses the initial step of fatty acid import into the mitochondrial matrix, the site of beta-oxidation, and its inhibition by malonyl-CoA is a primary control point for this process. Fatty Acids 71-81 carnitine palmitoyltransferase 1B Rattus norvegicus 34-39 17148751-10 2007 At lower fatty acid levels, constitutively active CPT I expression enhanced beta-oxidation. Fatty Acids 9-19 carnitine palmitoyltransferase 1B Rattus norvegicus 50-55 17062841-0 2007 CPT I overexpression protects L6E9 muscle cells from fatty acid-induced insulin resistance. Fatty Acids 53-63 carnitine palmitoyltransferase 1B Rattus norvegicus 0-5 17062841-2 2007 In this study, we tested the hypothesis that overexpression of carnitine palmitoyltransferase I (CPT I) could protect myotubes from fatty acid-induced insulin resistance by reducing lipid accumulation in the muscle cell. Fatty Acids 132-142 carnitine palmitoyltransferase 1B Rattus norvegicus 63-95 17062841-2 2007 In this study, we tested the hypothesis that overexpression of carnitine palmitoyltransferase I (CPT I) could protect myotubes from fatty acid-induced insulin resistance by reducing lipid accumulation in the muscle cell. Fatty Acids 132-142 carnitine palmitoyltransferase 1B Rattus norvegicus 97-102 16509570-3 2006 Malonyl-CoA is a potent, endogenous, and allosteric inhibitor of carnitine palmitoyltransferase-I (CPT-I), a key enzyme for mitochondrial fatty acid oxidation. Fatty Acids 138-148 carnitine palmitoyltransferase 1B Rattus norvegicus 65-97 16509570-3 2006 Malonyl-CoA is a potent, endogenous, and allosteric inhibitor of carnitine palmitoyltransferase-I (CPT-I), a key enzyme for mitochondrial fatty acid oxidation. Fatty Acids 138-148 carnitine palmitoyltransferase 1B Rattus norvegicus 99-104 15334378-12 2004 The increased fatty acid oxidation was associated with an increased content of carnitine palmitoyltransferase I (CPT-I) mRNA, but no difference in the content of CPT-I mRNA to the different fatty acids was found. Fatty Acids 14-24 carnitine palmitoyltransferase 1B Rattus norvegicus 79-111 15334378-12 2004 The increased fatty acid oxidation was associated with an increased content of carnitine palmitoyltransferase I (CPT-I) mRNA, but no difference in the content of CPT-I mRNA to the different fatty acids was found. Fatty Acids 14-24 carnitine palmitoyltransferase 1B Rattus norvegicus 113-118 15206948-3 2004 Malonyl-CoA decarboxylase (MCD) catalyzes the degradation of malonyl-CoA, removes a potent allosteric inhibition on CPT-I and thereby increases fatty acid oxidation in the heart. Fatty Acids 144-154 carnitine palmitoyltransferase 1B Rattus norvegicus 116-121 15030182-5 2004 The compartmentation of carnitine at its main functional location was expected to allow the increased CPT-I activity to ensure in vivo correct fatty acid oxidation rates. Fatty Acids 143-153 carnitine palmitoyltransferase 1B Rattus norvegicus 102-107 14966736-10 2004 The activity of carnitine palmitoyl transferase I (CPT I), an important enzyme in the control of fatty acid oxidation, was measured; data are expressed as nanomoles per minute per unit citrate synthase. Fatty Acids 97-107 carnitine palmitoyltransferase 1B Rattus norvegicus 16-49 14966736-10 2004 The activity of carnitine palmitoyl transferase I (CPT I), an important enzyme in the control of fatty acid oxidation, was measured; data are expressed as nanomoles per minute per unit citrate synthase. Fatty Acids 97-107 carnitine palmitoyltransferase 1B Rattus norvegicus 51-56 12069851-15 2002 The influence of mitochondrial OM fatty acyl chain composition upon two important enzymes of energy metabolism, hexokinase and CPT I, both of which have been linked to apoptosis, is of considerable importance for future studies on fatty acid-induced cell death. Fatty Acids 231-241 carnitine palmitoyltransferase 1B Rattus norvegicus 127-132 11988095-2 2002 Pancreatic beta-cells chronically exposed to fatty acids show higher carnitine palmitoyltransferase I (CPT I) protein levels, higher palmitate oxidation rates and an altered insulin response to glucose. Fatty Acids 45-56 carnitine palmitoyltransferase 1B Rattus norvegicus 69-101 11988095-2 2002 Pancreatic beta-cells chronically exposed to fatty acids show higher carnitine palmitoyltransferase I (CPT I) protein levels, higher palmitate oxidation rates and an altered insulin response to glucose. Fatty Acids 45-56 carnitine palmitoyltransferase 1B Rattus norvegicus 103-108 11988095-5 2002 The overexpression of CPT I in INS1E cells caused a more than a 5-fold increase in the levels of CPT I protein (detected by Western blotting), a 6-fold increase in the CPT activity, and an increase in fatty acid oxidation at 2.5 mM glucose (1.7-fold) and 15 mM glucose (3.1-fold). Fatty Acids 201-211 carnitine palmitoyltransferase 1B Rattus norvegicus 22-27 11988095-8 2002 This decrease depended on CPT I activity, since the presence of etomoxir, a specific inhibitor of CPT I, in the preincubation medium normalized the CPT I activity, the fatty-acid oxidation rate and the insulin secretion in response to glucose. Fatty Acids 168-178 carnitine palmitoyltransferase 1B Rattus norvegicus 26-31 11988095-8 2002 This decrease depended on CPT I activity, since the presence of etomoxir, a specific inhibitor of CPT I, in the preincubation medium normalized the CPT I activity, the fatty-acid oxidation rate and the insulin secretion in response to glucose. Fatty Acids 168-178 carnitine palmitoyltransferase 1B Rattus norvegicus 98-103 11988095-8 2002 This decrease depended on CPT I activity, since the presence of etomoxir, a specific inhibitor of CPT I, in the preincubation medium normalized the CPT I activity, the fatty-acid oxidation rate and the insulin secretion in response to glucose. Fatty Acids 168-178 carnitine palmitoyltransferase 1B Rattus norvegicus 98-103 11988095-13 2002 They also indicate that up-regulation of CPT I contributes to the loss of response to high glucose in beta-cells exposed to fatty acids. Fatty Acids 124-135 carnitine palmitoyltransferase 1B Rattus norvegicus 41-46 11329295-1 2001 The outer mitochondrial membrane enzyme carnitine palmitoyltransferase I (CPTI) catalyzes the initial and regulatory step in the beta-oxidation of fatty acids. Fatty Acids 147-158 carnitine palmitoyltransferase 1B Rattus norvegicus 40-72 11329295-1 2001 The outer mitochondrial membrane enzyme carnitine palmitoyltransferase I (CPTI) catalyzes the initial and regulatory step in the beta-oxidation of fatty acids. Fatty Acids 147-158 carnitine palmitoyltransferase 1B Rattus norvegicus 74-78 9794789-1 1998 The mitochondrial outer membrane enzyme carnitine palmitoyltransferase I (CPT I) plays a major role in the regulation of fatty acid entry into the mitochondrial matrix for beta-oxidation by virtue of its inhibition by malonyl-CoA. Fatty Acids 121-131 carnitine palmitoyltransferase 1B Rattus norvegicus 40-72 9989283-8 1999 It is concluded that fatty acids activate pre-existing, inactive CPT I without involvement of gene transcription and independently of malonyl-CoA. Fatty Acids 21-32 carnitine palmitoyltransferase 1B Rattus norvegicus 65-70 9794789-1 1998 The mitochondrial outer membrane enzyme carnitine palmitoyltransferase I (CPT I) plays a major role in the regulation of fatty acid entry into the mitochondrial matrix for beta-oxidation by virtue of its inhibition by malonyl-CoA. Fatty Acids 121-131 carnitine palmitoyltransferase 1B Rattus norvegicus 74-79 8999842-14 1997 The results indicate that the CPT I gene is an early response gene induced by fatty acids at the transcriptional level in beta- (INS-1) cells. Fatty Acids 78-89 carnitine palmitoyltransferase 1B Rattus norvegicus 30-35 9503162-3 1998 Hepatic mitochondrial outer membrane carnitine palmitoyltransferase I (CPT I), generally accepted as the main site of regulation of fatty acid oxidation, was unaffected by the presence of the extra-hepatic tumour. Fatty Acids 132-142 carnitine palmitoyltransferase 1B Rattus norvegicus 71-76 9349840-1 1997 The fatty acid composition of the diet has been found to influence the activity and sensitivity of mitochondrial carnitine palmitoyltransferase I (CPT I; EC 2.3.1.21) to inhibition by malonyl CoA in rat heart and skeletal muscle. Fatty Acids 4-14 carnitine palmitoyltransferase 1B Rattus norvegicus 147-152 9349840-3 1997 However, because manipulation of the nutritional state in these previous studies was restricted mainly to examining the effect of starvation, this study was undertaken to determine whether, as in liver, the fatty acid content and composition of the diet can regulate the activity and metabolic control of CPT I in heart and skeletal muscle. Fatty Acids 207-217 carnitine palmitoyltransferase 1B Rattus norvegicus 305-310 9349840-8 1997 These studies indicate that the fatty acid composition of the diet is involved in the regulation of mitochondrial CPT I activity in heart and skeletal muscle. Fatty Acids 32-42 carnitine palmitoyltransferase 1B Rattus norvegicus 114-119 9173869-1 1997 Two important factors that determine the flux of hepatic beta-oxidation of long-chain fatty acids are the availability of fatty acid and the activity of carnitine palmitoyltransferase I (CPT I). Fatty Acids 86-96 carnitine palmitoyltransferase 1B Rattus norvegicus 153-185 9173869-1 1997 Two important factors that determine the flux of hepatic beta-oxidation of long-chain fatty acids are the availability of fatty acid and the activity of carnitine palmitoyltransferase I (CPT I). Fatty Acids 86-96 carnitine palmitoyltransferase 1B Rattus norvegicus 187-192 8999842-0 1997 Fatty acids rapidly induce the carnitine palmitoyltransferase I gene in the pancreatic beta-cell line INS-1. Fatty Acids 0-11 carnitine palmitoyltransferase 1B Rattus norvegicus 31-63 8999842-3 1997 We have therefore studied the regulation of carnitine palmitoyltransferase I (CPT I) gene expression by fatty acids in the pancreatic beta-cell line INS-1 since this enzyme catalyzes the limiting step of fatty acid oxidation in various tissues. Fatty Acids 104-115 carnitine palmitoyltransferase 1B Rattus norvegicus 44-76 8999842-3 1997 We have therefore studied the regulation of carnitine palmitoyltransferase I (CPT I) gene expression by fatty acids in the pancreatic beta-cell line INS-1 since this enzyme catalyzes the limiting step of fatty acid oxidation in various tissues. Fatty Acids 104-115 carnitine palmitoyltransferase 1B Rattus norvegicus 78-83 9714790-1 1998 Carnitine palmitoyltransferase I (CPT-I) catalyzes the rate-determining step in mitochondrial fatty acid beta-oxidation. Fatty Acids 94-104 carnitine palmitoyltransferase 1B Rattus norvegicus 0-32 9714790-1 1998 Carnitine palmitoyltransferase I (CPT-I) catalyzes the rate-determining step in mitochondrial fatty acid beta-oxidation. Fatty Acids 94-104 carnitine palmitoyltransferase 1B Rattus norvegicus 34-39 9730105-1 1998 BACKGROUND: Pharmacological inhibition of carnitine palmitoyl transferase I (CPT-I), the enzyme controlling the rate of fatty acid transport into the mitochondria, prevents the contractile dysfunction, myosin isozyme shift and deterioration in sarcoplasmic reticulum Ca2+ handling that occurs in rat models of left ventricular hypertrophy. Fatty Acids 120-130 carnitine palmitoyltransferase 1B Rattus norvegicus 42-75 9730105-1 1998 BACKGROUND: Pharmacological inhibition of carnitine palmitoyl transferase I (CPT-I), the enzyme controlling the rate of fatty acid transport into the mitochondria, prevents the contractile dysfunction, myosin isozyme shift and deterioration in sarcoplasmic reticulum Ca2+ handling that occurs in rat models of left ventricular hypertrophy. Fatty Acids 120-130 carnitine palmitoyltransferase 1B Rattus norvegicus 77-82 9486313-9 1998 Thus reversible inhibitors of CPT I represent a class of novel hypoglycemic agents that inhibit fatty acid oxidation without inducing cardiac hypertrophy. Fatty Acids 96-106 carnitine palmitoyltransferase 1B Rattus norvegicus 30-35 8999842-3 1997 We have therefore studied the regulation of carnitine palmitoyltransferase I (CPT I) gene expression by fatty acids in the pancreatic beta-cell line INS-1 since this enzyme catalyzes the limiting step of fatty acid oxidation in various tissues. Fatty Acids 104-114 carnitine palmitoyltransferase 1B Rattus norvegicus 44-76 2597132-10 1989 (6) Transfer to carnitine of all three fatty acids (as potassium salts) by carnitine palmitoyltransferase-I (CPT-I) was similarly inhibited by increasing concentrations of malonyl-CoA. Fatty Acids 39-50 carnitine palmitoyltransferase 1B Rattus norvegicus 75-107 8999842-3 1997 We have therefore studied the regulation of carnitine palmitoyltransferase I (CPT I) gene expression by fatty acids in the pancreatic beta-cell line INS-1 since this enzyme catalyzes the limiting step of fatty acid oxidation in various tissues. Fatty Acids 104-114 carnitine palmitoyltransferase 1B Rattus norvegicus 78-83 8999842-6 1997 It was detectable after 1 h and reached a maximum after 3 h. The induction of CPT I mRNA by fatty acids did not require their oxidation, and 2-bromopalmitate, a nonoxidizable fatty acid, increased CPT I mRNA to the same extent as palmitate. Fatty Acids 92-103 carnitine palmitoyltransferase 1B Rattus norvegicus 78-83 8999842-6 1997 It was detectable after 1 h and reached a maximum after 3 h. The induction of CPT I mRNA by fatty acids did not require their oxidation, and 2-bromopalmitate, a nonoxidizable fatty acid, increased CPT I mRNA to the same extent as palmitate. Fatty Acids 92-102 carnitine palmitoyltransferase 1B Rattus norvegicus 78-83 8999842-9 1997 The half-life of the CPT I transcript was unchanged by fatty acids, and nuclear run-on analysis showed a rapid (less than 45 min) and pronounced transcriptional activation of the CPT I gene by fatty acids. Fatty Acids 193-204 carnitine palmitoyltransferase 1B Rattus norvegicus 179-184 9075190-6 1997 This possession by CPT I of a high "affinity" toward these nonessential fatty acyl CoAs, but a lower "affinity" toward linoleoyl CoA, the ester of an essential fatty acid, may enable this latter fatty acid to be spared from oxidation when its concentration in the diet is low. Fatty Acids 160-170 carnitine palmitoyltransferase 1B Rattus norvegicus 19-24 7721804-6 1995 Because the myocardial carnitine content is very low at birth and rises dramatically over the next several weeks, it can be estimated that L-CPT I (Km for carnitine of only 30 microM compared with a value of 500 microM for M-CPT I) is responsible for some 60% of total cardiac fatty acid oxidation in the newborn rat; the value falls to approximately 4% in adult animals. Fatty Acids 277-287 carnitine palmitoyltransferase 1B Rattus norvegicus 141-146 7866292-13 1994 It is proposed that the effects of dietary lipid manipulation upon CTP I activity and sensitivity to inhibition by malonyl CoA are due to alterations in the fatty acid composition of the phospholipids in the mitochondrial membrane where CPT I resides. Fatty Acids 157-167 carnitine palmitoyltransferase 1B Rattus norvegicus 237-242 8424771-16 1993 239, 485-488] and that control of the flux of hepatic fatty acids into the oxidative pathway is largely lost from the reaction catalysed by mitochondrial overt carnitine palmitoyltransferase (CPT I) during this phase of recovery from the starved state. Fatty Acids 54-65 carnitine palmitoyltransferase 1B Rattus norvegicus 192-197 1736904-1 1992 Fatty acid oxidation was studied in the presence of inhibitors of carnitine palmitoyltransferase I (CPT I), in normal and in peroxisome-proliferated rat hepatocytes. Fatty Acids 0-10 carnitine palmitoyltransferase 1B Rattus norvegicus 100-105 1736904-9 1992 These results show that inhibitors of the mitochondrial CPT I may also inhibit the peroxisomal octanoyl transferase; they also support the hypothesis that the octanoyltransferase has the capacity to control or regulate peroxisomal fatty acid oxidation. Fatty Acids 231-241 carnitine palmitoyltransferase 1B Rattus norvegicus 56-61 2166437-1 1990 Malonyl-CoA is a potent inhibitor of carnitine palmitoyltransferase I (CPT-I), the rate-limiting enzyme for fatty acid oxidation in mitochondria from liver of fed rats. Fatty Acids 108-118 carnitine palmitoyltransferase 1B Rattus norvegicus 37-69 2166437-1 1990 Malonyl-CoA is a potent inhibitor of carnitine palmitoyltransferase I (CPT-I), the rate-limiting enzyme for fatty acid oxidation in mitochondria from liver of fed rats. Fatty Acids 108-118 carnitine palmitoyltransferase 1B Rattus norvegicus 71-76 2378434-6 1990 The present results show that ethanol feeding to rats leads to profound alterations in the regulatory properties of hepatic CPT-I, which seem to be determinant for the decreased capacity of fatty acid oxidation by the liver in this state. Fatty Acids 190-200 carnitine palmitoyltransferase 1B Rattus norvegicus 124-129 9016810-7 1997 Hence, stimulation of hepatic fatty acid oxidation by AMPK seems to rely on the activation of CPT-I by two different mechanisms: deinhibition of CPT-I induced by depletion of intracellular malonyl-CoA levels and malonyl-CoA-independent stimulation of CPT-I, which might involve modulation of interactions between CPT-I and cytoskeletal components. Fatty Acids 30-40 carnitine palmitoyltransferase 1B Rattus norvegicus 94-99 9016810-7 1997 Hence, stimulation of hepatic fatty acid oxidation by AMPK seems to rely on the activation of CPT-I by two different mechanisms: deinhibition of CPT-I induced by depletion of intracellular malonyl-CoA levels and malonyl-CoA-independent stimulation of CPT-I, which might involve modulation of interactions between CPT-I and cytoskeletal components. Fatty Acids 30-40 carnitine palmitoyltransferase 1B Rattus norvegicus 145-150 9016810-7 1997 Hence, stimulation of hepatic fatty acid oxidation by AMPK seems to rely on the activation of CPT-I by two different mechanisms: deinhibition of CPT-I induced by depletion of intracellular malonyl-CoA levels and malonyl-CoA-independent stimulation of CPT-I, which might involve modulation of interactions between CPT-I and cytoskeletal components. Fatty Acids 30-40 carnitine palmitoyltransferase 1B Rattus norvegicus 145-150 9016810-7 1997 Hence, stimulation of hepatic fatty acid oxidation by AMPK seems to rely on the activation of CPT-I by two different mechanisms: deinhibition of CPT-I induced by depletion of intracellular malonyl-CoA levels and malonyl-CoA-independent stimulation of CPT-I, which might involve modulation of interactions between CPT-I and cytoskeletal components. Fatty Acids 30-40 carnitine palmitoyltransferase 1B Rattus norvegicus 145-150 8770079-1 1996 The mitochondrial carnitine palmitoyltransferase (CPT) system is composed of two proteins, CPT-I and -II, which, together with carnitine acylcarnitine translocase, are involved in the transport of fatty acids into the mitochondrial matrix for beta-oxidation. Fatty Acids 197-208 carnitine palmitoyltransferase 1B Rattus norvegicus 91-104 8654430-0 1996 Cyclic AMP and fatty acids increase carnitine palmitoyltransferase I gene transcription in cultured fetal rat hepatocytes. Fatty Acids 15-26 carnitine palmitoyltransferase 1B Rattus norvegicus 36-68 8654430-9 1996 While linoleate and Bt2cAMP stimulated CPT I gene transcription by twofold and fourfold, respectively, the fatty acid also increased the half-life of CPT I mRNA (50%). Fatty Acids 107-117 carnitine palmitoyltransferase 1B Rattus norvegicus 150-155 8358330-3 1993 Carnitine palmitoyltransferase I (CPT I), the rate-limiting enzyme for fatty acid oxidation, in platelets obtained from diabetes showed a higher Vmax for palmitoyl-CoA and an increased I50 (concentration giving 50% inhibition of CPT I activity) for malonyl-CoA inhibition. Fatty Acids 71-81 carnitine palmitoyltransferase 1B Rattus norvegicus 0-32 8358330-3 1993 Carnitine palmitoyltransferase I (CPT I), the rate-limiting enzyme for fatty acid oxidation, in platelets obtained from diabetes showed a higher Vmax for palmitoyl-CoA and an increased I50 (concentration giving 50% inhibition of CPT I activity) for malonyl-CoA inhibition. Fatty Acids 71-81 carnitine palmitoyltransferase 1B Rattus norvegicus 34-39 8358330-6 1993 From these findings, fatty acid oxidation in platelets, as in the liver, is likely to be regulated by insulin and both increased CPT I activity and decreased sensitivity to malonyl-CoA inhibition are attributable to enhanced platelet fatty acid oxidation in diabetic rats. Fatty Acids 21-31 carnitine palmitoyltransferase 1B Rattus norvegicus 129-134 8358330-6 1993 From these findings, fatty acid oxidation in platelets, as in the liver, is likely to be regulated by insulin and both increased CPT I activity and decreased sensitivity to malonyl-CoA inhibition are attributable to enhanced platelet fatty acid oxidation in diabetic rats. Fatty Acids 234-244 carnitine palmitoyltransferase 1B Rattus norvegicus 129-134 8097087-7 1993 Investigation of the possible mechanisms that could contribute towards the rapid switching-off of fatty acid oxidation revealed that this was correlated with a very rapid rise and overshoot in hepatic malonyl-CoA concentration, but not with any change in the activity, or sensitivity to malonyl-CoA, of the mitochondrial overt carnitine palmitoyltransferase (CPT I). Fatty Acids 98-108 carnitine palmitoyltransferase 1B Rattus norvegicus 359-364 1811059-0 1991 Fatty acid accumulation during ischemia and reperfusion: effects of pyruvate and POCA, a carnitine palmitoyltransferase I inhibitor. Fatty Acids 0-10 carnitine palmitoyltransferase 1B Rattus norvegicus 89-121 2597132-10 1989 (6) Transfer to carnitine of all three fatty acids (as potassium salts) by carnitine palmitoyltransferase-I (CPT-I) was similarly inhibited by increasing concentrations of malonyl-CoA. Fatty Acids 39-50 carnitine palmitoyltransferase 1B Rattus norvegicus 109-114 3281653-13 1988 The results are discussed in relation to the temporal relationships of changes in the activity and properties of CPT I in vivo in relation to the effects of insulin and glucagon on fatty acid metabolism in vivo. Fatty Acids 181-191 carnitine palmitoyltransferase 1B Rattus norvegicus 113-118 3063212-10 1988 These changes in the regulation of CPT-I activity corresponded with those observed in the rate of fatty acid oxidation. Fatty Acids 98-108 carnitine palmitoyltransferase 1B Rattus norvegicus 35-40 21654328-7 2011 Cluster of differentiation 36 (CD36)-responsible for myocardial fatty acid uptake, carnitine palmitoyl transferase 1beta-a mitochondrial transporter protein and medium chain acyl-Co-A dehydrogenase-a key enzyme in beta oxidation of fatty acids were selected as indicators of fatty acid metabolism. Fatty Acids 232-243 carnitine palmitoyltransferase 1B Rattus norvegicus 83-120 32206097-10 2020 Further, ERRgamma can increase the fatty acid oxidation (FAO) in chemoresistant cells via regulation of CPT1B, the rate-limiting enzyme of FAO. Fatty Acids 35-45 carnitine palmitoyltransferase 1B Rattus norvegicus 104-109 29641977-5 2018 Furthermore, expression of the energy-sensitive proteins carnitine palmitoyltransferase I (CPTI), adenosine 5"-monophosphate-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor gamma (PPAR-gamma) were found to be down-regulated in uterus under NP exposure, which suggested the impaired fatty acid oxidation. Fatty Acids 313-323 carnitine palmitoyltransferase 1B Rattus norvegicus 57-89 27558315-1 2016 Oxfenicine is a carnitine-palmitoyl transferase 1b (CPT-1b)-specific inhibitor that has been shown to improve whole body insulin sensitivity while suppressing fatty acid (FA) oxidation and increasing circulating FA. Fatty Acids 159-169 carnitine palmitoyltransferase 1B Rattus norvegicus 16-50 27558315-1 2016 Oxfenicine is a carnitine-palmitoyl transferase 1b (CPT-1b)-specific inhibitor that has been shown to improve whole body insulin sensitivity while suppressing fatty acid (FA) oxidation and increasing circulating FA. Fatty Acids 159-169 carnitine palmitoyltransferase 1B Rattus norvegicus 52-58 26080315-7 2015 Carnitine palmitoyltransferase 1B (CPT1B), an enzyme in the fatty acid metabolism and PPAR pathways, was significantly over-expressed in the amygdala (P < 0.007) and in the blood (P < 0.01) of stressed rats compared with non-stressed controls. Fatty Acids 60-70 carnitine palmitoyltransferase 1B Rattus norvegicus 0-33 26080315-7 2015 Carnitine palmitoyltransferase 1B (CPT1B), an enzyme in the fatty acid metabolism and PPAR pathways, was significantly over-expressed in the amygdala (P < 0.007) and in the blood (P < 0.01) of stressed rats compared with non-stressed controls. Fatty Acids 60-70 carnitine palmitoyltransferase 1B Rattus norvegicus 35-40 24159189-8 2014 The enhancement of the fatty-acid beta-oxidation factors Cpt1b and Acox1 in eWAT was accompanied by an upregulation of de novo lipogenesis and reduced expression of the unsaturated-fatty-acid-synthesis enzyme gene, Scd1. Fatty Acids 23-33 carnitine palmitoyltransferase 1B Rattus norvegicus 57-62 21654328-7 2011 Cluster of differentiation 36 (CD36)-responsible for myocardial fatty acid uptake, carnitine palmitoyl transferase 1beta-a mitochondrial transporter protein and medium chain acyl-Co-A dehydrogenase-a key enzyme in beta oxidation of fatty acids were selected as indicators of fatty acid metabolism. Fatty Acids 232-242 carnitine palmitoyltransferase 1B Rattus norvegicus 83-120 21909411-0 2011 Oxidation of hepatic carnitine palmitoyl transferase-I (CPT-I) impairs fatty acid beta-oxidation in rats fed a methionine-choline deficient diet. Fatty Acids 71-81 carnitine palmitoyltransferase 1B Rattus norvegicus 56-61 21264498-9 2011 Metabolic shift identified by reduction in the expression of peroxisome proliferator-activated receptor-alpha, medium chain acyl CoA dehydrogenase, and carnitine palmitoyltransferase 1beta was seen at 4 months of age, implying that reduction of fatty acid oxidation is a consequence of hypertrophy. Fatty Acids 245-255 carnitine palmitoyltransferase 1B Rattus norvegicus 152-188 21909411-2 2011 The goal of the present study was to achieve more understanding on the modification/s of carnitinepalmitoyltransferase-I (CPT-I), the rate-limiting enzyme of the mitochondrial fatty acid beta-oxidation, during steatohepatitis. Fatty Acids 176-186 carnitine palmitoyltransferase 1B Rattus norvegicus 89-120 21909411-2 2011 The goal of the present study was to achieve more understanding on the modification/s of carnitinepalmitoyltransferase-I (CPT-I), the rate-limiting enzyme of the mitochondrial fatty acid beta-oxidation, during steatohepatitis. Fatty Acids 176-186 carnitine palmitoyltransferase 1B Rattus norvegicus 122-127 21909411-3 2011 A high fat/methionine-choline deficient (MCD) diet, administered for 4 weeks, was used to induce NASH in rats.We demonstrated that CPT-I activity decreased, to the same extent, both in isolated liver mitochondria and in digitonin-permeabilized hepatocytes from MCD-diet fed rats.At the same time, the rate of total fatty acid oxidation to CO(2) and ketone bodies, measured in isolated hepatocytes, was significantly lowered in treated animals when compared to controls. Fatty Acids 315-325 carnitine palmitoyltransferase 1B Rattus norvegicus 131-136 19111953-1 2009 The carnitine palmitoyltransferase-I (CPT-I) enzymes catalyze the regulated step in overall mitochondrial fatty acid oxidation. Fatty Acids 106-116 carnitine palmitoyltransferase 1B Rattus norvegicus 4-36 19111953-1 2009 The carnitine palmitoyltransferase-I (CPT-I) enzymes catalyze the regulated step in overall mitochondrial fatty acid oxidation. Fatty Acids 106-116 carnitine palmitoyltransferase 1B Rattus norvegicus 38-43 19111953-5 2009 The importance of fatty acid oxidation in the heart and the potential regulation via the liver isoform of CPT-I demands proof of the liver isoform in the heart. Fatty Acids 18-28 carnitine palmitoyltransferase 1B Rattus norvegicus 106-111 18629681-8 2008 Furthermore, the greater increase in CPT-I protein in contact sites as compared to outer membranes emphasizes the significance of contact sites in hepatic fatty acid oxidation. Fatty Acids 155-165 carnitine palmitoyltransferase 1B Rattus norvegicus 37-42