General Information:

Id: 3,892
Diseases: Diabetes mellitus, type II - [OMIM]
Insulin resistance
Mammalia
article
Reference: Ringseis R et al.(2012) Regulation of Genes Involved in Carnitine Homeostasis by PPARalpha across Different Species (Rat, Mouse, Pig, Cattle, Chicken, and Human) PPAR Res 2012 [PMID: 23150726]

Interaction Information:

Comment Peroxisome proliferator-activated receptor alpha (PPARalpha) is considered a master transcriptional regulator of lipid metabolism and energy homeostasis, because typical genes regulated by PPARalpha are involved in all aspects of fatty acid catabolism (cellular fatty acid uptake, activation of fatty acids, intracellular fatty acid transport, import of fatty acids into the mitochondria, and mitochondrial and peroxisomal fatty acid beta-oxidation), ketogenesis, as well as gluconeogenesis.
Formal Description
Interaction-ID: 39368

gene/protein

PPARA

affects_activity of

Drugbank entries Show/Hide entries for PPARA
Comment Peroxisome proliferator-activated receptor alpha (PPARalpha) is considered a master transcriptional regulator of lipid metabolism and energy homeostasis, because typical genes regulated by PPARalpha are involved in all aspects of fatty acid catabolism (cellular fatty acid uptake, activation of fatty acids, intracellular fatty acid transport, import of fatty acids into the mitochondria, and mitochondrial and peroxisomal fatty acid beta-oxidation), ketogenesis, as well as gluconeogenesis.
Formal Description
Interaction-ID: 39370

gene/protein

PPARA

affects_activity of

Drugbank entries Show/Hide entries for PPARA
Comment Peroxisome proliferator-activated receptor alpha (PPARalpha) is considered a master transcriptional regulator of lipid metabolism and energy homeostasis, because typical genes regulated by PPARalpha are involved in all aspects of fatty acid catabolism (cellular fatty acid uptake, activation of fatty acids, intracellular fatty acid transport, import of fatty acids into the mitochondria, and mitochondrial and peroxisomal fatty acid beta-oxidation), ketogenesis, as well as gluconeogenesis.
Formal Description
Interaction-ID: 39371

gene/protein

PPARA

affects_activity of

Drugbank entries Show/Hide entries for PPARA
Comment Peroxisome proliferator-activated receptor alpha (PPARalpha) is considered a master transcriptional regulator of lipid metabolism and energy homeostasis, because typical genes regulated by PPARalpha are involved in all aspects of fatty acid catabolism (cellular fatty acid uptake, activation of fatty acids, intracellular fatty acid transport, import of fatty acids into the mitochondria, and mitochondrial and peroxisomal fatty acid beta-oxidation), ketogenesis, as well as gluconeogenesis.
Formal Description
Interaction-ID: 39372

gene/protein

PPARA

affects_activity of

process

gluconeogenesis

Drugbank entries Show/Hide entries for PPARA
Comment Studies repeatedly reported that energy deprivation or treatment of rats with fibrates causes a marked, up to 5-fold elevation of the hepatic concentration of carnitine.
Formal Description
Interaction-ID: 39375

environment

calorie restriction

increases_quantity of

drug/chemical compound

Carnitine

in liver; via PPARA
Comment Studies repeatedly reported that energy deprivation or treatment of rats with fibrates causes a marked, up to 5-fold elevation of the hepatic concentration of carnitine.
Formal Description
Interaction-ID: 39376

drug/chemical compound

Fibrate

increases_quantity of

drug/chemical compound

Carnitine

in liver; via PPARA
Comment It was shown that elevation of hepatic carnitine concentration in response to fasting, or fibrates occurs only in wild-type mice but not in transgenic mice lacking a functional PPARalpha protein strengthening the assumption that PPARalpha is a critical regulator of carnitine homeostasis.
Formal Description
Interaction-ID: 39378

gene/protein

PPARA

increases_quantity of

drug/chemical compound

Carnitine

in liver
Drugbank entries Show/Hide entries for PPARA
Comment It was shown that elevation of hepatic carnitine concentration in response to fasting, or fibrates occurs only in wild-type mice but not in transgenic mice lacking a functional PPARalpha protein strengthening the assumption that PPARalpha is a critical regulator of carnitine homeostasis.
Formal Description
Interaction-ID: 39379

gene/protein

PPARA

affects_activity of

Drugbank entries Show/Hide entries for PPARA
Comment It could be convincingly demonstrated that the mouse genes encoding the carnitine transporter novel organic cation transporter 2 (OCTN2/SLC22A5) and two enzymes of the carnitine biosynthetic pathway, gamma-butyrobetaine dioxygenase (BBOX1) and 4-trimethylaminobutyraldehyde dehydrogenase (ALDH9A1), are direct PPARalpha target genes as evidenced by the identification of functional peroxysome proliferator responsive elements (PPRE) within the regulatory region of the respective genes.
Formal Description
Interaction-ID: 39380

gene/protein

PPARA

increases_expression of

gene/protein

SLC22A5

Drugbank entries Show/Hide entries for PPARA or SLC22A5
Comment It could be convincingly demonstrated that the mouse genes encoding the carnitine transporter novel organic cation transporter 2 (OCTN2/SLC22A5) and two enzymes of the carnitine biosynthetic pathway, gamma-butyrobetaine dioxygenase (BBOX1) and 4-trimethylaminobutyraldehyde dehydrogenase (ALDH9A1), are direct PPARalpha target genes as evidenced by the identification of functional peroxysome proliferator responsive elements (PPRE) within the regulatory region of the respective genes.
Formal Description
Interaction-ID: 39382

gene/protein

PPARA

increases_expression of

gene/protein

BBOX1

Drugbank entries Show/Hide entries for PPARA or BBOX1
Comment It could be convincingly demonstrated that the mouse genes encoding the carnitine transporter novel organic cation transporter 2 (OCTN2/SLC22A5) and two enzymes of the carnitine biosynthetic pathway, gamma-butyrobetaine dioxygenase (BBOX1) and 4-trimethylaminobutyraldehyde dehydrogenase (ALDH9A1), are direct PPARalpha target genes as evidenced by the identification of functional peroxysome proliferator responsive elements (PPRE) within the regulatory region of the respective genes.
Formal Description
Interaction-ID: 39383

gene/protein

PPARA

increases_expression of

gene/protein

ALDH9A1

Drugbank entries Show/Hide entries for PPARA or ALDH9A1
Comment It is well established that PPARalpha activators exert distinct species-specific actions. In rodents, like mice and rats, administration of PPARalpha activators leads to a marked peroxisomal enzyme induction, peroxisome proliferation, and even hepatocarcinogenesis. In contrast, PPARalpha activators cannot induce peroxisome proliferation and hepatocarcinogenesis and the induction of peroxisomal metabolism pathways is much less pronounced in human hepatocytes and livers from nonhuman primates. This distinct response of the peroxisomes to PPARalpha activators is responsible for the classification of different species into proliferating (mice, rats) and nonproliferating ones (humans, monkeys, guinea pigs). Several factors are considered to account for the marked difference in the response to PPARalpha activators between different species: expression level of PPARalpha, degree of conservation and functionality of the PPRE in the regulatory region of target genes, and lack or overexpression of transcriptional coregulators.
Formal Description
Interaction-ID: 39384

gene/protein

PPARA

affects_activity of

in rodents
Drugbank entries Show/Hide entries for PPARA
Comment It is well established that PPARalpha activators exert distinct species-specific actions. In rodents, like mice and rats, administration of PPARalpha activators leads to a marked peroxisomal enzyme induction, peroxisome proliferation, and even hepatocarcinogenesis. In contrast, PPARalpha activators cannot induce peroxisome proliferation and hepatocarcinogenesis and the induction of peroxisomal metabolism pathways is much less pronounced in human hepatocytes and livers from nonhuman primates. This distinct response of the peroxisomes to PPARalpha activators is responsible for the classification of different species into proliferating (mice, rats) and nonproliferating ones (humans, monkeys, guinea pigs). Several factors are considered to account for the marked difference in the response to PPARalpha activators between different species: expression level of PPARalpha, degree of conservation and functionality of the PPRE in the regulatory region of target genes, and lack or overexpression of transcriptional coregulators.
Formal Description
Interaction-ID: 39388

gene/protein

PPARA

affects_activity of

in rodents
Drugbank entries Show/Hide entries for PPARA
Comment It is well established that PPARalpha activators exert distinct species-specific actions. In rodents, like mice and rats, administration of PPARalpha activators leads to a marked peroxisomal enzyme induction, peroxisome proliferation, and even hepatocarcinogenesis. In contrast, PPARalpha activators cannot induce peroxisome proliferation and hepatocarcinogenesis and the induction of peroxisomal metabolism pathways is much less pronounced in human hepatocytes and livers from nonhuman primates. This distinct response of the peroxisomes to PPARalpha activators is responsible for the classification of different species into proliferating (mice, rats) and nonproliferating ones (humans, monkeys, guinea pigs). Several factors are considered to account for the marked difference in the response to PPARalpha activators between different species: expression level of PPARalpha, degree of conservation and functionality of the PPRE in the regulatory region of target genes, and lack or overexpression of transcriptional coregulators.
Formal Description
Interaction-ID: 39396

gene/protein

PPARA

NOT affects_activity of

in humans
Drugbank entries Show/Hide entries for PPARA
Comment It is well established that PPARalpha activators exert distinct species-specific actions. In rodents, like mice and rats, administration of PPARalpha activators leads to a marked peroxisomal enzyme induction, peroxisome proliferation, and even hepatocarcinogenesis. In contrast, PPARalpha activators cannot induce peroxisome proliferation and hepatocarcinogenesis and the induction of peroxisomal metabolism pathways is much less pronounced in human hepatocytes and livers from nonhuman primates. This distinct response of the peroxisomes to PPARalpha activators is responsible for the classification of different species into proliferating (mice, rats) and nonproliferating ones (humans, monkeys, guinea pigs). Several factors are considered to account for the marked difference in the response to PPARalpha activators between different species: expression level of PPARalpha, degree of conservation and functionality of the PPRE in the regulatory region of target genes, and lack or overexpression of transcriptional coregulators.
Formal Description
Interaction-ID: 39397

gene/protein

PPARA

NOT affects_activity of

in humans
Drugbank entries Show/Hide entries for PPARA
Comment Carnitine is a water soluble quaternary amine (3-hydroxy-4-N,N,N-trimethylaminobutyric acid) which is essential for normal function of all tissues. The primary function of carnitine is to facilitate the translocation of activated long-chain fatty acids from the cytosol into the mitochondrial matrix, a process called carnitine shuttle, for subsequent fatty acid beta-oxidation.
Formal Description
Interaction-ID: 39399

drug/chemical compound

Carnitine

increases_activity of

Comment Carnitine is a water soluble quaternary amine (3-hydroxy-4-N,N,N-trimethylaminobutyric acid) which is essential for normal function of all tissues. The primary function of carnitine is to facilitate the translocation of activated long-chain fatty acids from the cytosol into the mitochondrial matrix, a process called carnitine shuttle, for subsequent fatty acid beta-oxidation.
Formal Description
Interaction-ID: 39421

increases_activity of

Comment Food of animal origin, such as meat and dairy products, containing high carnitine levels, makes the greatest contribution to total carnitine uptake. The intake of food of plant origin is negligible for dietary carnitine uptake due to its very low carnitine levels. Thus, dietary uptake of carnitine in strict vegetarians is very low. Nonetheless, plasma carnitine levels in vegetarians are only 15-30% lower than those in nonvegetarians, being yet within the normal physiological range, because vegetarians have a more efficient renal reabsorption of carnitine (urinary total carnitine excretion was 55% less in vegetarians than in nonvegetarians) and a greater rate of endogenous carnitine biosynthesis.
Formal Description
Interaction-ID: 39422

environment

vegetarian diet

increases_activity of

Comment Food of animal origin, such as meat and dairy products, containing high carnitine levels, makes the greatest contribution to total carnitine uptake. The intake of food of plant origin is negligible for dietary carnitine uptake due to its very low carnitine levels. Thus, dietary uptake of carnitine in strict vegetarians is very low. Nonetheless, plasma carnitine levels in vegetarians are only 15-30% lower than those in nonvegetarians, being yet within the normal physiological range, because vegetarians have a more efficient renal reabsorption of carnitine (urinary total carnitine excretion was 55% less in vegetarians than in nonvegetarians) and a greater rate of endogenous carnitine biosynthesis.
Formal Description
Interaction-ID: 39426

environment

vegetarian diet

increases_activity of

process

renal carnitine reabsorption

in kidney
Comment Food of animal origin, such as meat and dairy products, containing high carnitine levels, makes the greatest contribution to total carnitine uptake. The intake of food of plant origin is negligible for dietary carnitine uptake due to its very low carnitine levels. Thus, dietary uptake of carnitine in strict vegetarians is very low. Nonetheless, plasma carnitine levels in vegetarians are only 15-30% lower than those in nonvegetarians, being yet within the normal physiological range, because vegetarians have a more efficient renal reabsorption of carnitine (urinary total carnitine excretion was 55% less in vegetarians than in nonvegetarians) and a greater rate of endogenous carnitine biosynthesis.
Formal Description
Interaction-ID: 39427

environment

vegetarian diet

decreases_activity of

process

urinary carnitine excretion

in kidney
Comment In healthy vegetarians, carnitine deficiency may develop only if certain micronutrients, such as vitamin C, vitamin B6 , and iron, which are required as co-factors for carnitine biosynthesis are not provided from the diet in sufficient amounts.
Formal Description
Interaction-ID: 39428

drug/chemical compound

Ascorbate

affects_activity of

Comment In healthy vegetarians, carnitine deficiency may develop only if certain micronutrients, such as vitamin C, vitamin B6 , and iron, which are required as co-factors for carnitine biosynthesis are not provided from the diet in sufficient amounts.
Formal Description
Interaction-ID: 39433

drug/chemical compound

Pyridoxal phosphate

affects_activity of

Drugbank entries Show/Hide entries for Pyridoxal phosphate
Comment In healthy vegetarians, carnitine deficiency may develop only if certain micronutrients, such as vitamin C, vitamin B6 , and iron, which are required as co-factors for carnitine biosynthesis are not provided from the diet in sufficient amounts.
Formal Description
Interaction-ID: 39435

drug/chemical compound

Iron

affects_activity of

Comment The transport across the plasma membrane against a high concentration gradient (in skeletal muscle more than 100-fold) is mediated by the organic cation transporters (OCTNs) which belong to the solute carrier 22A family. The OCTN2 isoform, which is sodium-dependent and high-affinity, is considered the physiologically most important one due to its wide tissue expression. This transporter represents the molecular basis for the tubular reabsorption process of carnitine in the kidney and is therefore fundamental for maintaining normal carnitine levels in serum. Defects in the renal reabsorption process of carnitine due to a mutation in the OCTN2 gene are causative for severe carnitine deficiency in such patients.
Formal Description
Interaction-ID: 39437

gene/protein

SLC22A5

increases_activity of

across the plasma membrane
Drugbank entries Show/Hide entries for SLC22A5
Comment The transport across the plasma membrane against a high concentration gradient (in skeletal muscle more than 100-fold) is mediated by the organic cation transporters (OCTNs) which belong to the solute carrier 22A family. The OCTN2 isoform, which is sodium-dependent and high-affinity, is considered the physiologically most important one due to its wide tissue expression. This transporter represents the molecular basis for the tubular reabsorption process of carnitine in the kidney and is therefore fundamental for maintaining normal carnitine levels in serum. Defects in the renal reabsorption process of carnitine due to a mutation in the OCTN2 gene are causative for severe carnitine deficiency in such patients.
Formal Description
Interaction-ID: 39438

drug/chemical compound

Na+

affects_activity of

gene/protein

SLC22A5

Drugbank entries Show/Hide entries for SLC22A5
Comment The transport across the plasma membrane against a high concentration gradient (in skeletal muscle more than 100-fold) is mediated by the organic cation transporters (OCTNs) which belong to the solute carrier 22A family. The OCTN2 isoform, which is sodium-dependent and high-affinity, is considered the physiologically most important one due to its wide tissue expression. This transporter represents the molecular basis for the tubular reabsorption process of carnitine in the kidney and is therefore fundamental for maintaining normal carnitine levels in serum. Defects in the renal reabsorption process of carnitine due to a mutation in the OCTN2 gene are causative for severe carnitine deficiency in such patients.
Formal Description
Interaction-ID: 39440

gene/protein

SLC22A5

increases_activity of

process

renal carnitine reabsorption

in kidney
Drugbank entries Show/Hide entries for SLC22A5
Comment The OCTN1 isoform is considered to contribute less to carnitine transport than OCTN2 due to its low carnitine transport activity. OCTN1 is localized in the mitochondrial membrane in close proximity to CPT I, the rate-limiting enzyme for carnitine-dependent fatty acid oxidation. Due to this localization, OCTN1 has been proposed to operate on the mitochondrial influx and efflux of carnitine and acylcarnitine esters indicating that OCTN1 is mainly involved in maintaining intracellular carnitine homeostasis.
Formal Description
Interaction-ID: 39441

gene/protein

SLC22A4

is localized in

cellular component

mitochondrial outer membrane

Drugbank entries Show/Hide entries for SLC22A4
Comment The OCTN1 isoform is considered to contribute less to carnitine transport than OCTN2 due to its low carnitine transport activity. OCTN1 is localized in the mitochondrial membrane in close proximity to CPT I, the rate-limiting enzyme for carnitine-dependent fatty acid oxidation. Due to this localization, OCTN1 has been proposed to operate on the mitochondrial influx and efflux of carnitine and acylcarnitine esters indicating that OCTN1 is mainly involved in maintaining intracellular carnitine homeostasis.
Formal Description
Interaction-ID: 39445

gene/protein

SLC22A4

affects_activity of

Drugbank entries Show/Hide entries for SLC22A4
Comment The OCTN1 isoform is considered to contribute less to carnitine transport than OCTN2 due to its low carnitine transport activity. OCTN1 is localized in the mitochondrial membrane in close proximity to CPT I, the rate-limiting enzyme for carnitine-dependent fatty acid oxidation. Due to this localization, OCTN1 has been proposed to operate on the mitochondrial influx and efflux of carnitine and acylcarnitine esters indicating that OCTN1 is mainly involved in maintaining intracellular carnitine homeostasis.
Formal Description
Interaction-ID: 39448

gene/protein

SLC22A4

affects_activity of

process

carnitine homeostasis

Drugbank entries Show/Hide entries for SLC22A4
Comment Another OCTN isoform, namely, OCTN3, has been suggested to play a role for carnitine uptake into testis and to also mediate renal reabsorption of carnitine.
Formal Description
Interaction-ID: 39449

gene/protein

OCTN3

affects_activity of

into testis
Comment Another OCTN isoform, namely, OCTN3, has been suggested to play a role for carnitine uptake into testis and to also mediate renal reabsorption of carnitine.
Formal Description
Interaction-ID: 39450

gene/protein

OCTN3

affects_activity of

process

renal carnitine reabsorption

in kidney
Comment Administration of oxidized fat for 6 d causes an elevation of OCTN2 transcript levels in liver and small intestine and increases hepatic carnitine concentration of rats indicating that carnitine homeostasis is regulated also by nutritive PPARalpha activators.
Formal Description
Interaction-ID: 39451

environment

oxidized fat diet

increases_expression of

gene/protein

SLC22A5

in liver, in small intestine
Drugbank entries Show/Hide entries for SLC22A5
Comment Administration of oxidized fat for 6 d causes an elevation of OCTN2 transcript levels in liver and small intestine and increases hepatic carnitine concentration of rats indicating that carnitine homeostasis is regulated also by nutritive PPARalpha activators.
Formal Description
Interaction-ID: 39452

environment

oxidized fat diet

increases_quantity of

drug/chemical compound

Carnitine

in liver
Comment In humans 48 h starvation caused a slight decrease in the urinary excretion of free carnitine and a marked increase in that of acetyl carnitine. Albeit being speculative, the reduced urinary excretion of free carnitine in the starved subjects may be indicative of a PPARalpha-induced increase in the tubular reabsorption of carnitine in the kidney which is possibly mediated by an upregulation of OCTN2.
Formal Description
Interaction-ID: 39453

environment

fasting

decreases_quantity of

drug/chemical compound

Carnitine

in urine
Comment In humans 48 h starvation caused a slight decrease in the urinary excretion of free carnitine and a marked increase in that of acetyl carnitine. Albeit being speculative, the reduced urinary excretion of free carnitine in the starved subjects may be indicative of a PPARalpha-induced increase in the tubular reabsorption of carnitine in the kidney which is possibly mediated by an upregulation of OCTN2.
Formal Description
Interaction-ID: 39454

environment

fasting

increases_quantity of

drug/chemical compound

Acetylcarnitine

in urine
Comment In a study with human subjects, from which skeletal muscle biopsies were taken, no change in skeletal muscle carnitine levels were found in patients under starvation conditions.
Formal Description
Interaction-ID: 39455

environment

fasting

NOT affects_quantity of

drug/chemical compound

Carnitine

in skeletal muscle
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39457

gene/protein

CPT1A

affects_activity of

Drugbank entries Show/Hide entries for CPT1A
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39458

gene/protein

CPT1B

affects_activity of

Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39459

gene/protein

CPT1C

affects_activity of

Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39460

gene/protein

SLC25A20

affects_activity of

Drugbank entries Show/Hide entries for SLC25A20
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39461

gene/protein

PPARA

affects_expression of

gene/protein

CPT1A

Drugbank entries Show/Hide entries for PPARA or CPT1A
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39463

gene/protein

PPARA

affects_expression of

gene/protein

CPT1B

Drugbank entries Show/Hide entries for PPARA
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39464

gene/protein

PPARA

affects_expression of

gene/protein

CPT1C

Drugbank entries Show/Hide entries for PPARA
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39465

gene/protein

PPARA

affects_expression of

gene/protein

SLC25A20

Drugbank entries Show/Hide entries for PPARA or SLC25A20
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39466

gene/protein

PPARD

affects_expression of

gene/protein

CPT1A

Drugbank entries Show/Hide entries for PPARD or CPT1A
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39467

gene/protein

PPARD

affects_expression of

gene/protein

CPT1B

Drugbank entries Show/Hide entries for PPARD
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39468

gene/protein

PPARD

affects_expression of

gene/protein

CPT1C

Drugbank entries Show/Hide entries for PPARD
Comment Genes encoding proteins of the carnitine shuttle system, such as carnitine-palmitoyltransferase I and carnitine-acylcanitine translocase, were shown to be regulated by both PPARalpha and PPARdelta.
Formal Description
Interaction-ID: 39469

gene/protein

PPARD

affects_expression of

gene/protein

SLC25A20

Drugbank entries Show/Hide entries for PPARD or SLC25A20