General Information:

Id: 664
Diseases: Diabetes mellitus, type I - [OMIM]
Diabetes mellitus, type II - [OMIM]
Hypothyroidism
Insulin resistance
Mammalia
review
Reference: Coleman RA et al.(2000) Physiological and nutritional regulation of enzymes of triacylglycerol synthesis Annu. Rev. Nutr. 20: 77-103 [PMID: 10940327]

Interaction Information:

Comment Long-chain acyl-CoA synthetase (ACS) catalyzes the initial enzymatic step required for oxidation, elongation, and desaturation of fatty acids, and for the synthesis of complex lipids and acylated proteins. Tissues like liver and adipocytes express several different acyl-CoA synthetase isoforms.
Formal Description
Interaction-ID: 3555

gene/protein

ACS

affects_activity of

Drugbank entries Show/Hide entries for ACS
Comment Long-chain acyl-CoA synthetase (ACS) catalyzes the initial enzymatic step required for oxidation, elongation, and desaturation of fatty acids, and for the synthesis of complex lipids and acylated proteins. Tissues like liver and adipocytes express several different acyl-CoA synthetase isoforms.
Formal Description
Interaction-ID: 3564

gene/protein

ACS

affects_activity of

Drugbank entries Show/Hide entries for ACS
Comment Long-chain acyl-CoA synthetase (ACS) catalyzes the initial enzymatic step required for oxidation, elongation, and desaturation of fatty acids, and for the synthesis of complex lipids and acylated proteins.
Formal Description
Interaction-ID: 3565

gene/protein

ACS

affects_activity of

Drugbank entries Show/Hide entries for ACS
Comment Long-chain acyl-CoA synthetase (ACS) catalyzes the initial enzymatic step required for oxidation, elongation, and desaturation of fatty acids, and for the synthesis of complex lipids and acylated proteins. Tissues like liver and adipocytes express several different acyl-CoA synthetase isoforms.
Formal Description
Interaction-ID: 3566

gene/protein

ACS

affects_activity of

Drugbank entries Show/Hide entries for ACS
Comment The active site of acyl-CoA synthetase (ACS) lies on the cytosolic surface of the peroxisomal, endoplasmic reticulum, and outer mitochondrial membranes.
Formal Description
Interaction-ID: 3567

gene/protein

ACS

is localized in

cellular component

endoplasmic reticulum membrane

Drugbank entries Show/Hide entries for ACS
Comment The active site of acyl-CoA synthetase (ACS) lies on the cytosolic surface of the peroxisomal, endoplasmic reticulum, and outer mitochondrial membranes.
Formal Description
Interaction-ID: 3570

gene/protein

ACS

is localized in

cellular component

mitochondrial outer membrane

Drugbank entries Show/Hide entries for ACS
Comment The active site of acyl-CoA synthetase (ACS) lies on the cytosolic surface of the peroxisomal, endoplasmic reticulum, and outer mitochondrial membranes.
Formal Description
Interaction-ID: 3571

gene/protein

ACS

is localized in

cellular component

peroxisomal membrane

Drugbank entries Show/Hide entries for ACS
Comment Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial and committed step in the de novo synthesis of triacylglycerols and all cellular phospholipids except sphingomyelin.
Formal Description
Interaction-ID: 3575

gene/protein

GPAT

affects_activity of

Comment Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial and committed step in the de novo synthesis of triacylglycerols and all cellular phospholipids except sphingomyelin.
Formal Description
Interaction-ID: 3576

gene/protein

GPAT

affects_activity of

Comment Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial and committed step in the de novo synthesis of triacylglycerols and all cellular phospholipids except sphingomyelin.
Formal Description
Interaction-ID: 3577

gene/protein

GPAT

NOT affects_activity of

Comment Glycerol-3-phosphate acyltransferase (GPAT) isoforms are found in the endoplasmic reticulum and in the outer mitochondrial membrane, the active sites face the cytosol. In tissues other than liver, microsomal GPAT activity is approximately 10 times that of the mitochondrial fraction.
Formal Description
Interaction-ID: 3578

gene/protein

GPAT

is localized in

cellular component

endoplasmic reticulum membrane

Comment Glycerol-3-phosphate acyltransferase (GPAT) isoforms are found in the endoplasmic reticulum and in the outer mitochondrial membrane, the active sites face the cytosol. In tissues other than liver, microsomal GPAT activity is approximately 10 times that of the mitochondrial fraction.
Formal Description
Interaction-ID: 3580

gene/protein

GPAT

is localized in

cellular component

mitochondrial outer membrane

Comment Lysophosphatidic acid acyltransferase (LPAAT, now AGPAT 1-acyl-sn-glycerol-3-phosphate acyltransferase ) catalyzes the second step in the triacylglycerol synthesis, the acylation of sn-1-acyl-glycerol-3-phosphate at the sn-2 position to form phosphatidic acid.
Formal Description
Interaction-ID: 3583

gene/protein

AGPAT

affects_activity of

Comment Several isoforms of lysophosphatidic acid acyltransferase (LPAAT, AGPAT) exist, they are found in the endoplasmic reticulum and in mitochondria.
Formal Description
Interaction-ID: 3588

gene/protein

AGPAT

is localized in

cellular component

endoplasmic reticulum membrane

Comment Several isoforms of lysophosphatidic acid acyltransferase (LPAAT, AGPAT) exist, they are found in the endoplasmic reticulum and in mitochondria.
Formal Description
Interaction-ID: 3589

gene/protein

AGPAT

is localized in

cellular component

mitochondrial outer membrane

Comment Phosphatidate phosphohydrolase (PPH-1, now LPIN1) is unique among the enzymes of the triacylglycerol synthesis in that it is amphipatic and probably hydrolyzes phosphatidic acid to form diacylglycerol only when it associates with the endoplasmic reticulum.
Formal Description
Interaction-ID: 3590

gene/protein

LPIN1

is localized in

cellular component

cytoplasm

associated with endoplasmic reticulum membrane
Comment Phosphatidate phosphohydrolase (PPH-1, now LPIN1) is unique among the enzymes of the triacylglycerol synthesis in that it is amphipatic and probably hydrolyzes phosphatidic acid to form diacylglycerol only when it associates with the endoplasmic reticulum.
Formal Description
Interaction-ID: 3602

gene/protein

LPIN1

interacts (colocalizes) with

cellular component

endoplasmic reticulum membrane

Comment Phosphatidate phosphohydrolase (PPH-1, now LPIN1) is unique among the enzymes of the triacylglycerol synthesis in that it is amphipatic and probably hydrolyzes phosphatidic acid to form diacylglycerol only when it associates with the endoplasmic reticulum.
Formal Description
Interaction-ID: 3603

gene/protein

LPIN1

affects_activity of

Comment In addition to catalyzing the first reaction in the synthesis of ether lipids, peroxisomal dihydroxyacetone-phosphate-acyltransferase (DHAPAT) can also provide an alternate route for LPA synthesis via the acylation of dihydroxyacetone-P and the subsequent reduction of the 1-acyl-dihydroxyacetonephosphate product to lysophosphatidic acid. It is not known whether this route provides any significant amount of lysophosphatidic acid for triacylglycerol synthesis.
Formal Description
Interaction-ID: 3604

gene/protein

GNPAT

affects_activity of

Comment In addition to catalyzing the first reaction in the synthesis of ether lipids, peroxisomal dihydroxyacetone-phosphate-acyltransferase (DHAPAT) can also provide an alternate route for LPA synthesis via the acylation of dihydroxyacetone-P and the subsequent reduction of the 1-acyl-dihydroxyacetonephosphate product to lysophosphatidic acid. It is not known whether this route provides any significant amount of lysophosphatidic acid for triacylglycerol synthesis.
Formal Description
Interaction-ID: 3615

gene/protein

GNPAT

affects_activity of

Comment Dihydroxyacetone-phosphate-acyltransferase (DHAPAT) is located in peroxisomes.
Formal Description
Interaction-ID: 3617

gene/protein

GNPAT

is localized in

cellular component

peroxisomal membrane

Comment Absence of dihydroxyacetone-phosphate-acyltransferase (DHAPAT) in humans causes severe neurological impairment and skeletal deformities, but no alteration in triacylglycerol synthesis.
Formal Description
Interaction-ID: 3625

gene/protein

GNPAT

affects_activity of

disease

Neurological impairment

Comment Intestinal monoacylglycerol acyltransferase (MGAT) provides an alternate route for triacylglycerol synthesis by reacylating diet-derived sn-2-monoacylglycerols.
Formal Description
Interaction-ID: 3628

gene/protein

MOGAT

affects_activity of

in intestinal mucosa
Comment Diacylglycerol acyltransferase (DGAT), the enzyme unique to triacylglycerol synthesis, acylates diacylglycerol at the sn-3 position using either long- or medium-chain acyl-CoAs, and its highest activity is in tissues that specialize in TAG biosynthesis: adipose, liver, lactating mammary gland, small intestinal mucosa, and adrenal.
Formal Description
Interaction-ID: 3638

gene/protein

DGAT

affects_activity of

Comment Diacylglycerol acyltransferase (DGAT) is localized in the endoplasmic reticulum membrane.
Formal Description
Interaction-ID: 3640

gene/protein

DGAT

is localized in

cellular component

endoplasmic reticulum membrane

Comment Enzymes involved in triacylglycerol synthesis are coordinately regulated through the counter-regulatory hormones insulin and glucagon: insulin increases and the diabetic state reduces the activities of lipogenic enzymes.
Formal Description
Interaction-ID: 3643

complex/PPI

Insulin

increases_activity of

Comment Enzymes involved in triacylglycerol synthesis are coordinately regulated through the counter-regulatory hormones insulin and glucagon: insulin increases and the diabetic state reduces the activities of lipogenic enzymes.
Formal Description
Interaction-ID: 3646

gene/protein

Glucagon

decreases_activity of

Comment Enzymes involved in triacylglycerol synthesis are coordinately regulated through the counter-regulatory hormones insulin and glucagon: insulin increases and the diabetic state reduces the activities of lipogenic enzymes.
Formal Description
Interaction-ID: 3648

decreases_activity of

Comment Streptozotocin-induced diabetes decreased fatty acid synthase activity 39 %, mitochondrial GPAT activity 62 %, microsomal GPAT activity 32 %, and PPH-1 activity 37 % in rat epididymal fat pads, and insulin administration restored these enzyme activities.
Formal Description
Interaction-ID: 3651

disease

Streptozocin-induced diabetes

decreases_activity of

gene/protein

FASN

Drugbank entries Show/Hide entries for FASN
Comment Streptozotocin-induced diabetes decreased fatty acid synthase activity 39 %, mitochondrial GPAT activity 62 %, microsomal GPAT activity 32 %, and PPH-1 activity 37 % in rat epididymal fat pads, and insulin administration restored these enzyme activities.
Formal Description
Interaction-ID: 3663

disease

Streptozocin-induced diabetes

decreases_activity of

gene/protein

Mitochondrial GPAT

Comment Streptozotocin-induced diabetes decreased fatty acid synthase activity 39 %, mitochondrial GPAT activity 62 %, microsomal GPAT activity 32 %, and PPH-1 activity 37 % in rat epididymal fat pads, and insulin administration restored these enzyme activities.
Formal Description
Interaction-ID: 3664

disease

Streptozocin-induced diabetes

decreases_activity of

gene/protein

Microsomal GPAT

Comment Streptozotocin-induced diabetes decreased fatty acid synthase activity 39 %, mitochondrial GPAT activity 62 %, microsomal GPAT activity 32 %, and PPH-1 activity 37 % in rat epididymal fat pads, and insulin administration restored these enzyme activities.
Formal Description
Interaction-ID: 3665

disease

Streptozocin-induced diabetes

decreases_activity of

gene/protein

LPIN1

Comment Although diabetes decreases TAG synthetic enzymes in white adipocytes, it has no effect on these activities in brown adipocytes, despite an 80% decrease in the flux of (C14)glucose into triacylglycerol.
Formal Description
Interaction-ID: 3666

decreases_activity of

in white adipose tissue
Comment Although diabetes decreases TAG synthetic enzymes in white adipocytes, it has no effect on these activities in brown adipocytes, despite an 80% decrease in the flux of (C14)glucose into triacylglycerol.
Formal Description
Interaction-ID: 3668

NOT affects_activity of

in brown adipose tissue
Comment In perfused rat livers, insulin increases mitochondrial GPAT activity 34 % and microsomal GPAT activity 9 %.
Formal Description
Interaction-ID: 3669

complex/PPI

Insulin

increases_activity of

gene/protein

GPAT

Comment Thyroid hormone may also play a role in regulating enzymes of triacylglycerol synthesis, as hypothyroidism increases the activity of microsomal GPAT and DGAT and decreases mitochondrial GPAT and PPH-1.
Formal Description
Interaction-ID: 3671

increases_activity of

gene/protein

Microsomal GPAT

Comment Thyroid hormone may also play a role in regulating enzymes of triacylglycerol synthesis, as hypothyroidism increases the activity of microsomal GPAT and DGAT and decreases mitochondrial GPAT and PPH-1.
Formal Description
Interaction-ID: 3673

increases_activity of

gene/protein

DGAT

Comment Thyroid hormone may also play a role in regulating enzymes of triacylglycerol synthesis, as hypothyroidism increases the activity of microsomal GPAT and DGAT and decreases mitochondrial GPAT and PPH-1.
Formal Description
Interaction-ID: 3674

decreases_activity of

gene/protein

Mitochondrial GPAT

Comment Thyroid hormone may also play a role in regulating enzymes of triacylglycerol synthesis, as hypothyroidism increases the activity of microsomal GPAT and DGAT and decreases mitochondrial GPAT and PPH-1.
Formal Description
Interaction-ID: 3675

decreases_activity of

gene/protein

LPIN1

Comment Mitochondrial GPAT is positively regulated byt the cholesterol-responsive transcription factor SREBP-1, which up-regulates the synthesis of mRNAs for key regulatory enzymes or cholesterol and fatty acid synthesis.
Formal Description
Interaction-ID: 3676

gene/protein

SREBF1

increases_expression of

gene/protein

Mitochondrial GPAT

Comment In liver, over-expression of SREBP-1c increases fatty acid synthase mRNA threefold, and over-expression of SREBP-1a results in a tenfold increase in mRNAs of both fatty acid synthase and mitochondrial GPAT.
Formal Description
Interaction-ID: 3679

mRNA/protein variant

SREBF1c

increases_expression of

gene/protein

FASN

in liver
Drugbank entries Show/Hide entries for FASN
Comment In liver, over-expression of SREBP-1c increases fatty acid synthase mRNA threefold, and over-expression of SREBP-1a results in a tenfold increase in mRNAs of both fatty acid synthase and mitochondrial GPAT.
Formal Description
Interaction-ID: 3682

mRNA/protein variant

SREBF1a

increases_expression of

gene/protein

FASN

in liver
Drugbank entries Show/Hide entries for FASN
Comment In liver, over-expression of SREBP-1c increases fatty acid synthase mRNA threefold, and over-expression of SREBP-1a results in a tenfold increase in mRNAs of both fatty acid synthase and mitochondrial GPAT.
Formal Description
Interaction-ID: 3683

mRNA/protein variant

SREBF1a

increases_expression of

gene/protein

Mitochondrial GPAT

in liver
Comment SREBP and insulin-stimulated transcription of fatty acid synthase and mitochondrial GPAT mRNA may bei linked, SREBP-1c expression is itself regulated by an animal's nutritional state and by insulin.
Formal Description
Interaction-ID: 3684

complex/PPI

Insulin

affects_expression of

mRNA/protein variant

SREBF1c

Comment Dietary polyunsaturated fatty acid (PUFA) decreases the transcription of hepatic genes encoding such lipogenic enzymes as fatty acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, and malic enzyme, while concurrently increasing transcription of genes that encode enzymes required fo fatty acid oxidation, including carnithine palmitoyltransferase 1.
Formal Description
Interaction-ID: 3685

drug/chemical compound

Polyunsaturated fatty acid

decreases_expression of

gene/protein

FASN

in liver
Drugbank entries Show/Hide entries for FASN
Comment Dietary polyunsaturated fatty acid (PUFA) decreases the transcription of hepatic genes encoding such lipogenic enzymes as fatty acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, and malic enzyme, while concurrently increasing transcription of genes that encode enzymes required fo fatty acid oxidation, including carnithine palmitoyltransferase 1.
Formal Description
Interaction-ID: 3687

drug/chemical compound

Polyunsaturated fatty acid

decreases_expression of

gene/protein

ACACB

in liver
Drugbank entries Show/Hide entries for ACACB
Comment Dietary polyunsaturated fatty acid (PUFA) decreases the transcription of hepatic genes encoding such lipogenic enzymes as fatty acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, and malic enzyme, while concurrently increasing transcription of genes that encode enzymes required fo fatty acid oxidation, including carnithine palmitoyltransferase 1.
Formal Description
Interaction-ID: 3688

drug/chemical compound

Polyunsaturated fatty acid

decreases_expression of

gene/protein

SCD

in liver
Comment Dietary polyunsaturated fatty acid (PUFA) decreases the transcription of hepatic genes encoding such lipogenic enzymes as fatty acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, and malic enzyme, while concurrently increasing transcription of genes that encode enzymes required fo fatty acid oxidation, including carnithine palmitoyltransferase 1.
Formal Description
Interaction-ID: 3689

drug/chemical compound

Polyunsaturated fatty acid

decreases_expression of

gene/protein

ME

in liver
Comment Dietary polyunsaturated fatty acid (PUFA) decreases the transcription of hepatic genes encoding such lipogenic enzymes as fatty acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, and malic enzyme, while concurrently increasing transcription of genes that encode enzymes required fo fatty acid oxidation, including carnitine palmitoyltransferase 1.
Formal Description
Interaction-ID: 3690

drug/chemical compound

Polyunsaturated fatty acid

increases_expression of

gene/protein

CPT1

in liver
Comment Leptin regulates lipid homeostasis in adipose tissue, lver, muscle, and pancreas by up-regulating mRNA expression of oxidative enzymes, and by stimulating fatty acid oxidation.
Formal Description
Interaction-ID: 3700

gene/protein

LEP

increases_activity of

in adipose tissue, in liver, in muscle, in pancreas, in pancreatic islet
Comment In lean ZDF rats, adenovirus-mediated hyperleptinemia markedly decreases adipose tissue mRNA expression of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT.
Formal Description
Interaction-ID: 3702

gene/protein

LEP

affects_expression of

gene/protein

ACACA

in adipose tissue; in lean ZDF rats
Drugbank entries Show/Hide entries for ACACA
Comment In lean ZDF rats, adenovirus-mediated hyperleptinemia markedly decreases adipose tissue mRNA expression of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT.
Formal Description
Interaction-ID: 3704

gene/protein

LEP

affects_expression of

gene/protein

FASN

in adipose tissue; in lean ZDF rats
Drugbank entries Show/Hide entries for FASN
Comment In lean ZDF rats, adenovirus-mediated hyperleptinemia markedly decreases adipose tissue mRNA expression of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT.
Formal Description
Interaction-ID: 3705

gene/protein

LEP

affects_expression of

gene/protein

Mitochondrial GPAT

in adipose tissue; in lean ZDF rats
Comment In isolated islets from lean ZDF rats, leptin decreases mitochondrial GPAT and acetyl-CoA carboxylase mRNA expression 75 % - 80 %, and adding leptin to rat adipocytes decreases fatty acid synthase mRNA 90 % and increases PPARalpha mRNA twofold.
Formal Description
Interaction-ID: 3707

gene/protein

LEP

decreases_expression of

gene/protein

Mitochondrial GPAT

in pancreas, in pancreatic islets; in lean ZDF rats
Comment In isolated islets from lean ZDF rats, leptin decreases mitochondrial GPAT and acetyl-CoA carboxylase mRNA expression 75 % - 80 %, and adding leptin to rat adipocytes decreases fatty acid synthase mRNA 90 % and increases PPARalpha mRNA twofold.
Formal Description
Interaction-ID: 3708

gene/protein

LEP

decreases_expression of

gene/protein

ACACA

in pancreas, in pancreatic islets; in lean ZDF rats
Drugbank entries Show/Hide entries for ACACA
Comment In isolated islets from lean ZDF rats, leptin decreases mitochondrial GPAT and acetyl-CoA carboxylase mRNA expression 75 % - 80 %, and adding leptin to rat adipocytes decreases fatty acid synthase mRNA 90 % and increases PPARalpha mRNA twofold.
Formal Description
Interaction-ID: 3709

gene/protein

LEP

decreases_expression of

gene/protein

FASN

in adipose tissue; in lean ZDF rats
Drugbank entries Show/Hide entries for FASN
Comment In isolated islets from lean ZDF rats, leptin decreases mitochondrial GPAT and acetyl-CoA carboxylase mRNA expression 75 % - 80 %, and adding leptin to rat adipocytes decreases fatty acid synthase mRNA 90 % and increases PPARalpha mRNA twofold.
Formal Description
Interaction-ID: 3710

gene/protein

LEP

increases_expression of

gene/protein

PPARA

in adipose tissue; in lean ZDF rats
Drugbank entries Show/Hide entries for PPARA
Comment cAMP-dependent protein kinase inactivates GPAT in rat adipocyte microsomes, liver microsomes, and liver mitochondria.
Formal Description
Interaction-ID: 3711

complex/PPI

Protein kinase A

decreases_activity of

gene/protein

Microsomal GPAT

in adipose tissue, in liver
Comment cAMP-dependent protein kinase inactivates GPAT in rat adipocyte microsomes, liver microsomes, and liver mitochondria.
Formal Description
Interaction-ID: 3713

complex/PPI

Protein kinase A

decreases_activity of

gene/protein

Mitochondrial GPAT

in liver
Comment Phosphatidylinositol-specific phospholipase C mimics the insulin stimulation of microsomal GPAT in adipocytes and myocytes.
Formal Description
Interaction-ID: 3715

gene/protein

PLC

increases_activity of

gene/protein

Microsomal GPAT

in adipose tissue, in muscle
Drugbank entries Show/Hide entries for PLC
Comment Glucagon and cAMP treatment of hepatocytes results in translocation of PPH-1 to the cytosol, where it is inactive, this translocation is reversed when fatty acid is added.
Formal Description
Interaction-ID: 3721

gene/protein

Glucagon

decreases_activity of

gene/protein

LPIN1

in liver; by translocation of PPH-1 to cytosol
Comment Glucagon and cAMP treatment of hepatocytes results in translocation of PPH-1 to the cytosol, where it is inactive, this translocation is reversed when fatty acid is added.
Formal Description
Interaction-ID: 3722

drug/chemical compound

cAMP

decreases_activity of

gene/protein

LPIN1

in liver; by translocation of PPH-1 to cytosol
Drugbank entries Show/Hide entries for cAMP
Comment Partitioning of fatty acids between degradative and biosynthetic fates appears to be acutely regulated via reciprocal modulation of outer mitochondrial membrane enzymes, carnitine palmitoyltransferase-1 (CPT1) and mitochondrial GPAT. Coordinated regulation of CPT1 and mitochondrial GPAT is mediated by AMP-activated protein kinase (AMPK), which protects cells against the consequences of ATP depletion by inhibiting biosynthetic pathways and stimulating energy-generating pathways.
Formal Description
Interaction-ID: 3752

complex/PPI

AMPK

affects_activity of

Comment In response to increases in the cellular AMP/ATP ratio, AMPK phosphorylates and inactivates liver acetyl-CoA carboxylase and decreases its product, malonyl-CoA, a potent inhibitor of CPT1 and beta-oxidation.
Formal Description
Interaction-ID: 3753

complex/PPI

AMPK

increases_phosphorylation of

gene/protein

ACACB

in liver; if cellular AMP/ATP ratio increases
Drugbank entries Show/Hide entries for ACACB
Comment In response to increases in the cellular AMP/ATP ratio, AMPK phosphorylates and inactivates liver acetyl-CoA carboxylase and decreases its product, malonyl-CoA, a potent inhibitor of CPT1 and beta-oxidation.
Formal Description
Interaction-ID: 3754

complex/PPI

AMPK

decreases_activity of

gene/protein

ACACB

in liver; if cellular AMP/ATP ratio increases
Drugbank entries Show/Hide entries for ACACB
Comment In response to increases in the cellular AMP/ATP ratio, AMPK phosphorylates and inactivates liver acetyl-CoA carboxylase and decreases its product, malonyl-CoA, a potent inhibitor of CPT1 and beta-oxidation.
Formal Description
Interaction-ID: 3755

complex/PPI

AMPK

decreases_quantity of

drug/chemical compound

Malonyl-CoA

in liver; if cellular AMP/ATP ratio increases
Comment In response to increases in the cellular AMP/ATP ratio, AMPK phosphorylates and inactivates liver acetyl-CoA carboxylase and decreases its product, malonyl-CoA, a potent inhibitor of CPT1 and beta-oxidation.
Formal Description
Interaction-ID: 3756

drug/chemical compound

Malonyl-CoA

decreases_activity of

gene/protein

CPT1A

in liver
Drugbank entries Show/Hide entries for CPT1A
Comment In response to increases in the cellular AMP/ATP ratio, AMPK phosphorylates and inactivates liver acetyl-CoA carboxylase and decreases its product, malonyl-CoA, a potent inhibitor of CPT1 and beta-oxidation.
Formal Description
Interaction-ID: 3757

drug/chemical compound

Malonyl-CoA

decreases_activity of

in liver
Comment By decreasing malonyl-CoA, AMPK relieves the inhibition of CPT1 and thereby increases fatty acid oxidation.
Formal Description
Interaction-ID: 3758

complex/PPI

AMPK

increases_activity of

gene/protein

CPT1A

in liver; by decreasing malonyl-CoA inhibition
Drugbank entries Show/Hide entries for CPT1A
Comment By decreasing malonyl-CoA, AMPK relieves the inhibition of CPT1 and thereby increases fatty acid oxidation.
Formal Description
Interaction-ID: 3761

complex/PPI

AMPK

increases_activity of

in liver; by decreasing malonyl-CoA inhibition
Comment In both muscle and liver, activated AMPK inhibits fatty acid esterification into triacylglycerol (TAG) by AMPK-dependent inactivation of mitochondrial GPAT, but not DGAT or microsomal GPAT.
Formal Description
Interaction-ID: 3762

complex/PPI

AMPK

decreases_activity of

in liver, in muscle
Comment In both muscle and liver, activated AMPK inhibits fatty acid esterification into triacylglycerol (TAG) by AMPK-dependent inactivation of mitochondrial GPAT, but not DGAT or microsomal GPAT.
Formal Description
Interaction-ID: 3764

complex/PPI

AMPK

decreases_activity of

gene/protein

Mitochondrial GPAT

in liver, in muscle
Comment In both muscle and liver, activated AMPK inhibits fatty acid esterification into triacylglycerol (TAG) by AMPK-dependent inactivation of mitochondrial GPAT, but not DGAT or microsomal GPAT.
Formal Description
Interaction-ID: 3765

complex/PPI

AMPK

NOT decreases_activity of

gene/protein

DGAT

in liver, in muscle
Comment In both muscle and liver, activated AMPK inhibits fatty acid esterification into triacylglycerol (TAG) by AMPK-dependent inactivation of mitochondrial GPAT, but not DGAT or microsomal GPAT.
Formal Description
Interaction-ID: 3767

complex/PPI

AMPK

NOT decreases_activity of

gene/protein

Microsomal GPAT

in liver, in muscle
Comment Because AMPK is activated by physiological stresses such as exercise and starvation, and inactivated by high sucrose feeding, AMPK-mediated regulation of mitochondrial GPAT could provide a mechanism whereby acute changes in energy status produce immediate adjustments in cellular TAG synthesis.
Formal Description
Interaction-ID: 3768

environment

exercise

increases_activity of

complex/PPI

AMPK

Comment Because AMPK is activated by physiological stresses such as exercise and starvation, and inactivated by high sucrose feeding, AMPK-mediated regulation of mitochondrial GPAT could provide a mechanism whereby acute changes in energy status produce immediate adjustments in cellular TAG synthesis.
Formal Description
Interaction-ID: 3771

environment

fasting

increases_activity of

complex/PPI

AMPK

Comment Because AMPK is activated by physiological stresses such as exercise and starvation, and inactivated by high sucrose feeding, AMPK-mediated regulation of mitochondrial GPAT could provide a mechanism whereby acute changes in energy status produce immediate adjustments in cellular TAG synthesis.
Formal Description
Interaction-ID: 3772

environment

high-sucrose diet

decreases_activity of

complex/PPI

AMPK

Comment In rats training decreases intra-abdominal adipose tissue acyl-CoA synthetase (ACS) activity and ACS mRNA levels and increases muscle ACS activity and mRNA expression.
Formal Description
Interaction-ID: 3773

environment

exercise

decreases_activity of

gene/protein

ACS

in intra-abdominal adipose tissue
Drugbank entries Show/Hide entries for ACS
Comment In rats training decreases intra-abdominal adipose tissue acyl-CoA synthetase (ACS) activity and ACS mRNA levels and increases muscle ACS activity and mRNA expression.
Formal Description
Interaction-ID: 3774

environment

exercise

decreases_expression of

gene/protein

ACS

in intra-abdominal adipose tissue
Drugbank entries Show/Hide entries for ACS
Comment In rats training decreases intra-abdominal adipose tissue acyl-CoA synthetase (ACS) activity and ACS mRNA levels and increases muscle ACS activity and mRNA expression.
Formal Description
Interaction-ID: 3775

environment

exercise

increases_activity of

gene/protein

ACS

in muscle
Drugbank entries Show/Hide entries for ACS
Comment In rats training decreases intra-abdominal adipose tissue acyl-CoA synthetase (ACS) activity and ACS mRNA levels and increases muscle ACS activity and mRNA expression.
Formal Description
Interaction-ID: 3776

environment

exercise

increases_expression of

gene/protein

ACS

in muscle
Drugbank entries Show/Hide entries for ACS
Comment When rats are fed diets containing fructose or sucrose, training decreases liver activities of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT (37 % - 60 %) but does not affect the activities of liver microsomal GPAT or muscle mitochondrial GPAT.
Formal Description
Interaction-ID: 3777

environment

exercise and fructose- or sucrose-containing diet

decreases_activity of

gene/protein

ACACB

in liver
Drugbank entries Show/Hide entries for ACACB
Comment When rats are fed diets containing fructose or sucrose, training decreases liver activities of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT (37 % - 60 %) but does not affect the activities of liver microsomal GPAT or muscle mitochondrial GPAT.
Formal Description
Interaction-ID: 3779

environment

exercise and fructose- or sucrose-containing diet

decreases_activity of

gene/protein

FASN

in liver
Drugbank entries Show/Hide entries for FASN
Comment When rats are fed diets containing fructose or sucrose, training decreases liver activities of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT (37 % - 60 %) but does not affect the activities of liver microsomal GPAT or muscle mitochondrial GPAT.
Formal Description
Interaction-ID: 3780

environment

exercise and fructose- or sucrose-containing diet

decreases_activity of

gene/protein

Mitochondrial GPAT

in liver
Comment When rats are fed diets containing fructose or sucrose, training decreases liver activities of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT (37 % - 60 %) but does not affect the activities of liver microsomal GPAT or muscle mitochondrial GPAT.
Formal Description
Interaction-ID: 3781

environment

exercise and fructose- or sucrose-containing diet

NOT affects_activity of

gene/protein

Microsomal GPAT

in liver
Comment When rats are fed diets containing fructose or sucrose, training decreases liver activities of acetyl-CoA carboxylase, fatty acid synthase, and mitochondrial GPAT (37 % - 60 %) but does not affect the activities of liver microsomal GPAT or muscle mitochondrial GPAT.
Formal Description
Interaction-ID: 3782

environment

exercise and fructose- or sucrose-containing diet

NOT affects_activity of

gene/protein

Mitochondrial GPAT

in muscle
Comment Triacylglycerol (TAG) accumulation in muscle and pancreas occurs with insulin resistance and islet cell dysfunction, respectively.
Formal Description
Interaction-ID: 3783

cooccurs with

disease

Insulin resistance

Comment In type 2 diabetes, both hepatic triacylglycerol (TAG) sunthesis in liver and VLDL secretion increase.
Formal Description
Interaction-ID: 3784

increases_activity of

in liver
Comment In type 2 diabetes, both hepatic triacylglycerol (TAG) sunthesis in liver and VLDL secretion increase.
Formal Description
Interaction-ID: 3785

increases_activity of

in liver
Comment Absence of dihydroxyacetone-phosphate-acyltransferase (DHAPAT) in humans causes severe neurological impairment and skeletal deformities, but no alteration in triacylglycerol synthesis.
Formal Description
Interaction-ID: 12319

gene/protein

GNPAT

affects_activity of

phenotype

skeletal deformities

Comment Absence of dihydroxyacetone-phosphate-acyltransferase (DHAPAT) in humans causes severe neurological impairment and skeletal deformities, but no alteration in triacylglycerol synthesis.
Formal Description
Interaction-ID: 12320

gene/protein

GNPAT

NOT affects_activity of

Comment Triacylglycerol (TAG) accumulation in muscle and pancreas occurs with insulin resistance and islet cell dysfunction, respectively.
Formal Description
Interaction-ID: 13043

cooccurs with

phenotype

islet cell dysfunction