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acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
acyl-CoA + sn-glycerol 3-phosphate
CoA + lysophosphatidic acid
-
-
-
-
?
fatty acyl-CoA + glycerol-3-phosphate
CoA + lysophosphatidic acid
lauroyl-CoA + sn-glycerol 3-phosphate
CoA + 1-lauroyl-sn-glycerol 3-phosphate
-
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
palmitoyl-CoA + glycerol-3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
activity assay
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
-
less than 20% of activity with palmitoyl-CoA
-
?
additional information
?
-
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
acyl-CoA specificity of GPAT1 is 16:0 > 18:0 > 18:1
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
i.e. lysophosphatidic acid
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
no activity with hexanoyl-CoA, enzyme prefers saturated fatty acyl-CoAs
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
enzyme catalyzes the initial and rate-limiting step of glycerolipid synthesis with long-chain acyl-CoAs
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
key enzyme in de novo triacylglycerol synthesis
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
acylation of sn-glycerol 3-phosphate with longchain acyl-CoA
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
GPAT2 shows no acyl-CoA specificity
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
GPAT3 shows a specificity for 16:0, 18:1, 18:2 acyl-CoAs
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
GPAT4 shows no acyl-CoA specificity
-
-
?
fatty acyl-CoA + glycerol-3-phosphate
CoA + lysophosphatidic acid
-
-
-
-
?
fatty acyl-CoA + glycerol-3-phosphate
CoA + lysophosphatidic acid
-
-
-
?
fatty acyl-CoA + glycerol-3-phosphate
CoA + lysophosphatidic acid
-
long-chain fatty acyl-CoA
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
recombinant mitochondrial acyltransferase prefers palmitoyl-CoA over oleoyl-CoA
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
best acyl-donor
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
preferred substrate of isozyme mtGPAT1, not of isozyme mtGPAT2
-
-
?
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
-
the mitochondrial and microsomal isozymes show different substrate specificity
-
-
?
additional information
?
-
-
mtGPAT1 is essential for normal acyl-CoA metabolism: The absence of hepatic mtGPAT1 results in the partitioning of fatty acids away from triacylglycerol synthesis and toward oxidation and ketogenesis
-
-
?
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acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
acyl-CoA + sn-glycerol 3-phosphate
CoA + lysophosphatidic acid
-
-
-
-
?
additional information
?
-
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
i.e. lysophosphatidic acid
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
enzyme catalyzes the initial and rate-limiting step of glycerolipid synthesis with long-chain acyl-CoAs
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
key enzyme in de novo triacylglycerol synthesis
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
acylation of sn-glycerol 3-phosphate with longchain acyl-CoA
-
-
?
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway
-
-
-
additional information
?
-
-
mtGPAT1 is essential for normal acyl-CoA metabolism: The absence of hepatic mtGPAT1 results in the partitioning of fatty acids away from triacylglycerol synthesis and toward oxidation and ketogenesis
-
-
?
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-
brenda
the expression of GPAT2 is downregulated when 3T3-L1 cells differentiate into adipocytes, while GPAT1, 3, and 4 are upregulated (10fold, over 60, and 5fold, respectively)
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brown and white, high expression level
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-
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-
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lowest expression level
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-
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highest expression level
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low expression level
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-
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moderate expression
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GPAT3 colocalize with the PAT (perilipin) family protein TIP47 (PLIN3) to the apical surface of the enterocyte
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highest expression
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low expression level
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-
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-
CD4+
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-
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bone marrow-derived macrophages
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during lactation, GPAT4 mRNA is highly expressed in mammary gland epithelium, but not in the surrounding adipocytes of breast tissue
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inner medullary collecting duct 3 cell
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GPAT4 is expressed in around spermatids but not elongated spermatids during later spermiogenesis
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moderate expression
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-
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-
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-
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-
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primary hepatocyte
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-
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high expression level
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hypothesis: increased hepatic mtGPAT activity associated with obesity and insulin resistance contributes to increased triacylglycerol biosynthesis and inhibition of fatty acid oxidation, responses that would promote hepatic steatosis and dyslipidemia
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mRNA expression is induced by insulin
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-
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-
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-
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-
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pre- and post-adipocytes
brenda
Gpat3 mRNA increases 60fold during differentiation of 3T3-L1 preadipocytes to mature adipocytes, suggesting a critical role in adipocytes
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-
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-
mitochondrial acyltransferase
brenda
-
GPAT3 mRNA is dramatically upregulated during adipocyte differentiation
brenda
the expression of GPAT2 is downregulated when 3T3-L1 cells differentiate into adipocytes, while GPAT1, 3, and 4 are upregulated (10fold, over 60, and 5fold, respectively)
brenda
the expression of GPAT2 is downregulated when 3T3-L1 cells differentiate into adipocytes, while GPAT1, 3, and 4 are upregulated 10fold, over 60fold, and 5fold, respectively
brenda
-
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high expression level
brenda
expression detected by RT-PCR
brenda
highest expression in white adipose tissue, moderate in brown adipose tissue
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-
-
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-
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-
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moderate expression
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low expression level
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-
-
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-
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-
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-
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high expression
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-
-
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-
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-
-
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-
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-
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low expression
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moderate expression
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high expression level
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-
-
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-
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-
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-
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moderate expression
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-
-
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-
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-
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-
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moderate expression
brenda
moderate expression level
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-
-
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-
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-
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-
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-
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-
mitochondrial acyltransferase
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moderate expression
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low expression level
brenda
-
mitochondrial glycerol-3-phosphate acyltransferase-1 is essential in liver for the metabolism of excess acyl-CoAs
brenda
expression detected by RT-PCR
brenda
GPAT4 accounts for the primary microsomal GPAT activity in liver
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-
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moderate expression
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-
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low expression
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moderate expression
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low to moderate expression level
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-
-
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-
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-
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highest expression
brenda
high expression level, GPAT3 expression analysis throughout the small intestine reveals that GPAT3 is abundantly expressed in the apical surface of enterocytes in the small intestine
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-
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-
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-
-
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-
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moderate expression
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-
-
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-
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high expression
brenda
expression detected by RT-PCR: GPAT4 is strongly expressed in testis. First expression is detected in mice at 2 weeks postnatally. Expression is abundant from the third week, plateaus at week 5-6 and then maintains at a high level in the adult
brenda
GPAT2 expression in mouse testis fluctuates during sexual maturation, Gpat2 expression in mouse testis is maximal at the pachytene stage
brenda
GPAT2 is mainly expressed in pachytene spermatocytes of testis
brenda
GPAT4 is widely expressed postnatally in spermatocytes and around spermatids in mice testis
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-
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-
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low level
brenda
moderate expression
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
tissue distribution, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
expression pattern of GPAT isozymes, overview
brenda
additional information
GPAT2 mRNA expression is increased and the content of triacylglycerol is significantly elevated in testis during sexual maturation in mice. Tissue distribution, overview
brenda
additional information
GPAT2 mRNA expression is increased and the content of triacylglycerol is significantly elevated in testis during sexual maturation in mice. Tissue distribution, overview
brenda
additional information
GPAT2 mRNA expression is increased and the content of triacylglycerol is significantly elevated in testis during sexual maturation in mice. Tissue distribution, overview
brenda
additional information
GPAT2 mRNA expression is increased and the content of triacylglycerol is significantly elevated in testis during sexual maturation in mice. Tissue distribution, overview
brenda
additional information
GPAT3 is predominantly expressed in the small intestine and adipose tissue, tissue distribution and expression pattern, overview
brenda
additional information
-
GPAT3 is predominantly expressed in the small intestine and adipose tissue, tissue distribution and expression pattern, overview
brenda
additional information
the GPAT2 isoform expression is restricted to male germ cells and cancer cells
brenda
additional information
-
the GPAT2 isoform expression is restricted to male germ cells and cancer cells
brenda
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malfunction
GPAT1 -/- mice contain reduced amounts of C16:0 and increased C18:0 and C18:1 in liver phosphatidylcholine and phosphatidylethanolamine. Phosphatidylcholine and phosphatidylethanolamine in Gpat1-/- liver also contain 40% more C20:4 at the sn-2 position, suggesting that esterification at the sn-2 position is influenced by fatty acids at the sn-1 position. GPAT1 overexpression in liver of mice leads to increased incorporation of C16:0 fatty acids into lysophosphatidic acid, diacylglycerol, triacylglycerol
malfunction
GPAT1-deficient mice fed a high-fat/high sucrose diet have reduced hepatic triacylglycerol but increased plasma beta-hydroxybutyrate and liver acylcarnitine levels, suggesting enhanced beta-oxidation. In the high-fat-fed GPAT1-deficient mice, elevated beta-oxidation is associated with increased hepatic acyl-CoA content and activation state of AMP-activated protein kinase. These results suggest that enhanced beta-oxidation represents increased energy flow to fatty acid oxidation caused by a blockage of the glycerolipid synthesis pathway. In GPAT1-overexpressing mice, liver fatty acid oxidation measured ex vivo is decreased. Due to the enhanced beta-oxidation in Gpat1-/- mice, liver mitochondria exhibit a greater mitochondrial dysfunction (oxidative stress, increased hepatocyte apoptosis, lower level odf DNA repair genes)
malfunction
overexpression of GPAT1 in CHO, HEK-293 and primary rodent hepatocytes is sufficient to increase fatty acid incorporation into triglycerides and phospholipids. Gpat1-/- mice have a severe block in hepatic de novo synthesis of total phospholipids. Knockout of GPAT1 activity in cardiomyocytes and hepatocytes increases the arachidonate and oleate content of phosphocholine and phosphoethanolamine. Gpat1-/- mice are less susceptible to carcinogen-induced liver tumorigenesis. Gpat1-/- mice fed a high-sucrose diet to stimulate de novo lipogenesis have a 50% reduction in hepatic and plasma triglycerides, increased hepatic content of long-chain acylcarnitines and reduced very low density lipoprotein (VLDL) secretions. Liver-specific adenoviral expression of GPAT1 results in triglycerides and diacylglycerol accumulation, decreased fatty acid beta-oxidation, and hyperlipidemia
malfunction
the T-cell phenotype under GPAT1 deficiency is comparable to that in an older mice, where GPAT1 activity decreases largely due to immune depression and results in increased susceptibility to infections. T-cells harvested from GPAT1-/- mice show significant reduction in interleukin-2 secretion upon antigen stimulation, and induced apoptosis accompanied by altered mass and composition of phospholipids. LPA produced as a result of increased expression of GPAT1 via glucosamine prevents mouse embryonic stem cells from hypoxia-induced apoptosis through the mammalian target of repamycin (mTOR) activation. The alteration of lipid composition in GPAT1-/- mice decreases the susceptibility to carcinogen-induced liver tumorigenesis. GPAT1 deficiency in ob/ob mice leads to a decrease in hepatic steatosis, triacylglycerol (about 59%), and diacylglycerol (about 74%), leading to the improvement of hepatic and systemic insulin sensitivity. The GPAT1-null mice also exhibit significant decreased plasma glucose levels and lowered plasma TAG content in ob/ob background. The levels of acyl-CoA are observed to be elevated. The overexpression of GPAT1 leads to impaired insulin signaling, reduced insulin-induced suppression of gluconeogenesis, substantially prevents mTOR complex2 (mTORC2) activity, and disassembles the link of mTOR/rictor mediated by PA, which induces peripheral and hepatic insulin resistance
metabolism
relation between three isoforms GPAT1, 3, and 4 and insulin resistance, overview. GPAT1 preferentially catalyzes saturated fatty acids (FAs) (palmitate or C16:0) and selectively transfers acyl-CoA to the sn-1 position of glycerol 3-phosphate. Subsequently, lysophosphatidic acid, phosphatidic acid, and diacylglycerol are produced in the glycerophospholipid pathway. These intermediate substrates serve as the critical component of the ubiquitous biological membranes and mediate intercellular signal transduction. Mitochondrial GPAT1 is a critical regulator of triacylglycerol metabolism and systemic energy homeostasis
metabolism
substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids. The successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, overview
physiological function
Gpat1 mRNA levels increase more than 20fold in mouse liver in an insulin-dependent manner by refeeding of a high-carbohydrate diet after fasting, which is associated with active hepatic lipogenesis
physiological function
the mouse Gpat1 gene promoter region contains three sterol regulatory elements responsible for SREBP-1-mediated transactivation. Ectopic expression of SREBP-1c in 3T3-L1 adipocytes or in liver of transgenic mice dramatically increases Gpat1 mRNA
physiological function
isoform GPAT1-/- hepatocytes are not able to incorporate de novo synthesized fatty acid into triacylglycerol but oxidize twice as much exogenous fatty acid as controls. The hepatic content of long-chain acylcarnitine in fasted Gpat1-/- mice is 3-fold higher than in controls. When compared with control and isoform Gpat-/- mice, after the fasting-refeeding protocol, Gpat1-/- hepatic triacylglycerol is depleted, and long-chain acylcarnitine content is 3.5fold higher
physiological function
GPAT1 dictates fatty acid composition at the level of AGPATs or by acyl-chain remodeling by lysophospholipid acyltransferases (LPLATs). GPAT1 determines the metabolic fate of exogenous fatty acids
physiological function
GPATs play a pivotal role in the regulation of triglyceride and phospholipid synthesis. GPATs play a critical role in the development of obesity, hepatic steatosis, and insulin resistance. Mitochondrial isozyme GPAT1 activity has a huge impact on the regulation of triacylglycerol synthesis, is responsible for 30-50% of the total GPAT activity in the liver and approximately 30% of the total activity in the heart. GPAT1 is regulated at the transcriptional and posttranscriptional levels, and is highly expressed in adipose tissues and liver cells. GPAT1 plays a substantial role in modulating the cytokine production and proliferation of murine T-lymphocytes. Mitochondrial GPAT1 is a critical regulator of triacylglycerol metabolism and systemic energy homeostasis
malfunction
Gpat4-/- mice have severely impaired lactation, a reduced size and number of alveoli, reduced numbers of fat droplets in mammary gland, and reduced triacylglycerol and diacylglycerol content in milk. Gonadal white adipose tissue mass and plasma leptin levels are reduced in Gpat4-/- mice, and subdermal adipose tissue, is nearly absent. The reduced body weight of Gpat4-/- mice is associated with increased energy expenditure
malfunction
-
livers and hearts from mice deficient in GPAT1 (Gpat1 -/-) have a decreased content of glycerolipid intermediates and triacylglycerol, an altered composition of liver phospholipids, and elevated markers of oxidative stress. Compared with control C57BL/6 mice, infection of Gpat1 -/- mice with coxsackievirus B3 results in higher mortality, an 50% increase in heart pathology, a significant increase in liver viral titers, and a 100fold increase in heart viral titers. Heart mRNA levels for proinflammatory cytokines TNF-alpha, IL-6, and IL-1B are increased in the Gpat1-/- mice. Loss of Gpat1 also results in dysregulation of specific immune cells
malfunction
-
T-lymphocyte proliferation is inhibited and activation induced apoptosis is increased in GPAT-1 knockout mice. Th-1 (IL-2 and IFN-gamma) cytokine secretion is reduced, and Th-2 (IL-4 and IL-10) cytokine secretion is increased. An increased arachidonate content and subsequent increased prostaglandin E2 secretion is shown in knockout mice, which may inhibit T-lymphocyte proliferation
malfunction
-
enzyme deficiency results in altered or dysfunctional mitochondria
malfunction
in hepatocytes, the absence of isoform GPAT-1, but not GPAT-4, increases fatty acid oxidation and increases ketogenesis during fasting
malfunction
gene disruption Gpat3-/- mutant mice exhibit attenuated plasma triglyceride excursion and accumulate lipid in the enterocytes, and a lack of lipids in the lamina propria and intercellular space in Gpat3-/- mice. Gpat3-/- enterocytes display a compensatory increase in the synthesis of phospholipid and cholesteryl ester. When fed a Western-type diet, hepatic triglyceride and cholesteryl ester accumulation is significantly higher in Gpat3-/- mice compared with the wild-type mice accompanied by elevated levels of alanine aminotransferase, a marker of liver injury. Dysregulation of bile acid metabolism is also evident in Gpat3-null mice. Although wild-type mice show marked lipid staining in the lamina propria, Gpat3-/- mice exhibit a striking reduction in transitory lipids. Phenotype overview. Analysis of effects of GPAT3 deletion on intestinal lipid profile, gene expression, and gut nutrient sensing
malfunction
Gpat3-/- mice have about 80% reduction in GPAT activity in white adipose tissue, are resistant to weight gain and have improved insulin sensitivity in response to a high-fat diet. In enterocytes from Gpat3-/- mice, excess fatty acids are oxidized and esterified to cholesterol, which are stored and secreted in chylomicrons. Gpat3-/- mice fed a high-fat diet have decreased weight gain, fat mass and enlarged livers, indicating an important role in fatty acid storage in white adipose tissue. Liver enlargement in Gpat3-/- mice is due to cholesterol ester storage resulting from dysregulation of intestinal cholesterol secretion. Overexpression of endoplasmic reticulum-localized GPAT3 or GPAT4 in cultured cells does not affect incorporation of exogenous fatty acids into the major phospholipid classes
malfunction
knockdown of GPAT3 and 4 almost completely prevents the formation of lipid droplets. Deficiency of GPAT greatly reduces TAG synthesis and impairs adipogenesis. Phenotype of GPAT4 knockout mice, overview. The body weight is significantly lower (25%) in GPAT4-/- mice fed with normal chow diet compared to that of the mice in the wild-type group. High fat diet-fed GPAT4-null mice exhibit increased thermogenic gene expression in brown adipose tissue and perform a dramatic hyper-metabolism. The levels of triacylglycerol and diacylglycerol of milk decreases by 90% in GPAT4-null mice due to an extraordinary decline in the number and size of fat droplets in mammary epithelial acinars and ducts. Pups nursed by GPAT4-/- mice die within 48 h after birth unless wild-type mice replace the GPAT4-/- mice to feed the pups. GPAT4 overexpression in hepatocytes leads to impaired insulin-suppressed gluconeogenesis and decreased insulin-stimulated glycogen synthesis, as well as inhibited phosphorylation of Akt (Ser473 and Thr308) stimulated by insulin. Eventually, the changes lead to the impaired glucose homeostasis. Overexpression of GPAT4 inhibits the association between rictor and the mTOR, and even the mTORC2 (mTOR complex 2) activity. Like GPAT1, overexpression of GPAT4 increases the content of phosphatidic acid, which is produced in triacylglycerol synthesis pathway, particularly di16:0-phosphatidic acid. The lipid signal (such as di16:0PA) produced by GPAT4 interferes with the insulin signaling in hepatocytes of mice, which results in hepatic insulin resistance and impaired glucose homeostasis
malfunction
knockdown of GPAT3 and 4 almost completely prevents the formation of lipid droplets. Deficiency of GPAT greatly reduces TAG synthesis and impairs adipogenesis. The activity of GPAT decreases dramatically with GPAT3-specific siRNA knockdown in 3T3-L1 cells, which directly inhibits lipid synthesis. GPAT3-/- mice have increased energy expenditure, improved glucose homeostasis (lower fed glucose level, but not fasting glucose and insulin levels), decreased fat pad size, altered serum lipid levels (increased plasma free cholesterol, especially the low-density lipoprotein cholesterol level, and decreased plasma TAG), but enlarged liver size with increased plasma ALT/AST levels. Inhibition of GPAT3 may improve lipid and glucose metabolism, and provide beneficial effects in the treatment of metabolic diseases. Though increased energy expenditure is observed in both female and male mice. A sexual dimorphism in the GPAT3-deficient phenotype is demonstrated. GPAT3-/- female mice are protected from dietary-induced obesity (DIO) and the hepatic cholesterol metabolism is primarily altered only in GPAT3-/- male mice
malfunction
the gene is silenced in vivo by inoculating lentiviral particles carrying the sequence of a short-hairpin RNA targeting Gpat2 mRNA into mouse testis. Histological and gene expression analysis shows impaired spermatogenesis and arrest at the pachytene stage. The enzyme deficiency triggers apoptotic mechanisms and affects reproductive capacity
malfunction
the liver and brown adipose tissue of Gpat4-/- mice have a 65% reduction in NEM-sensitive GPAT activity, but activity in white adipose tissue is unaffected due to high levels of GPAT3 expression. Female Gpat4-/- mice fed a high-fat diet have increased PPARgamma-mediated Ucp1 expression and thermogenesis in brown adipose tissue resulting from elevated acyl-CoAs due to diminished esterification. Incorporation of exogenous oleate into phospholipid is unaffected in tissues of Gpat4-/- mice. Overexpression of endoplasmic reticulum-localized GPAT3 or GPAT4 in cultured cells does not affect incorporation of exogenous fatty acids into the major phospholipid classes
malfunction
the phagocytic capacity of Gpat3-/- and Gpat4-/- bone marrow-derived macrophages is impaired. Additionally, inhibiting fatty acid beta-oxidation reduces phagocytosis only partially, suggesting that lipid accumulation is not necessary for the energy requirements for phagocytosis
malfunction
the phagocytic capacity of Gpat3-/- and Gpat4-/- bone marrow-derived macrophages is impaired. Additionally, inhibiting fatty acid beta-oxidation reduces phagocytosis only partially, suggesting that lipid accumulation is not necessary for the energy requirements for phagocytosis. Gpat4-/- bone marrow-derived macrophages express and release more pro-inflammatory cytokines and chemokines after macrophage activation
metabolism
isoform GPAT-1, but not GPAT-4, metabolizes fatty acid synthesized de novo from [14C]acetate and diverts fatty acids away from mitochondrial oxidation
metabolism
enzyme GPAT is involved in the glycerolipid synthesis, it is the first and rate-limiting enzyme of the pathway. Glycerolipid synthesis and GPAT3/GPAT4 activity are induced during macrophage activation. Macrophage activation stimulates lipid droplet formation and increases triacylglycerol and phospholipid content, after Kdo2-lipid A (KLA) activation
metabolism
GPAT3 is involved in intestinal lipid metabolism, role of the intestinal glycerol 3-phosphate pathway in dietary lipid absorption. During lipid absorption, enterocytes transiently store triglycerides in cytosolic lipid droplets before packaging and secretion in chylomicron particles, isozyme Gpat3 localizes in the proximity to lipid droplets
metabolism
relation between three isoforms GPAT1, 3, and 4 and insulin resistance, overview. GPAT2 may play an important role in the regulation of reproductive system
metabolism
relation between three isoforms GPAT1, 3, and 4 and insulin resistance, overview. GPAT3 and GPAT4 enzyme activity can be regulated by insulin upon phosphorylation at the Thr and Ser residues. Lysophosphatidic acid (LPA) produced by GPAT4 can stimulate mitogenic activity. LPA serves as a mitogen regulating various cellular processes, such as cell proliferation and cytoskeletal reorganization. Like mitochondrial GPAT1, GPAT4 is also associated with hepatic lipid accumulation and contributes to the development of insulin resistance
metabolism
relation between three isoforms GPAT1, 3, and 4 and insulin resistance, overview. GPAT3 is recognized as a major isoform in the adipocytes for the synthesis of triacylglycerol. GPAT3 and GPAT4 enzyme activity can be regulated by insulin upon phosphorylation at the Thr and Ser residues. GPAT3 serves as an enzyme, playing critical roles in dietary lipid absorption, enteric and hepatic lipid homeostasis, as well as entero-endocrine hormone production. GPAT3 has been shown to be involved in the regulation of intestinal lipid metabolism, thyroid-stimulating hormone (TSH) induces lipid production by activating the PPARgamma/AMPK/GPAT3 pathway in a thyroxine-independent manner
metabolism
substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids. The successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, overview
physiological function
a 60% knockdown of Gpat3 mRNA in 3T3-L1 cells with small interfering (si)RNA results in a 55% decrease in fatty acid incorporation into lysophosphatidic acid. Gpat1 mRNA levels also show a large induction during 3T3-L1 adipocyte differentiation, suggesting that this isoform also contributes to GPAT activity in adipocytes
physiological function
-
cis-acting promoter sequences for the mouse GPAT1 gene are identified: promoter 1a which includes part of the classical sequence and the downstream promoter 1b. Promoter 1a facilitates transcription of two alternative GPAT1 transcript variants, GPAT1-V1 and V2, while promoter 1b produces a third transcript variant, GPAT1-V3
physiological function
GC-1 spermatogonia cells show a marked increase in proliferation after transfection with GPAT4. Cell cycle analysis shows a decrease in the percentage of cells in the G0/G1 phase and an increase in the S phase. Thus, GPAT4 might play an important role in spermatogenesis, especially in mid-meiosis
physiological function
Gpat3 mRNA levels in ob/ob mice are decreased by 70% in white adipose tissue and increased 2fold in liver compared with wild-type animals. Treatment of ob/ob mice with rosiglitazone, a potent peroxisome proliferator-activated receptor (PPAR)gamma agonist, increases Gpat3, but not Gpat1, mRNA in white adipose tissue, suggesting that Gpat3 is a PPARgamma target gene
physiological function
-
the enzyme is essential for the response to the increased metabolic demands associated with T cell activation
physiological function
the metabolic rate of Gpat4-/- mice fed a 45% fat diet is 12% higher than controls, and core body temperature is 1ºC higher. A 45% fat diet increases the Gpat4-/- brown adipose tissue expression of peroxisome proliferator-activated receptor alpha target genes, Cpt1alpha, Pgc1alpha, and Ucp1, and brown adipose tissue mitochondria oxidize oleate and pyruvate at higher rates than controls. Gpat4-/- neonatal brown adipose tissue preadipocytes differentiated to adipocytes incorporate 33% less fatty acid into triacylglycerol and 46% more into the pathway of beta-oxidation
physiological function
a role for GPAT4 in suppressing inflammatory responses. GPAT4 is required for enhanced glycerolipid synthesis in activated macrophages
physiological function
glycerol-3-phosphate acyltransferases (GPAT) catalyze the first and rate-limiting step in the de novo glycerolipid synthesis. Glycerol-3-phosphate acyltransferase 2 is essential for normal spermatogenesis. GPAT is regulated by epigenetic mechanisms in combination with vitamin A derivatives, analysis of GPAT2 role in the developing male germ cells, overview. GPAT2 protein is necessary for the normal development of male gonocytes. GPAT2 is necessary to reach or to complete the pachytene stage in which GPAT2 interacts with MILI to synthesize piRNAs by the primary pathway
physiological function
GPAT3 is required for enhanced glycerolipid synthesis in activated macrophages
physiological function
GPATs play a pivotal role in the regulation of triglyceride and phospholipid synthesis. GPATs play a critical role in the development of obesity, hepatic steatosis, and insulin resistance. GPAT2 is a murine MILI (mouse Piwi-like)-binding protein and is also involved in the primary biosynthesis of piRNA, which interacts with PIWI. GPAT2 expression is unchanged in fasted or fasted-refed rodents, further implying that GPAT2 is unrelated to triacylglycerol synthesis or energy storage in the liver, and its transcription might not be under the regulation of SREBP1 or ChREBP. GPAT2 may play an important role in the regulation of reproductive system
physiological function
GPATs play a pivotal role in the regulation of triglyceride and phospholipid synthesis. GPATs play a critical role in the development of obesity, hepatic steatosis, and insulin resistance. GPAT4 plays a unique role in triacylglycerol synthesis and maintains systemic energy balance during lactation in inguinal adipose tissue. GPAT4 is a positive regulator of body weight. GPAT4 plays a critical role in triacylglycerol synthesis during development
physiological function
GPATs play a pivotal role in the regulation of triglyceride and phospholipid synthesis. GPATs play a critical role in the development of obesity, hepatic steatosis, and insulin resistance. Microsomal GPAT3 catalyzes a broad range of reactions using long-chain acyl-CoA as substrates, including saturated and unsaturated fatty acids. GPAT3 play a crucial role in lipid formation. GPAT3 serves as an enzyme, playing critical roles in dietary lipid absorption, enteric and hepatic lipid homeostasis, as well as entero-endocrine hormone production. GPAT3 plays a critical role in regulating glucose, energy, and lipid homeostasis
physiological function
isozyme GPAT3 is primarily involved in triglyceride (TG) storage in adipocytes. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation
physiological function
isozyme GPAT4 is a primary contributor to lysophosphatidic acid synthesis in liver and brown adipose tissue. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation. GPAT4 expression and high-fat diet-induced insulin resistance are linked to altered levels of palmitate-enriched phosphatidic acid and diacylglycerol and altered mTORC2
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g., G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g., G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g., G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g., G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g. G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g. G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g. G3P)
additional information
the GPAT/AGPAT family acyltransferases contain four well-conserved domains (motif I-IV), which catalyze the transferase reaction and are involved in binding to the substrate (acyl acceptor, e.g. G3P)
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E315A
28% of wild-type mitochondrial acyltransferase activity
E315Q
47% of wild-type mitochondrial acyltransferase activity
F313A
17% of wild-type mitochondrial acyltransferase activity
F313Y
88% of wild-type mitochondrial acyltransferase activity
R278H
10% of wild-type mitochondrial acyltransferase activity
R278K
76% of wild-type mitochondrial acyltransferase activity
R279A
101% of wild-type mitochondrial acyltransferase activity
R279H
95% of wild-type mitochondrial acyltransferase activity
R279K
101% of wild-type mitochondrial acyltransferase activity
R318H
2.6% of wild-type mitochondrial acyltransferase activity
R318K
11% of wild-type mitochondrial acyltransferase activity
additional information
overexpression and knockout of GPAT1
additional information
overexpression and knockout of GPAT1
additional information
overexpression and knockout of GPAT1
additional information
overexpression and knockout of GPAT1
additional information
-
construction of isozyme mtGPAT1-knockout mice
additional information
changes in GPAT4 activity in overexpressing Cos-7 cells and knockout mice
additional information
changes in GPAT4 activity in overexpressing Cos-7 cells and knockout mice
additional information
changes in GPAT4 activity in overexpressing Cos-7 cells and knockout mice
additional information
changes in GPAT4 activity in overexpressing Cos-7 cells and knockout mice
additional information
construction of GPAT2 knockout mice
additional information
construction of GPAT2 knockout mice
additional information
construction of GPAT2 knockout mice
additional information
construction of GPAT2 knockout mice
additional information
construction of GPAT4 knockout or null mice. Overexpression of GPAT4 in HEK-293 cells leads to increase the formation of lysophosphatidic acid, phosphatidic acid, and diacylglycerol, while triacylglycerol levels are unchanged. GPAT4-deficient mice have decreased body weight gain and subcutaneous fat pad, lowered hepatic and plasmatic triglycerides levels, and improved insulin resistance compared to controls. In addition, GPAT4-/- mice are protected from dietary-induced obesity (DIO) and the development of insulin resistance in the liver and muscle cells through decreased content of di16:0 PA
additional information
construction of GPAT4 knockout or null mice. Overexpression of GPAT4 in HEK-293 cells leads to increase the formation of lysophosphatidic acid, phosphatidic acid, and diacylglycerol, while triacylglycerol levels are unchanged. GPAT4-deficient mice have decreased body weight gain and subcutaneous fat pad, lowered hepatic and plasmatic triglycerides levels, and improved insulin resistance compared to controls. In addition, GPAT4-/- mice are protected from dietary-induced obesity (DIO) and the development of insulin resistance in the liver and muscle cells through decreased content of di16:0 PA
additional information
construction of GPAT4 knockout or null mice. Overexpression of GPAT4 in HEK-293 cells leads to increase the formation of lysophosphatidic acid, phosphatidic acid, and diacylglycerol, while triacylglycerol levels are unchanged. GPAT4-deficient mice have decreased body weight gain and subcutaneous fat pad, lowered hepatic and plasmatic triglycerides levels, and improved insulin resistance compared to controls. In addition, GPAT4-/- mice are protected from dietary-induced obesity (DIO) and the development of insulin resistance in the liver and muscle cells through decreased content of di16:0 PA
additional information
construction of GPAT4 knockout or null mice. Overexpression of GPAT4 in HEK-293 cells leads to increase the formation of lysophosphatidic acid, phosphatidic acid, and diacylglycerol, while triacylglycerol levels are unchanged. GPAT4-deficient mice have decreased body weight gain and subcutaneous fat pad, lowered hepatic and plasmatic triglycerides levels, and improved insulin resistance compared to controls. In addition, GPAT4-/- mice are protected from dietary-induced obesity (DIO) and the development of insulin resistance in the liver and muscle cells through decreased content of di16:0 PA
additional information
generation of Gpat4-/- mice in a C57BL6/J background
additional information
generation of Gpat4-/- mice in a C57BL6/J background
additional information
GPAT activity increases significantly after GPAT3 overexpression in COS-7 cells. The activity of GPAT decreases dramatically with GPAT3-specific siRNA knockdown in 3T3-L1 cells, which directly inhibits lipid synthesis
additional information
GPAT activity increases significantly after GPAT3 overexpression in COS-7 cells. The activity of GPAT decreases dramatically with GPAT3-specific siRNA knockdown in 3T3-L1 cells, which directly inhibits lipid synthesis
additional information
GPAT activity increases significantly after GPAT3 overexpression in COS-7 cells. The activity of GPAT decreases dramatically with GPAT3-specific siRNA knockdown in 3T3-L1 cells, which directly inhibits lipid synthesis
additional information
GPAT activity increases significantly after GPAT3 overexpression in COS-7 cells. The activity of GPAT decreases dramatically with GPAT3-specific siRNA knockdown in 3T3-L1 cells, which directly inhibits lipid synthesis
additional information
GPAT3 knockout (Gpat3-/-) mice are generated
additional information
-
GPAT3 knockout (Gpat3-/-) mice are generated
additional information
the gene is silenced in vivo by inoculating lentiviral particles carrying the sequence of a short-hairpin RNA targeting Gpat2 mRNA into mouse testis, expression of 5 different shRNA-Gpat2 vectors, subcloning in HEK-293 cells. Histological and gene expression analysis shows impaired spermatogenesis and arrest at the pachytene stage. Defects in reproductive fitness are also observed, and the analysis of apoptosis-related gene expression demonstrates the activation of apoptosis in Gpat2-silenced germ cells. The decrease in germ cell number in shRNA-Gpat2 mice seminiferous tubules correlates with apoptosis activation, without retrotransposon derepression
additional information
-
the gene is silenced in vivo by inoculating lentiviral particles carrying the sequence of a short-hairpin RNA targeting Gpat2 mRNA into mouse testis, expression of 5 different shRNA-Gpat2 vectors, subcloning in HEK-293 cells. Histological and gene expression analysis shows impaired spermatogenesis and arrest at the pachytene stage. Defects in reproductive fitness are also observed, and the analysis of apoptosis-related gene expression demonstrates the activation of apoptosis in Gpat2-silenced germ cells. The decrease in germ cell number in shRNA-Gpat2 mice seminiferous tubules correlates with apoptosis activation, without retrotransposon derepression
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158438
2020
Mus musculus (Q14DK4), Mus musculus (Q61586), Mus musculus (Q8C0N2), Mus musculus (Q8K2C8), Homo sapiens (Q53EU6), Homo sapiens (Q6NUI2), Homo sapiens (Q86UL3), Homo sapiens (Q9HCL2)
brenda
Khatun, I.; Clark, R.; Vera, N.; Kou, K.; Erion, D.; Coskran, T.; Bobrowski, W.; Okerberg, C.; Goodwin, B.
Characterization of a novel intestinal glycerol-3-phosphate acyltransferase pathway and its role in lipid homeostasis
J. Biol. Chem.
291
2602-2615
2016
Mus musculus (Q8C0N2), Mus musculus
brenda
Yu, J.; Loh, K.; Song, Z.Y.; Yang, H.Q.; Zhang, Y.; Lin, S.
Update on glycerol-3-phosphate acyltransferases the roles in the development of insulin resistance
Nutr. Diabetes
8
34
2018
Mus musculus (Q14DK4), Mus musculus (Q61586), Mus musculus (Q8C0N2), Mus musculus (Q8K2C8), Homo sapiens (Q53EU6), Homo sapiens (Q86UL3), Homo sapiens (Q9HCL2), Mus musculus C57BL/6J (Q8K2C8)
brenda