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Acyl-CoA dehydrogenase, long chain

long-chain acyl-CoA dehydrogenase, LCAD, ACADL
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, VLCAD, CAN, fibrillin-1, HAD
Papers on long-chain acyl-CoA dehydrogenase
Elevations of C14:1 and C14:2 Plasma Acylcarnitines in Fasted Children: A Diagnostic Dilemma.
New
Graham et al., Houston, United States. In J Pediatr, Dec 2015
OBJECTIVES: To test whether follow-up testing for very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency uncovers a diagnosis in patients with elevations of C14:1 and C14:2 plasma acylcarnitines after a controlled fasting study performed for clinically suspected hypoglycemia and to compare the acylcarnitine profiles from fasted patients without VLCAD deficiency vs patients with known VLCAD deficiency to determine whether metabolite testing distinguishes these groups.
Lethal Neonatal Progression of Fetal Cardiomegaly Associated to ACAD9 Deficiency.
New
Bekri et al., Rouen, France. In Jimd Rep, Nov 2015
ACAD9, a member of acyl-CoA dehydrogenase family, has high homology with VLCAD (very long-chain acyl-CoA dehydrogenase) and harbors a homodimer structure.
Application of an Image Cytometry Protocol for Cellular and Mitochondrial Phenotyping on Fibroblasts from Patients with Inherited Disorders.
New
Bross et al., Århus, Denmark. In Jimd Rep, Oct 2015
To assess the use of our protocol for analysis of HDFs from patients with inherited diseases, we analysed HDFs from two patients with very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency (VLCADD), one with a severe clinical phenotype and one with a mild one.
Mitochondrial dysfunction in fatty acid oxidation disorders: insights from human and animal studies.
Review
Amaral et al., Porto Alegre, Brazil. In Biosci Rep, 2014
We will briefly summarize the current knowledge obtained from patients and genetic mouse models with these disorders indicating that disruption of mitochondrial energy, redox and calcium homoeostasis is involved in the pathophysiology of the tissue damage in the more common FAOD, including medium-chain acyl-CoA dehydrogenase (MCAD), long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) and very long-chain acyl-CoA dehydrogenase (VLCAD) deficiencies.
Nitrate enhances skeletal muscle fatty acid oxidation via a nitric oxide-cGMP-PPAR-mediated mechanism.
Murray et al., Cambridge, United Kingdom. In Bmc Biol, 2014
In C2C12 myotubes, nitrate increased expression of the PPARα targets Cpt1b, Acadl, Hadh and Ucp3, and enhanced oxidative phosphorylation rates with palmitoyl-carnitine; however, these changes in gene expression and respiration were prevented by inhibition of either sGC or protein kinase G. Elevation of cGMP, via the inhibition of phosphodiesterase 5 by sildenafil, also increased expression of Cpt1b, Acadl and Ucp3, as well as CPT1B protein levels, and further enhanced the effect of nitrate supplementation.
Dynamics of Fat Mass in DUhTP Mice Selected for Running Performance - Fat Mobilization in a Walk.
Hoeflich et al., Germany. In Obes Facts, 2014
Following mild physical activity, subcutaneous fat derived from DUhTP mice showed increased levels of long chain acyl dehydrogenase (LCAD; +230%; p < 0.05) and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1-α; p < 0.01).
Renal response to short- and long-term exercise in very-long-chain acyl-CoA dehydrogenase-deficient (VLCAD(-/-)) mice.
Spiekerkoetter et al., Freiburg, Germany. In Mol Cell Pediatr, 2014
BACKGROUND: Deficiency of very long-chain acyl-CoA dehydrogenase (VLCAD) is the most common disorder of mitochondrial β-oxidation of long-chain fatty acids.
Role of CoA and acetyl-CoA in regulating cardiac fatty acid and glucose oxidation.
Review
Lopaschuk et al., Edmonton, Canada. In Biochem Soc Trans, 2014
We find that acetylation of the fatty acid β-oxidative enzymes, LCAD (long-chain acyl-CoA dehydrogenase) and β-HAD (β-hydroxyacyl-CoA dehydrogenase) is associated with an increase in activity and fatty acid oxidation in heart from obese mice with heart failure.
Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease.
Review
Verdin et al., San Francisco, United States. In J Biol Chem, 2013
SIRT3 regulates the acetylation level and enzymatic activity of key metabolic enzymes, such as acetyl-CoA synthetase, long-chain acyl-CoA dehydrogenase, and 3-hydroxy-3-methylglutaryl-CoA synthase 2, and enhances fat metabolism during fasting.
SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism.
Review
Verdin et al., San Francisco, United States. In Cold Spring Harb Symp Quant Biol, 2010
Activated SIRT3 deacetylates several key metabolic enzymes-acetyl-coenzyme A synthetase, long-chain acyl-coenzyme A (acyl-CoA) dehydrogenase (LCAD), and 3-hydroxy-3-methylglutaryl CoA synthase 2-and enhances their enzymatic activity.
State of the art in muscle lipid diseases.
Review
Nishino et al., Tokyo, Japan. In Acta Myol, 2010
This group includes beta-oxidation cycle defects and deficiencies of carnitine palmitoyltransferase II (CPTH) and very-long-chain acyl-CoA dehydrogenase (VLCAD).
Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I.
Impact
Vogel et al., Nijmegen, Netherlands. In Cell Metab, 2010
It closely resembles very long-chain acyl-CoA dehydrogenase (VLCAD), involved in mitochondrial beta oxidation of long-chain fatty acids.
Low expression of long-chain acyl-CoA dehydrogenase in human skeletal muscle.
GeneRIF
Tarnopolsky et al., Canada. In Mol Genet Metab, 2010
LCAD is minimally expressed in human skeletal muscle and likely does not play a significant role in long-chain fatty acid oxidation.
Resistance to high-fat diet-induced obesity and insulin resistance in mice with very long-chain acyl-CoA dehydrogenase deficiency.
Impact
GeneRIF
Shulman et al., New Haven, United States. In Cell Metab, 2010
mice with an inherited deficiency of very long-chain acyl-CoA dehydrogenase (VLCAD), were protected from high-fat diet-induced obesity and liver and muscle insulin resistance.
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation.
Impact
GeneRIF
Verdin et al., San Francisco, United States. In Nature, 2010
LCAD is deacetylated in wild-type mice under fasted conditions and by SIRT3 in vitro and in vivo; hyperacetylation of LCAD reduces its enzymatic activity
A genome-wide perspective of genetic variation in human metabolism.
Impact
Suhre et al., München, Germany. In Nat Genet, 2010
For eight out of nine replicated loci (FADS1, ELOVL2, ACADS, ACADM, ACADL, SPTLC3, ETFDH and SLC16A9), the genetic variant is located in or near genes encoding enzymes or solute carriers whose functions match the associating metabolic traits.
Cardiac hypertrophy in mice with long-chain acyl-CoA dehydrogenase or very long-chain acyl-CoA dehydrogenase deficiency.
GeneRIF
Wood et al., Birmingham, United States. In Lab Invest, 2009
substantial cardiac hypertrophy in LCAD-deficient mice
Genome-wide microarray expression analysis of CD4+ T Cells from nonobese diabetic congenic mice identifies Cd55 (Daf1) and Acadl as candidate genes for type 1 diabetes.
GeneRIF
Ridgway et al., Pittsburgh, United States. In J Immunol, 2008
Novel candidate genes in T1D CD55 and Acadl were identified.
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