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anti-Human ACADVL Anticorps:
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Human Monoclonal ACADVL Primary Antibody pour IHC (p), ELISA - ABIN559746
De Pauw, Demine, Tejerina, Dieu, Delaive, Kel, Renard, Raes, Arnould: Mild mitochondrial uncoupling does not affect mitochondrial biogenesis but downregulates pyruvate carboxylase in adipocytes: role for triglyceride content reduction. dans American journal of physiology. Endocrinology and metabolism 2012
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Cow (Bovine) Polyclonal ACADVL Primary Antibody pour IHC, WB - ABIN2785735
Soon, Libe, Benn, Gill, Shaw, Sywak, Groussin, Bertagna, Gicquel, Bertherat, McDonald, Sidhu, Robinson: Loss of heterozygosity of 17p13, with possible involvement of ACADVL and ALOX15B, in the pathogenesis of adrenocortical tumors. dans Annals of surgery 2007
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Human Polyclonal ACADVL Primary Antibody pour ELISA, WB - ABIN4277522
Gobin-Limballe, Djouadi, Aubey, Olpin, Andresen, Yamaguchi, Mandel, Fukao, Ruiter, Wanders, McAndrew, Kim, Bastin: Genetic basis for correction of very-long-chain acyl-coenzyme A dehydrogenase deficiency by bezafibrate in patient fibroblasts: toward a genotype-based therapy. dans American journal of human genetics 2007
Sequencing of the ACADVL gene revealed that all individuals with activities below 24% were true Very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) patients, individuals with residual activities between 24 and 27% carried either one or two mutations. Twenty new mutations could be identified and functionally classified based on their effect on enzyme function.
The authors provide novel insights into the cellular energy household of cells from HADHA/ACADVL patients and demonstrate for the first time a connection between fatty acid metabolism, mitochondrial morphology and reactive oxygen species in patients with these rare genetic disorders.
VLCADD is relatively rare in southern China, for which late-onset form is common
There are currently no biochemical markers for prediction of disease severity and for the need for treatment in VLCAD deficiency. Mutation analysis may offer predictive value but this may not be robust enough for a large proportion of those mutations that have not been previously reported in clinically affected patients.
We retrospectively analyzed early outcomes for individuals who were diagnosed with VLCAD deficiency by NBS and describe initial presentations, diagnosis, clinical outcomes and treatment in a cohort of 52 individuals ages 1-18year.
LCHAD and MCAD are differentially expressed in maternal and fetal tissues during normal late pregnancy, which may represent a metabolic adaptation in response to physiological maternal dyslipidemia during late pregnancy.
following variants should be considered likely pathogenic c.1273G > A (p.A425T), c.1001T > G (p.M334R), c.538G > A (p.A180T), c.640T > G (p.F214V), c.1076C > T (p.A359V), c.1019G > T (p.G340V), c.889_891delGAG (p.E297del), and c.1103A > C (p.Q368P); patients homozygous for the most common pathogenic variant, c.848T > C (p.V283A) can be expected to have a more benign clinical course
11 mutations in ACADVL gene in 7 patients, 7 reported (p.S22X, p.W427X, p.A213T, p.G222R, p.R450H, c.296-297delCA, c.1605+1G>T), 4 novel (p.S72F, p.Q100X, p.M437T, p.D466Y). p.R450H and p.D466Y (14.28%, 2/14 alleles) mutations identified in 2 alleles.
Case Report: missense mutation within the ACADVL gene responsible for very-long-chain acyl-CoA dehydrogenase deficiency and sudden infant death.
These results emphasize the importance of functional investigation of abnormal NBS or clinical testing suggestive but not diagnostic of very-long-chain acyl-CoA dehydrogenase .
These findings support the importance of considering that mutations may be present in the ACADVL gene when a significant partial deficiency is found in CPTII activity, but no mutations in the CPT2 gene can be identified.
Identification of 2 VLCAD mutations leads to precautions in the management of the children with VLCAD deficiency.
The expressions of LCHAD gene and protein are remarkably reduced in early onset severe preeclampsia and HELLP syndrome.
Analyzed potential rhabdomyolysis-susceptibility genes (RYR 1, CPT II, VLCAD and CYP 2D6) from autopsy samples of methamphetamine abusers; no obvious relationship between the genetic mutations observed in this study and rhabdomyolysis was seen.
Down regulation of ACADVL is associated with cervical squamous cell carcinoma.
Missense mutations in Very-Long-Chain Acyl-CoA Dehydrogenase is associated with inborn errors of lipid metabolism.
This study confirms that VLCAD deficiency, although being less frequent than CPT II deficiency, should be systematically considered in the differential diagnosis of exercise-induced rhabdomyolysis.
Results suggest a novel regulatory mechanism for homeostatic VLCAD activity, whose dysregulation might be involved in the production of oxidative stress and in the pathogenesis of idiopathic pulmonary fibrosis.
A new a unique mutation (IVS13+25G>A) is reported in a compound heterozygote carrying the 1748 C>T mutation in exon 18.
the bacterial expression system developed here will significantly advance our understanding of both the clinical aspects of VLCAD deficiency and the basic biochemistry of the enzyme
our results demonstrate that infection as a stress produces perturbations in metabolism in Acadvl(-/-) that differ greatly from WT infected and Acadvl(-/-) pair-fed controls. This model system will be useful for studying the effects of infection on tissue metabolism as well as evaluating interventions aimed at modulating the effects of metabolic decompensation.
the MCL-1 BH3 interaction with VLCAD revealed a separable, gain-of-function role for MCL-1 in the regulation of lipid metabolism.
Triheptanoin was not able to prevent the development of systolic dysfunction in VLCAD(-/-) mice despite an upregulation of cardiac glucose oxidation. Strikingly, the anaplerotic effects of triheptanoin were restricted to the liver.
observed strong upregulation of peroxisomal beta-oxidation in VLCAD(-/-) mice
SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase
Studies conducted with permeabilized mitochondria and different chain length acyl-CoA derivatives suggest that VLCAD is also a source of reactive oxygen species production in mitochondria of high fat diet animals.
We demonstrate here that both dietary interventions with respect to the fat content of the diet reverse endogenous compensatory mechanisms in muscle that have evolved in VLCAD(-/-) mice resulting in pronounced energy deficiency
VLCAD(-/-) mice develop tissue-specific strategies to compensate deficiency of VLCAD either by induction of other mitochondrial acyl-CoA dehydrogenases or by enhancement of glucose oxidation.
Report a longer QTc interval and lipid alterations in VLCAD null mice.
Four VLCAD-/- deficient mice died unexpectedly on the treadmill during the early stages of training. The VLCAD-/- deficient mice that survived adapted to the aerobic interval training similarly to the non-deficient mice.
Medium-chain triglycerides impair lipid metabolism and induce hepatic steatosis in very long-chain acyl-CoA dehydrogenase (VLCAD)-deficient mice
Data show that in VLCAD knockout mice fed a long-chain triglyceride diet, fasting results in accumulation of liver lipids, hepatopathy and upregulation of peroxisomal and microsomal oxidation pathways as well as antioxidant enzyme activities and TBARS.
medium-chain triglyceride application prevents acylcarnitine accumulation in skeletal muscle from very-long-chain acyl-CoA-dehydrogenase-deficient mice
Authors conclude that mice with VLCAD deficiency have altered expression of a variety of genes in the fatty acid metabolic pathway from birth, reflecting metabolic feedback circuits.
carnitine and acylcarnitine profiles in liver, skeletal muscle, bile, and blood from VLCAD knock-out animals
evidence of impaired gluconeogenesis as one of the causes for hypoglycaemia observed in VLCAD deficiency
Carnitine supplementation induces acylcarnitine production in tissues of very long-chain acyl-CoA dehydrogenase-deficient mice, without replenishing low free carnitine.
Metabolic cardiomyopathy, expressed as hypertrophy, developed in mice because of either VLCAD deficiency or LCAD deficiency.
Bovine ACADVL gene had a significant effect on chest width (P<0.05), chest depth (P<0.05), and hip width (P<0.05) in the Qinchuan breed.
The protein encoded by this gene is targeted to the inner mitochondrial membrane where it catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product reduces myocardial fatty acid beta-oxidation and is associated with cardiomyopathy. Alternative splicing results in multiple transcript variants encoding different isoforms.
acyl-Coenzyme A dehydrogenase, very long chain
, very long-chain specific acyl-CoA dehydrogenase, mitochondrial
, VLCAD very-long-chain acyl-CoA dehydrogenase
, Very long chain Acyl-Coa dehydrogenase
, acyl-coenzyme A dehydrogenase, very long chain
, Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
, Very-long-chain acyl-CoA dehydrogenase