HAD

(redirected from 3-Hydroxyacyl-CoA Dehydrogenase)
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AcronymDefinition
HADHIV (Human Immunodeficiency Virus) Associated Dementia
HADHospitalisation à Domicile (French: Home Hospitalization)
HADHome Affairs Department (Hong Kong)
HADHole Accumulation Diode (Sony)
HADHole Accumulated Diode (Sony)
HADHuman Adenovirus (pathogen)
HADHumanitarian Aid & Development (various locations)
HADHearing Aid Dispenser
HADHole Accumulation Diode
HAD3-Hydroxyacyl-CoA Dehydrogenase (deficiency)
HADHarrow Association of Disabled (UK)
HADHealth Assessment Document
HADHemadsorption (laboratory virus testing)
HADHuman Adjuvant Disease
HADAtlantic Haddock
HADHospital Anxiety Depression
HADHomeland Air Defense
HADHardware Data Acquisition
HADHubble Data Archive
HADHeadbangers Against Disco
HADHalmstad, Sweden - Halmstad (Airport Code)
HADHeinemann Australian Dictionary
HADHigh Availability Device
HADHeat Activated Device
HADHigh Aluminum Defect
HADHarness Assembly Drawing (electrical wire assembly drawing for manufacturing of cable harness assemblies)
HADHeat Acquisition Devices
HADHorizontal Acoustic Depiction
HADHeated Air Ducting
References in periodicals archive ?
Dietary Management of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD).
19) In addition to its effect on palmitoyl-CoA and acyl coenzyme A oxidase, sesamin was also noted to amplify the action of numerous other hepatic fatty acid oxidation enzymes, including carnitine palmitoyltransferase, acyl-CoA dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase, enoyi-CoA hydratase and 3-ketoaeyl-CoA thiolase, as well as to improve, in a dose-dependent manner, the activity of 2,4-dienoyl-CoA reductase and [DELTA]3, [DELTA]2-enoyl-CoA isomerase, both of which are involved in the auxiliary pathway for beta-oxidation of unsaturated fatty acids.
The second step is carried out by an enoyl-CoA hydratase, and the enzyme involved in the third step is an L 3-hydroxyacyl-CoA dehydrogenase using NAD as cofactor for the reaction, which is reduced to NADH transferring electrons to complex 1 of the respiratory chain.
Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-Enoyl-CoA hydratase, 3-Hydroxyacyl-CoA dehydrogenase, and [[DELTA].
Likewise, enzyme activities of 3-hydroxyacyl-CoA dehydrogenase and carnityl palmitoyl-CoA transferase are good indicators of lipid metabolism.
2; encoded by KCNJ11) (7); glucokinase (GK; encoded by GCK) (8); glutamate dehydrogenase (GDH; encoded by GLUD-1) (9); short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD; encoded by HADH) (10); and ectopic expression on [beta]-cell plasma membrane of SLC16A1 [encodes monocarboxylate transporter 1 (MCT1)] (11).
The disease has been associated with a deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD).
In our previous research using comparative proteomic techniques, we observed that the expression of acetyl-Coenzyme A acetyltransferase 2 and 3-hydroxyacyl-CoA dehydrogenase type-2, those enzymes involved in fatty acid degradation, were decreased in the liver tissues of ketotic cows, which suggested that the ability to utilize fatty acids to produce C[O.
The 3 enzymes involved are long-chain enoyl-CoA hydratase (LCEH), long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), and long-chain 3-ketoacyl-CoA thiolase (LCTH).
Five enzymes/proteins were identified as being differentially expressed in the livers of ketotic cows: expression of 3-hydroxyacyl-CoA dehydrogenase type-2 (HCDH), acetylcoenzyme A acetyltransferase 2 (ACAT) and elongation factor Tu (EF-Tu) were down-regulated, whereas that of alpha-enolase and creatine kinase were up-regulated.
Use of proper standards enabled us to identify this signal as 3-HG, an important metabolite accumulating in glutaric aciduria type I and short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (11).
It is important to note than increased C14 and C14:1 may be produced in other disorders as well, such as carnitine palmitoyltransferase II (CPT II), carnitine/acylcarnitine translocase (CACT), MADD, and long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency.