Disease relevance of Bdh1

• These results suggest that the decrease in BDH content in hepatoma cells results from a decrease in functional BDH-mRNA [1].
• The expressed activity in E. coli could be inhibited in a dose-dependent manner by BDH antiserum [2].
• Hypothyroidism, on the other hand, affects BDH activity in neither heart nor liver [3].
• A rat liver bacteriophage lambda expression library was probed using polyclonal antibodies raised to purified rat liver D-beta-hydroxybutyrate dehydrogenase (BDH) [2].

High impact information on Bdh1

• BDH activity in normal rat hepatocyte mitochondria was 321 nmol/min/mg, which was greatly reduced to 10.7 nmol/min/mg and 1.7 nmol/min/mg in H4-II-EC3 and RLT-3C cell mitochondria, respectively [1].
• Quantitation of D-beta-hydroxybutyrate dehydrogenase (BDH) in normal rat hepatocytes was compared with that in two rat hepatoma cell lines, H4-II-EC3 and RLT-3C [1].
• These results suggest that there is a reciprocal correlation between BDH activity and cell growth and protein synthesis rates [1].
• A computer-based comparison of the amino acid sequence of BDH with other reported sequences reveals a homology with the superfamily of short-chain alcohol dehydrogenases, which are distinct from the classical zinc-dependent alcohol dehydrogenases [4].
• The largest clone contained 1435 base pairs and encoded the entire amino acid sequence of mature BDH and the leader peptide of precursor BDH [4].

Chemical compound and disease context of Bdh1

• The coupling of a decrease in BDH activity with an increase in activity of succinyl-CoA: acetoacetyl-CoA transferase in hepatoma cells may play a role in generating additional energy required for the rapid growth of tumor cells [1].

Biological context of Bdh1

• 5. The concentrations of hydroxyacyl-CoA dehydrogenase and carnitine palmitoyltransferase were equivalent to the more active enzymes of the tricarboxylic acid cycle, indicating the capacity for extensive lipid oxidation, and the presence of 3-hydroxybutyrate dehydrogenase suggests that these tissues can also oxidize ketone bodies [5].
• The process of reactivation of BDH by phospholipids, which follows a second-order mechanism, reveals that (1) at least 2 mol of lecithins is essential for the reactivation of the enzyme, and (2) the enzyme contains two dependent binding sites for lecithins [6].
• This result indicates that in vivo the control of the expression of the BDH gene by insulin is mainly transcriptional and/or post-transcriptional (mRNA stability) [7].
• Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD) [8].
• With regard to the inhibitory effect on BDH and GDH following cadmium intoxication, it does not appear to be imputable to lipid peroxidation since in vitro investigations indicate that the presence of vitamin E does not remove the inhibition at all [9].

Anatomical context of Bdh1

• Precursor BDH synthesized by in vitro translation primed with RNA of H4-II-EC3 cells or RLT-3C cells was 3.0 and 1.1% of that translated from normal rat hepatocyte RNA [1].
• D-beta-Hydroxybutyrate dehydrogenase (BDH), purified as soluble, lipid-free apoenzyme (inactive) from either beef heart or rat liver mitochondria, can be reactivated by short-chain lecithins in the monomeric state [10].
• The Arrhenius-plot characteristics for 3-hydroxybutyrate dehydrogenase in membranes of diabetic and normal mitochondria were similar [11].
• The 3-hydroxybutyrate dehydrogenase activity also develops earlier in the medulla oblongata than in the other regions [12].
• The activity of 3-oxoacid CoA-transferase is higher in the macrophage, but that of 3-hydroxybutyrate dehydrogenase is very much lower than those in the lymphocytes [13].

Associations of Bdh1 with chemical compounds

• 5. The results suggest that inhibition of 3-hydroxybutyrate dehydrogenase and 3-oxo acid CoA-transferase activities may impair ketone-body utilization and hence lipid synthesis in the developing brain [14].
• The distribution of beta-hydroxybutyrate dehydrogenase (3-hydroxybutyrate dehydrogenase, EC 1.1.1.30) in the developing rat cerebellum has been determined using a histochemical method [15].
• The enzymic determination of D-3-hydroxybutyrate and acetoacetate normally involves the use of 3-hydroxybutyrate dehydrogenase (HBDH, EC 1.1.1.30) of bacterial origin [16].
• Cytochrome c oxidase, citrate synthase, 3-hydroxybutyrate dehydrogenase, 3-oxoacid coenzyme A transferase, and acetoacetyl-coenzyme A thiolase activities during the suckling period were in most stages lower than controls; subsequently, activities in undernourished rats reached or surpassed the control values [17].
• Diabetic mitochondria also showed decreased 3-hydroxybutyrate dehydrogenase and succinyl-CoA: 3-oxoacid CoA-transferase activities, but cytochrome content and NADH-dehydrogenase, succinate dehydrogenase, cytochrome oxidase and acetoacetyl-CoA thiolase activities proved normal [11].

Other interactions of Bdh1

• 1. The effects of phenylalanine and its metabolites (phenylacetate, phenethylamine, phenyl-lactate, o-hydroxyphenylacetate and phenylpyruvate) on the activity of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) 3-oxo acid CoA-transferase (EC 2.8.3.5) and acetoacetyl-CoA thiolase (EC 2.3.1.9) in brain of suckling rats were investigated [14].
• The enzymes whose developmental patterns were studied were: pyruvate dehydrogenase (EC 1.2.4.1), 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30), citrate synthase (EC 4.1.3.7), NAD-linked isocitrate dehydrogenase (EC 1.1.1.41) and fumarase (EC 4.2.1.2) [12].
• 4. When isolated mitochondria are incubated under conditions such that the glutamate dehydrogenase and 3-hydroxybutyrate dehydrogenase reactions reach equilibrium, the thermodynamically active concentration of ammonia is not equal to the concentration measured in the protein-free extracts [18].
• The zonal distribution of cytosolic acetyl-CoA carboxylase, mitochondrial 3-hydroxyacyl-CoA dehydrogenase and 3-hydroxybutyrate dehydrogenase was studied in microdissected liver tissue [19].
• Other inner membrane proteins (core protein 1, beta subunit of F1 ATPase, subunit IV of cytochrome oxidase, 3-hydroxybutyrate dehydrogenase) and non-mitochondrial proteins (rat serum albumin, beta 2-microglobulin) were not altered significantly by hormone treatment [20].

Analytical, diagnostic and therapeutic context of Bdh1

• In vitro translations of isolated RNA followed by immunoprecipitation revealed that the increase in BDH activity and content was correlated with an increase in the level of functional BDH-mRNA in both liver and brain [21].
• Antiserum against rat liver BDH inhibited both enzymes to an equivalent extent in a titration assay [22].
• Adrenalectomy and ovariectomy increase liver mRNA content and polypeptide level, as well as activity of BDH [23].
• The expression of mitochondrial membrane-bound D-beta-hydroxybutyrate dehydrogenase (BDH), a ketone body-converting enzyme, has been estimated by two immunological techniques: immunohistofluorescence and Western blotting [24].

References