Bdh1

Official Full Name

3-hydroxybutyrate dehydrogenase, type 1

Organism

Mus musculus

GeneID

71911

Background

Predicted to enable 3-hydroxybutyrate dehydrogenase activity and phospholipid binding activity. Predicted to be involved in steroid metabolic process. Located in mitochondrial inner membrane. Is expressed in several structures, including alimentary system; genitourinary system; integumental system; nervous system; and sensory organ. Orthologous to human BDH1 (3-hydroxybutyrate dehydrogenase 1). [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

Bdh1; Bdh; 2310032J20Rik;

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Detailed Information

D-β-hydroxybutyrate dehydrogenase 1 (BDH1) encodes a member of the short-chain dehydrogenase/reductase gene family. This coding protein forms the homotrimeric enzyme required for positioning in mitochondrial membrane, which has special requirements for the activity of phospholipase. The encoded protein catalyzes the mutual conversion of acetoacetate and (R)-3-hydroxybutyrate, the two major ketone bodies produced during fatty acid catabolism. Alternatively spliced transcript variants encoding the same protein have been described.

BDH1 is Significantly Up-regulated in Overload-Induced Heart Failure

Congestive heart failure is a crucial clinical problem associated with a high mortality rate. Deprivation of cardiac energy metabolism induces cardiac remodeling, ATP production and myocardial energy damage, leading to pathological hypertrophy and heart failure. Many studies have described myocardial metabolism with both glucose and fatty acid utilization in failing hearts. It is well known that cardiac ketone body metabolism is evolutionally conserved and widely used in various organs, which can act as an energy substitute in cases of glucose deprivation. Ketone bodies consist of 3 compounds: acetone, acetoacetate and β-hydroxybutyrate (βOHB), βOHB is reconverted to acetyl-CoA as an energy source. Thus ketone bodies act as a significant energy supplier to avoid energy crisis in the case of impaired glucose or oxygen delivery, for example in advanced heart failure.

After the transverse aortic constriction of the heart, BDH1 expresses an increased enzyme that catalyzes the NAD+/NADH coupled interconversion of acetoacetate and βOHB. In addition, the ketone body oxidation of the aortic transverse heart is elevated. Recent study has shown that BDH1 expression is enhanced in the case of overload-induced heart failure. These data indicate that under the circumstance of BDH1 overexpression, the generation of βOHB is increased, and the utilization of ketone bodies as an alternate fuel source is also increased.

BDH1 Fig 1. Metabolism of ketone bodies (Zhang J, et al. Journal of Lipid Research. 2018).

Under nutrient limiting conditions, cancer cells reactivate gene expression or metabolic pathways to achieve proliferation. A recent study has determined BDH1 and OXCT1 (3-oxoacid CoA transferase 1) expression levels in transplanted tumors, and found no increase in the expression of BDH1 and OXCT1 in tumors derived from PANC-1 cell xenografts, indicating that ketolysis was not activated in xenograft tumors. In contrast, qRT-PCR result has shown that the expression of of BDH1 and OXCT1 in HeLa cell xenografts are upregulated. Metabolic adaptations, such as reactivation of key ketone catabolism enzymes, may be one of the main reasons for failure of KD (ketogenic diet) therapy on lung cancer cell xenografts. This metabolic adaptation can be observed in nutrient-deficient hepatocellular carcinoma cells that utilize ketone bodies to provide energy and cancer progression. Therefore, studying the potential mechanism of reactivation of gene expression can further enhance the anti-tumor effect of KD therapy.

References:

Motoki Uchihashi, et al. Cardiac-specific Bdh1 overexpression ameliorates oxidative stress and cardiac remodeling in pressure overload–induced heart failure. Circulation: Heart Failure. 2017.
Zhang J, Jia P-P, Liu Q-L, et al. Low ketolytic enzyme levels in tumors predict ketogenic diet responses in cancer cell lines in vitro and in vivo. Journal of Lipid Research. 2018.
Sikder K, Shukla S, K, Patel N, Singh H, Rafiq K, High Fat Diet Upregulates Fatty Acid Oxidation and Ketogenesis via Intervention of PPAR-γ. Cell Physiol Biochem. 2018.
Yo-Han Kim, Noriyuki Toji, Keiichiro Kizaki, Shiro Kushibiki, Toshihiro Ichijo, and Shigeru Sat. Effects of dietary forage and calf starter on ruminal pH and transcriptomic adaptation of the rumen epithelium in Holstein calves during the weaning transition. Physiol Genomics. 2016.
Zhang, Jie; Jia, Ping-Ping; Liu, Qing-Le; et al. Low ketolytic enzyme levels in tumors predict ketogenic diet responses in cancer cell lines in vitro and in vivo. JOURNAL OF LIPID RESEARCH. 2018.

Quick Inquiry

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!

Inquiry