Succinyl-CoA:3-ketoacid coenzyme A transferase (SCOT): Development of an antibody to human SCOT and diagnostic use in hereditary SCOT deficiency

Abstract

Succinyl-CoA:3-ketoacid CoA transferase (SCOT) is a key enzyme for ketone body utilization. Hereditary SCOT deficiency in humans (McKusick catalogue number 245050) is characterized by intermittent ketoacidotic attacks and permanent hyperketonemia. Since previously-available antibody to rat SCOT did not crossreact with human SCOT, we developed an antibody against recombinant human SCOT expressed in a bacterial system. The recombinant SCOT was insoluble except under denaturing conditions. Antibody raised to this polypeptide recognized denatured SCOT and proved useful for immunoblot analysis. On immunoblots, SCOT was easily detectable in control fibroblasts and lymphocytes but was detected neither in fibroblast extracts from four SCOT-deficient patients, nor in lymphocytes from two SCOT-deficient patients. These data indicate that immunoblot analysis is useful for diagnosis of SCOT deficiency in combination with enzyme assay.

A Combined Metabolomic and Proteomic Study Revealed the Difference in Metabolite and Protein Expression Profiles in Ruminal Tissue From Goats Fed Hay or High-Grain Diets

“…Of these differentially expressed proteins, our data revealed that HG diet feeding decreased the expression of proteins involved in fatty acid metabolism, such as long-chain 3-hydroxyacyl-CoA dehydrogenase ( HADHA ), succinyl-coa:3-ketoacid-coenzyme a transferase ( OXCT1 ), and FABP3. Among these downregulated expression of proteins, HADHA protein can catalyze the third step of mitochondrial beta-oxidation (Haglind et al, 2015), FABP3 protein act as a transport of fatty acids to the mitochondria or peroxisome for beta-oxidation (Furuhashi and Hotamisligil, 2008), ATP binding cassette subfamily d member 3 ( ABCD3 ) functions as a transporter for moving the fatty acids into peroxisome for beta-oxidation (van Roermund et al, 2014), and OXCT1 was a key enzyme for ketone body utilization (Song et al, 1997). Thus, the downregulated expression of these proteins indicates a decreased catabolism of fatty acids in the HG group.…”

Oxaliplatin-induced cardiotoxicity in mice is connected to the changes in energy metabolism in the heart tissue

“…Downregulation of Oxct1 would restrict the heart's ability to utilize ketone bodies resulting in decreased energy production and ketone bodies accumulation. An increase in ketones may lead to clinically dangerous ketoacidosis in patients with loss of appetite and lethargy (56).…”