Disease relevance of OXCT1

• A single approximately 3.2-kb SCOT mRNA is present in human tissues (heart > leukocytes >> fibroblasts), but no signal is detectable in the human hepatoma cell line HepG2 [1].
• In SCOT-deficient patients retaining some residual activity, permanent ketosis may be absent [2].
• We constructed a tertiary structural model of human SCOT by homology modeling based on the known structure of Acidaminococcus fermentans glutaconate CoA transferase [3].
• The leading edge of the rod a-wave recorded from normal observers and patients with congenital stationary night blindness (CSNB) was described by a linear process for flash intensities up to the maximum available flash intensity, 2.0 log scot td-sec [4].
• In this study, the effect of MAA on the growth of human gastric cancer cells was examined in relation to SCOT expression [5].

High impact information on OXCT1

• Sequence alignment of the human SCOT peptides with other known CoA transferases revealed several conserved regions of potential functional importance [1].
• Succinyl CoA: 3-oxoacid CoA transferase (SCOT; E.C.2.8.3.5) mediates the rate-determining step of ketolysis in extrahepatic tissues, the esterification of acetoacetate to CoA for use in energy production [1].
• We mapped the human SCOT locus (OXCT) to the cytogenetic band 5p13 by in situ hybridization [1].
• These data and other recently described mutations in the AVPR2 in North American pedigrees, descended from Ulster Scot ancestors and other origins, make the assertion of a founder effect proposed in the Hopewell hypothesis invalid [6].
• Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5; locus symbol OXCT) is the key enzyme of ketone body utilization [7].

Chemical compound and disease context of OXCT1

• Patients homozygous for the T435N mutation of succinyl-CoA:3-ketoacid CoA Transferase (SCOT) do not show permanent ketosis [2].
• Succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency is an inborn error of ketone body utilization, characterized by intermittent ketoacidotic crises and persistent ketosis [8].
• A defect in the human gene encoding succinyl-CoA: 3-oxoacid CoA-transferase causes a metabolic disease which leads to severe ketoacidosis, thus reflecting the importance of this family of enzymes [9].
• CONCLUSION: Parenteral nutrition with MAA may provide preferential energy for patients with some types of gastric cancer with SCOT deficiency [5].
• Growth-inhibitory effects of the ketone body, monoacetoacetin, on human gastric cancer cells with succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency [5].

Biological context of OXCT1

• This paper describes and characterizes three missense mutations in two SCOT-deficient siblings from Japan. They are genetic compounds who inherited the mutation C456F (c1367 G-->T) from their mother [7].
• Here we describe the human SCOT gene, which spans more than 100 kb and contains 17 exons, on chromosome 5p13 [3].
• As the level of illumination was raised within this range, the contrast sensitivity of the rod system increased, reaching a peak of about 50 (and providing an acuity of 6 c/deg) at 20 scot. td, whereupon the rod system began to saturate [10].
• Dark adaptation experiments and spectral sensitivity determinations indicated that, in the adaptational range from about 1.6 to 2.8 log scot td, 530 nm and 440 nm flashes were detected by rod and S cone photoreceptors, respectively [11].
• The kinds and amounts of the lipids of each stage (egg, coracidium, procercoid, plerocercoid, adult) in the life-cycle of the cestode Spirometra mansonoides, and of environmental lipids, have been examined by combinations of TEAE-cellulose and silicic acid column, silica gel thin-layer and SCOT column gas-liquid chromatography [12].

Anatomical context of OXCT1

• SCOT was detected in all tissues except liver: myocardium > brain, kidney and adrenal glands [13].
• Mitochondria from human placental tissue show activity of 3-oxoacid-CoA transferase and acetoacetyl-CoA thiolase [14].
• Succinyl-CoA: 3-ketoacid CoA transferase (SCOT), whose defect is the third inherited disorder of ketone body catabolism, was collected in the organelle fraction [15].
• In the SAGm18B line, GFP is expressed in the central nervous system, and the insertion captured a transcript of a gene for succinyl CoA:3-oxoacid CoA-transferase (SCOT) [16].
• In the fetus of the family, SCOT activity was not detected in either chorionic villi or cultured amniocytes [17].

Associations of OXCT1 with chemical compounds

• Physiologically the two mitochondrial enzymes have different roles: SCOT mediates energy production from ketone bodies (ketolysis), whereas T2 functions both in ketogenesis and ketolysis [13].
• We hypothesize that the high residual SCOT activity in homogenates may be an artifact caused by use of the substrate, acetoacetyl-CoA by other enzymes [7].
• A 6-bp deletion at the splice donor site of the first intron resulted in aberrant splicing using a cryptic splice site within exon 1 in a patient with succinyl-CoA: 3-Ketoacid CoA transferase (SCOT) deficiency [18].
• After extraction this compound is methylated with diazomethane and determined by gas-liquid chromatography using a capillary SCOT column with a mixed stationary phase, a solid injection system and a nitrogen-selective detector [19].
• Although he was a pupil of the great John Hunter, the young Astley Cooper possessed good manners and a gift of oratory of which the Scot, his teacher, was devoid [20].

Analytical, diagnostic and therapeutic context of OXCT1

• To our knowledge, this report is the first of prenatal diagnosis of SCOT deficiency [17].
• SCOT mRNA expression was examined by RT-PCR [5].

References