High impact information on Crat

• The structures reveal significant differences in the acyl group binding pocket between carnitine octanoyltransferase and carnitine acetyltransferase [1].
• Cloning and characterization of murine carnitine acetyltransferase: evidence for a requirement during cell cycle progression [2].
• The cell cycle induction pattern of the CARAT gene was analysed in mouse fibroblasts at different stages of the unperturbed cell cycle [2].
• Among those measured, CARAT expression was highest, relative to liver, in heart muscle (56-fold) and testis (21-fold) [2].
• The specific activities of carnitine palmitoyltransferase I and carnitine acetyltransferase are significantly increased in the crude mitochondrial fraction isolated from the brains of the type II diabetic mice, whereas the specific activity of pyruvate dehydrogenase complex is decreased [3].

Biological context of Crat

• Crat mapped to Chromosome (Chr) 2, at a position approximately 18 cM from the centromere and 2 cM proximal to the gene Ass1 [4].

Anatomical context of Crat

• In agreement with the literature on rat liver 2,4-dichlorophenoxyacetic acid and 2,4,5-trichlorophenoxyacetic acid were found to cause extensive proliferation of peroxisomes (as judged by the total levels of "mitochondrial" protein, carnitine acetyltransferase, cyanide-insensitive palmitoyl-CoA oxidation and catalase) in mouse liver [5].
• TPA is a potent tumour promoter and treatment with this compound of the two cell lines induced peroxisomal fatty acid beta-oxidation, carnitine acetyltransferase, palmitoyl-CoA hydrolase, and catalase activities after 240 h of treatment [6].
• Dietary clofibrate for 21 days induced a rise in the specific activities of crotonase, acyl-CoA oxidase and carnitine acetyltransferase in a crude particulate fraction from mouse small intestinal mucosa [7].
• Particulate acyl-CoA oxidase activity was localized in microperoxisomes, while beta-hydroxyacyl-CoA dehydrogenase, carnitine acetyltransferase, carnitine octanoyltransferase and probably enoyl-CoA hydratase were partially localized in these organelles with most of the activity residing in the mitochondria [8].

Associations of Crat with chemical compounds

• Stimulation of the corresponding enzyme activities was dose-related and cycloheximide inhibited the TPA-induced enzyme activities, except that of carnitine acetyltransferase [6].
• Carnitine acetyltransferase (CAT; EC 2.3.1.7), the key enzyme for the translocation of acetyl units between intracellular compartments, was present in low activities in glucose-grown cells; its activity was increased some 100-fold in triolein-grown cells but only 4-fold in serum-grown cells [9].
• The effect of structurally divergent herbicides on mouse liver xenobiotic-metabolizing enzymes (P-450-dependent mono-oxygenases, epoxide hydrolases and glutathione S-transferases) and carnitine acetyltransferase [10].
• MCPP and 2,4-DP also increased cytosolic epoxide hydrolase and carnitine acetyltransferase activities suggestive of peroxisome proliferation [10].

Other interactions of Crat

• Peroxisomal enzyme activity measurements revealed no change in catalase, but dose-dependent increases in carnitine acetyltransferase and cyanide-insensitive beta-oxidation in both sexes [11].
• Choline acetyltransferase and carnitine acetyltransferase in the placenta of the mouse [12].

Analytical, diagnostic and therapeutic context of Crat

• Sequence analysis of the full-length cDNA clone and homology comparisons have revealed 87% homology to the human CARAT gene [2].

References