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Pathway Description
Carnitine-Acylcarnitine Translocase Deficiency
Homo sapiens
Disease Pathway
Carnitine-acylcarnitine translocase deficiency, also called CACT deficiency, is an extremely rare inherited inborn error of metabolism (IEM) of fatty acid oxidation. It is an autosomal recessive disorder caused by a defective carnitine-acylcarnitine translocase gene. Carnitine-acylcarnitine translocase is a transporter protein that is responsible for transporting carnitine-fatty acid complexes and carnitine across the inner mitochondrial membrane. Defects in the CACT enzyme prevent the shuttle-like action of carnitine from moving fatty acids across the mitochondrial membrane and therefore there is decreased fatty acid catabolism. As a result, CACT deficiency prevents the body from using certain fats for energy, particularly during periods without food (fasting). Individuals with CACT may have extremely low levels of ketones (hypoketosis) and low blood sugar (hypoglycemia). Together these signs are called hypoketotic hypoglycemia. Signs and symptoms of this disorder usually begin soon after birth and may include breathing problems, seizures, and an irregular heartbeat (arrhythmia). Individuals with CACT deficiency also usually have excess ammonia in the blood (hyperammonemia), an enlarged liver (hepatomegaly), and a weakened heart muscle (cardiomyopathy). Many CACT-deficient newborns do not survive. Others who are afflicted with a milder form of the disorder develop signs and symptoms in early childhood and are at risk for nervous system damage, liver failure, coma, and death.
References
Carnitine-Acylcarnitine Translocase Deficiency References
[Metagen: CARNITINE-ACYLCARNITINE TRANSLOCASE DEFICIENCY](http://metagene.de/program/d.prg?id_d=342)
[OMIM: 212138](http://omim.org/entry/212138})
[NIH](http://ghr.nlm.nih.gov/condition/carnitine-acylcarnitine-translocase-deficiency)
Pande SV, Murthy MS: Carnitine-acylcarnitine translocase deficiency: implications in human pathology. Biochim Biophys Acta. 1994 Jul 18;1226(3):269-76.
Pubmed: 8054358
Beta Oxidation of Very Long Chain Fatty Acids References
Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.
Lodish, H. et al. Molecular cell biology. (2004) New York: W.H Freeman.
Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.
Vance, D.E., and Vance, J.E. Biochemistry of lipids, lipoproteins, and membranes (4th ed.) (2002) Amsterdam; Boston: Elsevier.
Lawson LD, Kummerow FA: beta-Oxidation of the coenzyme A esters of elaidic, oleic, and stearic acids and their full-cycle intermediates by rat heart mitochondria. Biochim Biophys Acta. 1979 May 25;573(2):245-54. doi: 10.1016/0005-2760(79)90058-4.
Pubmed: 444549
Yu W, Liang X, Ensenauer RE, Vockley J, Sweetman L, Schulz H: Leaky beta-oxidation of a trans-fatty acid: incomplete beta-oxidation of elaidic acid is due to the accumulation of 5-trans-tetradecenoyl-CoA and its hydrolysis and conversion to 5-trans-tetradecenoylcarnitine in the matrix of rat mitochondria. J Biol Chem. 2004 Dec 10;279(50):52160-7. doi: 10.1074/jbc.M409640200. Epub 2004 Oct 4.
Pubmed: 15466478
Wanders RJ, Vreken P, den Boer ME, Wijburg FA, van Gennip AH, IJlst L: Disorders of mitochondrial fatty acyl-CoA beta-oxidation. J Inherit Metab Dis. 1999 Jun;22(4):442-87.
Pubmed: 10407780
Muoio DM, Seefeld K, Witters LA, Coleman RA: AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target. Biochem J. 1999 Mar 15;338 ( Pt 3):783-91.
Pubmed: 10051453
Hunt MC, Solaas K, Kase BF, Alexson SE: Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. J Biol Chem. 2002 Jan 11;277(2):1128-38. doi: 10.1074/jbc.M106458200. Epub 2001 Oct 22.
Pubmed: 11673457
Zammit VA: The malonyl-CoA-long-chain acyl-CoA axis in the maintenance of mammalian cell function. Biochem J. 1999 Nov 1;343 Pt 3:505-15.
Pubmed: 10527927
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