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Pathway Description
Canavan Disease
Rattus norvegicus
Category:
Metabolite Pathway
Sub-Category:
Disease
Created: 2018-09-10
Last Updated: 2019-08-30
Canavan Disease (Canavan-Van Bogaert-Bertrand Disease; Aminoacylase 2 Deficiency; Spongy Degeneration of the Central Nervous System; Aspartoacylase Deficiency; ASP Deficiency; ACY2 Deficiency; ASPA) is a rare autosomal recessive disease caused by a defect in the ASPA gene which codes for aspartoacylase. A deficiency in this enzyme results in accumulation of N-Acetyl-L-aspartic acid in plasma, spinal fluid, and urine. Symptoms, which present at birth, include myclonus, irritability, hypotonia, motor retardation, and poor head control. The neurological complications are due to demyelination of neurons and leukodystrophy. Premature death often results, though lithium citrate can be used as a treatment.
References
Canavan Disease References
Bokhari MR, Bokhari SRA: Canavan Disease
Pubmed: 28613566
Matalon R, Rady PL, Platt KA, Skinner HB, Quast MJ, Campbell GA, Matalon K, Ceci JD, Tyring SK, Nehls M, Surendran S, Wei J, Ezell EL, Szucs S: Knock-out mouse for Canavan disease: a model for gene transfer to the central nervous system. J Gene Med. 2000 May-Jun;2(3):165-75. doi: 10.1002/(SICI)1521-2254(200005/06)2:3<165::AID-JGM107>3.0.CO;2-R.
Pubmed: 10894262
Aspartate Metabolism References
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Pubmed: 15057822
Florea L, Di Francesco V, Miller J, Turner R, Yao A, Harris M, Walenz B, Mobarry C, Merkulov GV, Charlab R, Dew I, Deng Z, Istrail S, Li P, Sutton G: Gene and alternative splicing annotation with AIR. Genome Res. 2005 Jan;15(1):54-66. doi: 10.1101/gr.2889405.
Pubmed: 15632090
Konno R: Rat D-amino-acid oxidase cDNA: rat D-amino-acid oxidase as an intermediate form between mouse and other mammalian D-amino-acid oxidases. Biochim Biophys Acta. 1998 Jan 21;1395(2):165-70. doi: 10.1016/s0167-4781(97)00185-1.
Pubmed: 9473656
Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ: A novel asparaginase-like protein is a sperm autoantigen in rats. Mol Reprod Dev. 2002 Jun;62(2):233-47. doi: 10.1002/mrd.10092.
Pubmed: 11984834
Dieterich DC, Landwehr M, Reissner C, Smalla KH, Richter K, Wolf G, Bockers TM, Gundelfinger ED, Kreutz MR: Gliap--a novel untypical L-asparaginase localized to rat brain astrocytes. J Neurochem. 2003 Jun;85(5):1117-25. doi: 10.1046/j.1471-4159.2003.01766.x.
Pubmed: 12753071
Amaya Y, Matsubasa T, Takiguchi M, Kobayashi K, Saheki T, Kawamoto S, Mori M: Amino acid sequence of rat argininosuccinate lyase deduced from cDNA. J Biochem. 1988 Jan;103(1):177-81. doi: 10.1093/oxfordjournals.jbchem.a122227.
Pubmed: 2834354
Matsubasa T, Takiguchi M, Amaya Y, Matsuda I, Mori M: Structure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genes. Proc Natl Acad Sci U S A. 1989 Jan;86(2):592-6. doi: 10.1073/pnas.86.2.592.
Pubmed: 2789519
Kawamoto S, Kaneko T, Mizuki N, Ohsuga A, Fukushima J, Amaya Y, Mori M, Okuda K: Molecular cloning and nucleotide sequence of rat brain argininosuccinate lyase cDNA with an extremely long 5'-untranslated sequence: evidence for the identity of the brain and liver enzymes. Brain Res Mol Brain Res. 1989 May;5(3):235-41. doi: 10.1016/0169-328x(89)90040-5.
Pubmed: 2725197
Hershfield JR, Madhavarao CN, Moffett JR, Benjamins JA, Garbern JY, Namboodiri A: Aspartoacylase is a regulated nuclear-cytoplasmic enzyme. FASEB J. 2006 Oct;20(12):2139-41. doi: 10.1096/fj.05-5358fje. Epub 2006 Aug 25.
Pubmed: 16935940
Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr: Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):456-61. doi: 10.1073/pnas.0607817104. Epub 2006 Dec 28.
Pubmed: 17194761
Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871.
Pubmed: 22673903
Kuwahara T, Takamoto S, Ito A: Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues. Agric Biol Chem. 1990 Jan;54(1):253-7.
Pubmed: 1368522
Kwan SW, Abell CW: cDNA cloning and sequencing of rat monoamine oxidase A: comparison with the human and bovine enzymes. Comp Biochem Physiol B. 1992 May;102(1):143-7. doi: 10.1016/0305-0491(92)90286-z.
Pubmed: 1526120
Tsugeno Y, Ito A: A key amino acid responsible for substrate selectivity of monoamine oxidase A and B. J Biol Chem. 1997 May 30;272(22):14033-6. doi: 10.1074/jbc.272.22.14033.
Pubmed: 9162023
Mirande M, Waller JP: Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase. J Biol Chem. 1989 Jan 15;264(2):842-7.
Pubmed: 2642907
Lazard M, Agou F, Cavarelli J, Latreille MT, Moras D, Mirande M: Genomic organization of the rat aspartyl-tRNA synthetase gene family: a single active gene and several retropseudogenes. Gene. 1996 Nov 21;180(1-2):197-205. doi: 10.1016/s0378-1119(96)00455-6.
Pubmed: 8973367
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000175
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