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Glutamate decarboxylase 1 (brain, 67kDa) (GAD67), also known as GAD1, is a human gene.[1]

This gene encodes one of several forms of glutamic acid decarboxylase, identified as a major autoantigen in insulin-dependent diabetes. The enzyme encoded is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for this enzyme has been identified in the human pancreas since it has been identified as an autoantigen and an autoreactive T cell target in insulin-dependent diabetes. This gene may also play a role in the stiff man syndrome. Deficiency in this enzyme has been shown to lead to pyridoxine dependency with seizures. Alternative splicing of this gene results in two products, the predominant 67-kD form and a less-frequent 25-kD form.[1]

See alsoEdit


GAD1 has been shown to interact with GAD2.[2]


  1. 1.0 1.1 Entrez Gene: GAD1 glutamate decarboxylase 1 (brain, 67kDa).
  2. Dirkx, R, Thomas A, Li L, Lernmark A, Sherwin R S, De Camilli P, Solimena M (February 1995). Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2-terminal region of the 65-kDa isoform of glutamic acid decarboxylase. J. Biol. Chem. 270 (5): 2241–6.

Further readingEdit

  • Kelly CD, Edwards Y, Johnstone AP, et al. (1992). Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase. Ann. Hum. Genet. 56 (Pt 3): 255–65.
  • Bu DF, Erlander MG, Hitz BC, et al. (1992). Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2115–9.
  • Giorda R, Peakman M, Tan KC, et al. (1991). Glutamic acid decarboxylase expression in islets and brain. Lancet 338 (8780): 1469–70.
  • Persson H, Pelto-Huikko M, Metsis M, et al. (1990). Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells. Mol. Cell. Biol. 10 (9): 4701–11.
  • Cram DS, Barnett LD, Joseph JL, Harrison LC (1991). Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. Biochem. Biophys. Res. Commun. 176 (3): 1239–44.
  • Dirkx R, Thomas A, Li L, et al. (1995). Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2-terminal region of the 65-kDa isoform of glutamic acid decarboxylase. J. Biol. Chem. 270 (5): 2241–6.
  • Bu DF, Tobin AJ (1994). The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics 21 (1): 222–8.
  • Yamashita K, Cram DS, Harrison LC (1993). Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets. Biochem. Biophys. Res. Commun. 192 (3): 1347–52.
  • Kawasaki E, Moriuchi R, Watanabe M, et al. (1993). Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet. Biochem. Biophys. Res. Commun. 192 (3): 1353–9.
  • Asada H, Kawamura Y, Maruyama K, et al. (1997). Mice lacking the 65 kDa isoform of glutamic acid decarboxylase (GAD65) maintain normal levels of GAD67 and GABA in their brains but are susceptible to seizures. Biochem. Biophys. Res. Commun. 229 (3): 891–5.
  • McHale DP, Mitchell S, Bundey S, et al. (1999). A gene for autosomal recessive symmetrical spastic cerebral palsy maps to chromosome 2q24-25. Am. J. Hum. Genet. 64 (2): 526–32.
  • Chessler SD, Lernmark A (2000). Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. J. Biol. Chem. 275 (7): 5188–92.
  • Luo J, Kaplitt MG, Fitzsimons HL, et al. (2002). Subthalamic GAD gene therapy in a Parkinson's disease rat model. Science 298 (5592): 425–9.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.
  • Chessler SD, Hampe CS, Ortqvist E, et al. (2003). Immune reactivity to GAD25 in type 1 diabetes mellitus. Autoimmunity 35 (5): 335–41.
  • Demakova EV, Korobov VP, Lemkina LM (2003). [Determination of gamma-aminobutyric acid concentration and activity of glutamate decarboxylase in blood serum of patients with multiple sclerosis]. Klin. Lab. Diagn. (4): 15–7.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat. Genet. 36 (1): 40–5.
  • Flace P, Benagiano V, Lorusso L, et al. (2004). Glutamic acid decarboxylase immunoreactive large neuron types in the granular layer of the human cerebellar cortex. Anat. Embryol. 208 (1): 55–64.
  • De Luca V, Muglia P, Masellis M, et al. (2004). Polymorphisms in glutamate decarboxylase genes: analysis in schizophrenia. Psychiatr. Genet. 14 (1): 39–42.
  • Kanno K, Suzuki Y, Yamada A, et al. (2004). Association between nonsyndromic cleft lip with or without cleft palate and the glutamic acid decarboxylase 67 gene in the Japanese population. Am. J. Med. Genet. A 127 (1): 11–6.

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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