Two genes encode distinct glutamate decarboxylases

doi:10.1016/0896-6273(91)90077-D

Neuron

Volume 7, Issue 1, July 1991, Pages 91-100

https://doi.org/10.1016/0896-6273(91)90077-D Get rights and content

Abstract

γ-Aminobutyric acid (GABA) is the most widely distributed known inhibitory neurotransmitter in the vertebrate brain. GABA also serves regulatory and trophic roles in several other organs, including the pancreas. The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid sequence, antigenicity, cellular and subcellular location, and interaction with the GAD co-factor pyridoxal phosphate. These forms, GAD₆₅ and GAD₆₇, derive from two genes. The distinctive properties of the two GADS provide a substrate for understanding not only the multiple roles of GABA in the nervous system, but also the autoimmune response to GAD in insulin-dependent diabetes mellitus.

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^†: Present address: Department of Molecular Biology MB-10, Scripps Clinic and Research Foundation, 10666 North Torrey Pines Road, La Jolla, California 92037.

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Neuron

ArticleTwo genes encode distinct glutamate decarboxylases

Abstract

Lancet

Biochem. Biophys. Res. Commun.

Anal. Biochem.

J. Biol. Chem.

Anal. Biochem.

Gene

Brain Res.

Brain Res.

Brain Res. Bull.

Neuroscience

Anal. Biochem.

Brain Res.

J. Mol. Biol.

Molecular Biology of the Cell

Antibodies to a 64,000 M, human islet cell antigen precede the clinical onset of insulin-dependent diabetes

J. Clin. Invest.

Identification of the 64K autoantigen in insulindependent diabetes as the GABA-synthesizing enzyme glutamic acid decarboxylase

Nature

Kinetics of brain glutamate decarboxylase-interactions with glutamate pyridoxal 5′-phosphate and glutamate-pyridoxal 5′-phosphate Schiff base. I

Neurochem.

Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers

J. Cell Biol.

A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain

Biochem. J.

p21ras is modified by a farnesyl isoprenoid

Characterization of the protein purified with monoclonal antibodies to glutamic acid decarboxylase

J. Neurosci.

Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease

Biochemistry

Calcium-dependent binding of brain glutamate decarboxylase to phospholipid vesicles

J. Neurochem.

Brain glutamate decarboxylase: properties of its calcium-dependent binding to liposomes and kinetics of the bound and the free enzyme

J. Neurchem.

Molecular cloning and analysis of cDNA encoding a plant tryptophan decarboxylase: comparison with animal dopa decarboxylase

Two forms of rat brain glutamicacid decarboxylase differ in their dependence on free pyridoxal phosphate

J. Neurochem.

The structural and functional heterogeneity of glutamic acid decarboxylase: a review

Neurochem. Res.

Sequence and structure of the dopa decarboxlyase gene of Drosophila: evidence for novel RNA splicing variants

EMBO J.

The distribution of glutamate decarboxylase and aspartatetransaminase in subcellular fractions of rat and guinea-pig brain

Biochem. J.

Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer

Multiple use of Southern blots

Biotechniques

Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNAorgenomic clones encodingthe iron-sulfur protein of succinate dehydrogenase from several species

Article
Two genes encode distinct glutamate decarboxylases