Disease relevance of GAD1

• Amacrine cells of the inner nuclear layer and displaced amacrine cells of the ganglion cell layer were labelled, using glutamic acid decarboxylase (GAD) immunohistochemistry and [3H]muscimol uptake [1].
• Alterations in expression of messenger RNAs encoding two isoforms of glutamic acid decarboxylase in the globus pallidus and entopeduncular nucleus in animals symptomatic for and recovered from experimental Parkinsonism [2].

Psychiatry related information on GAD1

• Furthermore, administration of antisense oligonucleotides against glutamic acid decarboxylase (GAD) mRNA into the same area produced a significant decrease in wakefulness and an increase in REM sleep [3].

High impact information on GAD1

• These include the co-localization of glutamic acid decarboxylase (GAD, the biosynthetic enzyme of the inhibitory neurotransmitter, gamma-aminobutyric acid) with the mitochondrial enzyme, cytochrome oxidase (CO) in functionally distinct subcompartments of ocular dominance columns [4].
• We have examined the regulation of expression of the genes for the neuronal growth-associated protein GAP43, the type II calcium/calmodulin-dependent protein kinase, and glutamic acid decarboxylase in the kitten visual cortex during normal postnatal development and after a period of visual deprivation [5].
• Since GABAergic cells are interneurons, a double-staining procedure was used to test for the coexistence of cholecystokinin (CCK), somatostatin (SRIF), neuropeptide Y (NPY), corticotropin-releasing factor (CRF), vasoactive intestinal polypeptide (VIP), and CaBP with glutamic acid decarboxylase (GAD) [6].
• Glutamic acid decarboxylase (GAD;E.C. 4.1.1.15) catalyzes the production of GABA, the major inhibitory neurotransmitter in the mammalian brain [7].
• Glutamic acid decarboxylase cDNA: nucleotide sequence encoding an enzymatically active fusion protein [7].

Biological context of GAD1

• The morphogenesis of glutamic acid decarboxylase in the neostriatum of the cat: neuronal and ultrastructural localization [8].
• Peripheral nerve stimulation increases Fos immunoreactivity without affecting type II Ca2+/calmodulin-dependent protein kinase, glutamic acid decarboxylase, or GABAA receptor gene expression in cat spinal cord [9].

Anatomical context of GAD1

• The GABA neurons and their processes in the cat motor thalamic nuclei were identified and studied with glutamic acid decarboxylase (GAD) immunocytochemistry at both the light and electron microscopic levels [10].
• Immunocytochemical methods were used to identify neurons in the ventral posterior nucleus of the cat and Galago senegalensis that contain glutamic acid decarboxylase (GAD), the synthetic enzyme for the inhibitory neurotransmitter, GABA [11].
• Electron microscopic immunocytochemistry of the same part of the reticular nucleus revealed processes immunoreactive for glutamic acid decarboxylase and identifiable as both collateral axon terminals and presynaptic dendrites of GABAergic reticular nucleus cells [12].
• We also measured levels of immunoreactivity of the inhibitory presynaptic terminal marker glutamic acid decarboxylase (GAD)65 in deprived relative to nondeprived ODCs [13].
• We have examined the distribution of neurons and terminals immunoreactive for glutamic acid decarboxylase (GAD) in the thalamus and adjacent structures of the opossum (Didelphis virginiana) and the rabbit and have compared this distribution with the distributions we described previously for the cat and bushbaby (Galago senegalensis) [14].

Associations of GAD1 with chemical compounds

• Immunohistochemical demonstration of differential substance P-, met-enkephalin-, and glutamic-acid-decarboxylase-containing cell body and axon distributions in the corpus striatum of the cat [15].
• Neurobiotin-labeled late-I neurons revealed immunoreactivity for glutamic acid decarboxylase as well as N-methyl-D-aspartate (NMDA) receptors [16].
• Cells were plotted with the aid of an image analysis system through the medullary reticular formation and raphe in adjacent sections immunostained for choline acetyltransferase, glutamic acid decarboxylase and serotonin [17].
• Transmitters were identified by using antibodies raised against vesicular glutamate transporters 1 and 2, glutamic acid decarboxylase and the glycine transporter 2 [18].
• Localization of L-glutamic acid decarboxylase mRNA in cat retinal horizontal cells by in situ hybridization [19].

Analytical, diagnostic and therapeutic context of GAD1

• Dual-color immunofluorescence revealed that focal accumulations of beta 2/beta 3-subunit immunoreactivity were frequently apposed by glutamic acid decarboxylase (GAD)-immunoreactive terminals [20].
• Immunocytochemical localization of glutamic acid decarboxylase (GAD) and glutamine synthetase (GS) in the area postrema of the cat. Light and electron microscopy [21].
• Western blot analysis showed that the expression of both GAD67 and GAD65 increased to approximately two-thirds of the adult level during the first 5 postnatal weeks and gradually increased thereafter [22].

References