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  • Anatomy of glutamic acid decarboxylase immunoreactive neurons and axons in the rat medial geniculate body. 3209752

    This is a study of the form, density, and distribution of glutamic acid decarboxylase (GAD) immunoreactive neurons and puncta (axon terminals) in the adult rat medial geniculate complex. GAD-positive elements were stained by either the peroxidase-antiperoxidase or avidin-biotin procedures. Thalamic architectonic subdivisions were defined independently in Golgi, Nissl, plastic-embedded semi-thin, and fiber-stained preparations, and from investigations of medial geniculate connectivity. GAD-positive neurons represent only approximately 1% of medial geniculate neurons. They occur in the three major medial geniculate subdivisions (ventral, dorsal, and medial). There is variability between subdivisions in the form and number of such neurons, and among the puncta. In the ventral division, immunopositive somata may have sparsely branched dendrites as long as 300-400 microns and capped with varicose expansions or bouton-like sprays of appendages. These closely appose the somata or primary dendrites of other cells; the axons of these GAD-positive neurons are also immunostained. In the dorsal division there are fewer GAD-positive neurons and their structure is different. Their dendrites are rarely immunoreactive for more than 100-150 microns; nor can their immunostained axons be traced very far. In the medial division the number of GAD-positive neurons, considering the relatively small size of this division, was high. These neurons rarely have immunostained dendrites, and more than one type of neuron is immunoreactive. The average somatic diameter of GAD-positive neurons is about 60% of that of non-immunostained cells in semi-thin material; however, the range of somatic area and the dendritic variability of these neurons suggest that cells representing more than one population are immunopositive and include all but the largest neurons. The puncta also show regional differences. Small (0.5-2 microns in diameter), medium (2-3 microns), or large (greater than 3 microns) puncta occur. In the ventral division, the predominantly medium-sized puncta are about four times as numerous on a unit/area basis than in the dorsal division, where they are far smaller and more delicate; medial division puncta are as numerous as those in the ventral division, but are much larger and coarser, and may form perisomatic arrangements. Controls were devoid of specific immunostaining.(ABSTRACT TRUNCATED AT 400 WORDS)
    Document Type:
    Reference
    Product Catalog Number:
    MAB351R
    Product Catalog Name:
    Anti-Glutamate Decarboxylase Antibody, 65 kDa isoform, clone GAD-6

  • Glutamic acid decarboxylase 65 and 67 expression in the lateral septum is up-regulated in association with the postpartum period in mice. 22750123

    The postpartum period in mammals undergoes a variety of physiological adaptations, including metabolic, behavioral and neuroendocrine alterations. GABA signaling has been strongly linked to various emotional states, stress responses and offspring protection. However, whether GABA signaling may change in the lateral septum (LS), a core brain region for regulating behavioral, emotional and stress responses in postpartum mice has not previously been examined. In this study, we tested whether the expression of two isoforms of glutamic acid decarboxylase (GAD), GAD65 (GAD2) and GAD67 (GAD1), the rate-limiting enzyme for GABA synthesis, exhibits altered expression in postpartum mice relative to nonmaternal, virgin mice. Using microdissected septal tissue from virgin and age-matched postpartum females, quantitative real-time PCR and Western blotting were carried out to assess GAD mRNA and protein expression, respectively. We found both protein and mRNA expression of GAD67 in the whole septum was up-regulated in postpartum mice. By contrast, no significant difference in the whole septum was observed in GAD65 expression. We then conducted a finer level of analysis using smaller microdissections and found GAD67 to be significantly increased in rostral LS, but not in caudal LS or medial septum (MS). Further, GAD65 mRNA expression in rostral LS, but not in caudal LS or MS was also significantly elevated in postpartum mice. These findings suggest that an increased GABA production in rostral LS of the postpartum mice via elevated GAD65 and GAD67 expression may contribute to multiple alterations in behavioral and emotional states, and responses to stress that occur during the postpartum period. Given that rostral LS contains GABA neurons that are projection neurons or local interneurons, it still needs to be determined whether the function of elevated GABA is for local or distant action or both.
    Document Type:
    Reference
    Product Catalog Number:
    MAB5406
    Product Catalog Name:
    Anti-GAD67 Antibody, clone 1G10.2

  • Rat brain glutamic acid decarboxylase sequence deduced from a cloned cDNA. 2299361

    A cDNA clone complementary to the rat brain glutamic acid decarboxylase mRNA was isolated from a rat brain cDNA expression library using an antibody specific to the enzyme. The cDNA insert has been shown to direct the synthesis of an active protein in Escherichia coli. In this study, the nucleotide sequence of this clone, which includes the complete coding region, is presented. The predicted protein is 593 amino acids in length. The first 557 residues display a 95% identity when compared with the corresponding cat sequence. However, the deduced amino acid sequence of the carboxy-terminal end of the rat protein, downstream of residue 557, is totally different from the cat, whereas it agrees with a published partial peptidic sequence of the rat protein.
    Document Type:
    Reference
    Product Catalog Number:
    AB1511

  • Pancreatic beta cells express two autoantigenic forms of glutamic acid decarboxylase, a 65-kDa hydrophilic form and a 64-kDa amphiphilic form which can be both membrane-b ... 1939164

    The 64-kDa pancreatic beta-cell autoantigen, which is a target of autoantibodies associated with early as well as progressive stages of beta-cell destruction, resulting in insulin-dependent diabetes (IDDM) in humans, has been identified as the gamma-aminobutyric acid-synthesizing enzyme glutamic acid decarboxylase. We have identified two autoantigenic forms of this protein in rat pancreatic beta-cells, a Mr 65,000 (GAD65) hydrophilic and soluble form of pI 6.9-7.1 and a Mr 64,000 (GAD64) component of pI 6.7. GAD64 is more abundant than GAD65 and has three distinct forms with regard to cellular compartment and hydrophobicity. A major portion of GAD64 is hydrophobic and firmly membrane-anchored and can only be released from membrane fractions by detergent. A second portion is hydrophobic but soluble or of a low membrane avidity, and a third minor portion is soluble and hydrophilic. All the GAD64 forms have identical pI and mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Results of pulse-chase labeling with [35S]methionine are consistent with GAD64 being synthesized as a soluble protein that is processed into a firmly membrane-anchored form in a process which involves increases in hydrophobicity but no detectable changes in size or charge. All the GAD64 forms can be resolved into two isoforms, alpha and beta, which differ by approximately 1 kDa in mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis but are identical with regard to all other parameters analyzed in this study. GAD65 has a shorter half-life than the GAD64 forms, remains hydrophilic and soluble, and does not resolve into isomers. Comparative analysis of the brain and beta-cell forms of GAD show that GAD65 and GAD64 in pancreatic beta-cells correspond to the larger and smaller forms of GAD in brain, respectively. The expression of different forms and the flexibility in subcellular localization of the GAD autoantigen in beta-cells may have implications for both its function and autoantigenicity.
    Document Type:
    Reference
    Product Catalog Number:
    ABN101
    Product Catalog Name:
    Anti-GAD65 Antibody

  • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. 10373413

    Within chromatin, reversible acetylation of core histones is critical for transcriptional activation of eukaryotic target genes. The recent identification of intrinsic histone acetyltransferase (HAT) catalytic activity from a number of transcriptional co-activators (including yeast GCN5, p300/CBP, P/CAF, and TAFII250), has underscored the importance of protein acetylation in transcriptional control. The GCN5 family is the prototype for a diverse group of at least four distinct human HATs families. Although there is now a clear link between in vivo HAT catalytic activity and gene activation, little is known about the molecular mechanisms of histone acetylation. Herein, we report the first detailed biochemical study that probes the catalytic mechanism and the function of invariant glutamic acid 173 within the GCN5 family of HATs. Our results suggest that the HAT reaction involves the formation of a ternary complex (histones, acetyl-CoA, and enzyme) where the epsilon-amino group of histone lysine residues directly attacks the bound acetyl-CoA. The acetylation reaction requires deprotonation of the epsilon-amino group prior to nucleophilic attack. Employing site-directed mutagenesis, chemical modification, steady-state, and pH-dependent rate analysis, it is demonstrated that glutamic acid 173 is an essential catalytic residue, acting as a general base catalyst by deprotonating the histone substrate.
    Document Type:
    Reference
    Product Catalog Number:
    12-372
    Product Catalog Name:
    Histone H4 Peptide, biotin conjugate, residues 2-24