Quantitative gene expression of two types of glycine transporter in the rat central nervous system

Goebel, Donald W.

doi:10.1016/s0169-328x(96)00079-4

Cited by 8 publications

(13 citation statements)

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“…RNA dot blots, Western blotting, and immunohistochemistry studies have shown that HMGN3 is highly expressed in the mouse eye and brain (23,53). Glyt1 is known to be predominantly expressed in glia cells in the central nervous system and in retinal neurons (1,7,19,33,54). The Glyt1a splice form has also been detected in the liver and the lung, which is consistent with our results showing expression of Glyt1a but not Glyt1b in the hepatoma cell line used here.…”

Section: Identification Ofsupporting

confidence: 92%

Chromosomal Proteins HMGN3a and HMGN3b Regulate the Expression of Glycine Transporter 1

West

Castellini

Duncan

et al. 2004

Molecular and Cellular Biology

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HMGN proteins promote chromatin unfolding, enhance access to nucleosomes, and modulate transcription from chromatin templates. It is not known whether they act indiscriminately as general modulators of transcription or whether they regulate specific gene expression. Here, we investigated the role of HMGN3, a recently discovered HMGN family member, in transcription in vivo. We created cell lines overexpressing HMGN3a or its splice variant, HMGN3b, and analyzed their gene expression profiles using microarrays and reverse transcriptase PCR. We found that ectopic expression of HMGN3a alters the expression of approximately 0.8% of genes. Both HMGN3a and HMGN3b upregulate the expression of the glycine transporter 1 gene (Glyt1). Glyt1 encodes a membrane transporter that regulates the glycine concentration in synaptic junctions. Both GLYT1 and HMGN3 are highly expressed in glia cells and the eye, and we show that both proteins are coexpressed in the retina. Chromatin immunoprecipitation assays showed that HMGN3 protein is recruited to a region of the Glyt1 gene encompassing the Glyt1a transcriptional start site. These results suggest that HMGN3 regulates Glyt1 expression and demonstrate that members of the HMGN family can regulate the transcription of specific genes.In eukaryotes, all of the DNA is complexed with histone proteins and packaged into a highly folded, well-ordered, and dynamic structure called chromatin. This packaging modulates the ability of regulatory factors to access their DNA targets and plays a major role in regulating various nuclear activities, including transcription (18,48). Chromatin folding is modulated by numerous nuclear factors including nucleosome remodeling complexes, histone-modifying enzymes, and architectural proteins such as linker histones and HMG proteins. Members of the HMG superfamily interact with chromatin and DNA and affect a wide range of DNA-dependent activities such as transcription, replication, and recombination (9).One of the HMG families, the HMGN family, is comprised of small, basic proteins that bind specifically to nucleosomes (8). HMGN proteins are highly conserved and found only in vertebrates. The two founding members of the family, HMGN1 and HMGN2 (formerly named HMG-14 and HMG-17) (8), have been studied extensively. They contain a highly conserved nucleosome binding domain, a bipartite nuclear localization signal, and a C-terminal chromatin-unfolding domain (12, 47). When incorporated into minichromosomes, HMGN proteins confer a more open chromatin structure that is more sensitive to nucleases and that is transcribed and replicated more efficiently (13,14,35,46,50). Their ability to unfold chromatin also enhances the rate of DNA repair, as recently demonstrated in mice lacking HMGN1 (5).Although HMGN proteins display little or no DNA sequence specificity when binding to nucleosomes (45), several lines of evidence indicate that HMGN binding within the nucleus is nonrandom. Immunofluorescence studies have shown that HMGN proteins are localized in many foci within t...

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Section: Identification Ofsupporting

confidence: 92%

Chromosomal Proteins HMGN3a and HMGN3b Regulate the Expression of Glycine Transporter 1

West

Castellini

Duncan

et al. 2004

Molecular and Cellular Biology

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“…In the control rat retina ( fig. 4E), the immunoreactivity was abundant in the IPL and the INL, as previously reported [4,7,18,19]. In the GK rat retina ( fig.…”

Section: Immunohistochemical Sectionssupporting

confidence: 86%

“…The immunohistochemical localization of glycine receptors showed a distinct labeling pattern within the mammalian IPL and the INL that contained the synaptic complex with hyperpolarizing bipolar cells [18]. This study of control rat retinas showed the immunoreactivity for glycine in the IPL and the INL, and we observed glycine immunoreactivity as bipolar cells and amacrine cells in the INL.…”

Section: Discussionsupporting

confidence: 59%

“…Previous studies reported that only a subset of amacrine cells could synthesize glycine, and that regulating the glycine content of the glycine-containing bipolar cells increased their content only by virtue of the gap-junction coupling to glycine-containing amacrine cells [18,19]. The immunohistochemical localization of glycine receptors showed a distinct labeling pattern within the mammalian IPL and the INL that contained the synaptic complex with hyperpolarizing bipolar cells [18].…”

Section: Discussionmentioning

confidence: 84%

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Immunohistochemical Localization of Amino Acids in the Diabetic Retina of Goto-Kakizaki Rats

Takeo-Goto

Doi

et al. 2002

Ophthalmic Res

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The Goto-Kakizaki (GK) rat is a spontaneous model of non-insulin-dependent diabetes mellitus without obesity and diabetic retinopathy. We examined the retinal distribution of L-glutamate, gamma aminobutyric acid (GABA), glycine, and L-aspartate as neurotransmitters in the GK rat retina, using an immunohistochemical method with high-affinity antibodies. The retinal structures in the GK rats were the same as the controls. However, in the GK rats, immunoreactivity of L-glutamate and GABA was observed in the Müller and photoreceptor cells in addition to the immunoreactivity in normal rats. There was no change in glycine distribution between GK rats and controls. In the GK rats, L-aspartate accumulated in the inner segment of the photoreceptor cells in addition to the normal distribution. We consider that these immunoreactivity patterns in the GK rat retina might be induced by ischemia associated with diabetes mellitus.

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“…Antisense 32 P-CTP labeled probes and unlabeled sense-stranded cRNA were generated using SP6-or T7-RNA polymerase, respectively, following an established transcription protocol (Krause et al, 1989). Concentrations of each standard and probe were determined using optical density measurements at 260 nm (for standards) or percent incorporation of radiolabeled CTP into the probe (Xia et al, 1992;Goebel, 1996;Goebel and Poosch, 1999).…”

Section: Generation Of Riboprobes and Standardsmentioning

confidence: 99%

Transient Down-regulation of NMDA Receptor Subunit Gene Expression in the Rat Retina Following NMDA-induced Neurotoxicity is Attenuated in the Presence of the Non-competitive NMDA Receptor Antagonist MK-801

Goebel

Poosch

2001

Experimental Eye Research

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Quantitative gene expression of two types of glycine transporter in the rat central nervous system

Cited by 8 publications

References 0 publications

Chromosomal Proteins HMGN3a and HMGN3b Regulate the Expression of Glycine Transporter 1

Chromosomal Proteins HMGN3a and HMGN3b Regulate the Expression of Glycine Transporter 1

Immunohistochemical Localization of Amino Acids in the Diabetic Retina of Goto-Kakizaki Rats

Transient Down-regulation of NMDA Receptor Subunit Gene Expression in the Rat Retina Following NMDA-induced Neurotoxicity is Attenuated in the Presence of the Non-competitive NMDA Receptor Antagonist MK-801

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