d-Serine/N-methyl-d-aspartate receptor signaling decreases DNA-binding activity of the transcriptional repressor DREAM in Müller glia from the retina

Chavira-Suárez, Erika; Ramı́rez, Mónica; Lamas, Marta

doi:10.1016/j.neulet.2007.12.021

Cited by 10 publications

(5 citation statements)

References 25 publications

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“…Interestingly, in contrast with neurons, KCNIP3‐Ia has been detected in nuclei in glial cells where it is translocated out of the nuclei upon activation of glutamate receptors (Edling et al. 2007; Chavira‐Suarez et al. 2008).…”

Section: Discussionmentioning

confidence: 99%

Subcellular localization and transcription regulatory potency of KCNIP/Calsenilin/DREAM/KChIP proteins in cultured primary cortical neurons do not provide support for their role in CRE‐dependent gene expression

Pruunsild

Timmusk

2012

Journal of Neurochemistry

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KCNIP3/KChIP3 (voltage‐dependent K+ channel interacting protein 3), alias Calsenilin and downstream regulatory element antagonist modulator (DREAM), is a multifunctional protein that modulates A‐type potassium channels, affects processing of amyloid precursor protein and regulates transcription. KCNIP3 has been described to negatively influence the activity of CREB (cAMP/Ca2+‐response element binding protein), an essential factor in neuronal activity‐dependent gene expression regulation. However, reports on intracellular localization of KCNIP3 in neurons are diverse and necessitate additional analyses of distribution of KCNIPs in cells to clarify the potential of KCNIP3 to fulfill its functions in different cell compartments. Here, we examined localization of the entire family of highly similar KCNIP proteins in neuronal cells and show that over‐expressed isoforms of KCNIP1/KChIP1, KCNIP2/KChIP2, KCNIP3/KChIP3, and KCNIP4/KChIP4 had varied, yet partially overlapping subcellular localization. In addition, although some of the over‐expressed KCNIP isoforms localized to the nucleus, endogenous KCNIPs were not detected in nuclei of rat primary cortical neurons. Moreover, we analyzed the role of KCNIP proteins in cAMP/Ca2+‐response element (CRE)‐dependent transcription by luciferase reporter assay and electrophoretic mobility shift assay and report that our results do not support the role for KCNIPs, including DREAM/Calsenilin/KChIP3, in modulation of CREB‐mediated transcription in neurons.

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Section: Discussionmentioning

confidence: 99%

Subcellular localization and transcription regulatory potency of KCNIP/Calsenilin/DREAM/KChIP proteins in cultured primary cortical neurons do not provide support for their role in CRE‐dependent gene expression

Pruunsild

Timmusk

2012

Journal of Neurochemistry

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“…Before transcription can occur, however, we believe that the DREAM protein must be translocated out of the nucleus. As mentioned earlier, activation of the NMDA receptor resulted in decreased nuclear localization of the DREAM protein in retinal Muller glial cells [31] and brain astrocytes [30]. Therefore, we assume that the dominant function of the NMDA receptor in the N+F group is to mediate the mechanisms for the translocation of the DREAM protein out of the nucleus.…”

Section: Discussionmentioning

confidence: 86%

“…During basal conditions or in the absence of intracellular Ca 2+ in brain astrocytes, the DREAM protein is bound to the DRE site of the c-Fos gene and assumes a nuclear localization [30]. Administration of glutamate, the neurotransmitter for the NMDA receptor, caused decreased nuclear localization of the DREAM protein, translocated it into the cytoplasm, and restored the distribution of the DREAM protein in brain astrocytes [30] as well as in retinal Muller glial cells [31]. Blockade of the NMDA receptor by the non-competitive antagonist MK801 reverses this effect [32].…”

Section: Discussionmentioning

confidence: 99%

The Effects of Pre-emptive Administration of Ketamine and norBNI on Pain Behavior, c-Fos, and Prodynorphin Protein Expression in the Rat Spinal Cord after Formalin-induced Pain Is Modulated by the DREAM Protein

2013

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BackgroundWe investigated the effects of pre-emptive administration of ketamine and norBNI on pain behavior and the expression of DREAM, c-Fos, and prodynorphin proteins on the ipsilateral side of the rat spinal cord at 2 and 4 hours after formalin injection.MethodsEighty-four male Sprague Dawley rats were divided into 4 major groups consisting of control rats (C) (n = 12), rats given only formalin injections (F) (n = 24), and rats treated with pre-emptive administration of either ketamine (K+F) (n = 24) or norBNI (N+F) (n = 24). The non-control groups were further divided into subgroups consisting of rats that were sacrificed at 2 and 4 hours (n = 12 for each group) after formalin injection. Pain behavior was recorded for 1 hour. After 2 and 4 hours, the rats were sacrificed and the spinal cords (L4-L5 sections) were removed for immunohistochemistry and Western blot analysis.ResultsThe pain behavior response was reduced in the K+F group compared to the other groups during the second phase of the formalin pain response. We detected an increase in the nuclear DREAM protein level in the K+F group at 2 and 4 hours and a transient decrease in the N+F group at 2 hours; however, it increased at 4 hours after injection. Fos-like immunoreactivity (FLI) and Prodynorphin-like immunoreactivity (PLI) neurons decreased in the K+F group but increased in the N+F group at 2 hours after injection. While FLI decreased, PLI increased in all groups at 4 hours after injection.ConclusionsWe suggest that NMDA and kappa opioid receptors can modulate DREAM protein expression, which can affect pain behavior and protein transcriptional processes at 2 hours and bring about either harmful or protective effects at 4 hours after formalin injection.

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“…First, a few studies have reported contradicting results regarding the role of DREAM in the retina. For example, previous studies have reported that the activation of NMDARs decreased the expression of the DREAM [ 27 ], while hyperglycemia up-regulated the expression of the same protein in cultured Müller cells [ 28 ]. Nonetheless, it is unclear how DREAM expressed in Müller cells affects the survival of RGCs and other cell types.…”

Section: Discussionmentioning

confidence: 99%

Decreased Expression of DREAM Promotes the Degeneration of Retinal Neurons

2015

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The intrinsic mechanisms that promote the degeneration of retinal ganglion cells (RGCs) following the activation of N-Methyl-D-aspartic acid-type glutamate receptors (NMDARs) are unclear. In this study, we have investigated the role of downstream regulatory element antagonist modulator (DREAM) in NMDA-mediated degeneration of the retina. NMDA, phosphate-buffered saline (PBS), and MK801 were injected into the vitreous humor of C57BL/6 mice. At 12, 24, and 48 hours after injection, expression of DREAM in the retina was determined by immunohistochemistry, western blot analysis, and electrophoretic mobility-shift assay (EMSA). Apoptotic death of cells in the retina was determined by terminal deoxynucleotidyl transferace dUTP nick end labeling (TUNEL) assays. Degeneration of RGCs in cross sections and in whole mount retinas was determined by using antibodies against Tuj1 and Brn3a respectively. Degeneration of amacrine cells and bipolar cells was determined by using antibodies against calretinin and protein kinase C (PKC)-alpha respectively. DREAM was expressed constitutively in RGCs, amacrine cells, bipolar cells, as well as in the inner plexiform layer (IPL). NMDA promoted a progressive decrease in DREAM levels in all three cell types over time, and at 48 h after NMDA-treatment very low DREAM levels were evident in the IPL only. DREAM expression in retinal nuclear proteins was decreased progressively after NMDA-treatment, and correlated with its decreased binding to the c-fos-DRE oligonucleotides. A decrease in DREAM expression correlated significantly with apoptotic death of RGCs, amacrine cells and bipolar cells. Treatment of eyes with NMDA antagonist MK801, restored DREAM expression to almost normal levels in the retina, and significantly decreased NMDA-mediated apoptotic death of RGCs, amacrine cells, and bipolar cells. Results presented in this study show for the first time that down-regulation of DREAM promotes the degeneration of RGCs, amacrine cells, and bipolar cells.

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d-Serine/N-methyl-d-aspartate receptor signaling decreases DNA-binding activity of the transcriptional repressor DREAM in Müller glia from the retina

Cited by 10 publications

References 25 publications

Subcellular localization and transcription regulatory potency of KCNIP/Calsenilin/DREAM/KChIP proteins in cultured primary cortical neurons do not provide support for their role in CRE‐dependent gene expression

Subcellular localization and transcription regulatory potency of KCNIP/Calsenilin/DREAM/KChIP proteins in cultured primary cortical neurons do not provide support for their role in CRE‐dependent gene expression

The Effects of Pre-emptive Administration of Ketamine and norBNI on Pain Behavior, c-Fos, and Prodynorphin Protein Expression in the Rat Spinal Cord after Formalin-induced Pain Is Modulated by the DREAM Protein

Decreased Expression of DREAM Promotes the Degeneration of Retinal Neurons

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