Opsin, G-protein and 48-kDa protein in normal and rd mouse retinas: Developmental expression of mRNAS and proteins and light/dark cycling of mRNAs

Bowes, Cathy; Veen, Theo van; Farber, Débora B.

doi:10.1016/0014-4835(88)90049-8

Cited by 145 publications

(84 citation statements)

References 21 publications

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“…, Lerner, et al, 2001 Rho expression varies during development, dramatically increasing during maturation of rod outer-segments. (Bowes, et al, 1988) In mature retina, Rho expression continues to be regulated to follow the circadian patterns of rod outer-segment formation. (Bowes, et al, 1988, Matsumoto and Bok, 1984, von Schantz, et al, 1999 The Rho proximal promoter region is sufficient for rod-specific expression and includes several DNA sequence elements that bind to proteins in vitro.…”

Section: Discussionmentioning

confidence: 99%

“…Outer-segment length and Rhodopsin protein concentration continue to increase until P30. (Bowes, et al, 1988) To examine the relative FIZ1 protein content of mouse neural retina throughout the retinal maturation period, samples were compared representing post-natal days P1, P9, P15, P21, and P32. (Fig.…”

Section: Neural Retina Fiz1 Protein Expression Increases During Photomentioning

confidence: 99%

“…This pattern agreed with previously published data (northern blot), and provided a genetic marker for photoreceptor-specific gene expression during maturation. (Bowes, et al, 1988) Relative Fiz1 mRNA levels also increased in concentration throughout the maturation period when examined relative to Gapdh mRNA levels using the Amplitaq Gold real-time PCR method. (Fig.…”

Section: Neural Retina Fiz1 Mrna Content Increases During Photoreceptmentioning

confidence: 99%

“…This expression pattern is similar for other rodspecific visual transduction genes, including Pde6b. (Bowes, et al, 1988) If FIZ1 has influence on the expression level of photoreceptor specific genes, such as Rho, it is expressed during the correct time period.…”

Section: Fiz1 Protein Expression In Retinal Developmentmentioning

confidence: 99%

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FIZ1 is expressed during photoreceptor maturation, and synergizes with NRL and CRX at rod-specific promoters in vitro

Mali

Zhang

Hoerauf

et al. 2007

Experimental Eye Research

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FIZ1 (Flt-3 Interacting Zinc-finger) interacts and co-purifies with the rod-specific transcription factor NRL (Neural Retina Leucine zipper). We hypothesize that FIZ1 is part of an interface between cell-specific factors, like NRL, and more ubiquitous regulatory networks that vary the absolute expression levels of some rod-specific genes (i.e. Rhodopsin). As part of an ongoing exploration of FIZ1's role in neural retina, in vivo, we have taken the first look at FIZ1 expression in the developing mouse retina during the retinal maturation period. Using the normal C57/B6 mouse as a model, multiple approaches were used including: immunoblotting, immunohistochemistry, and quantitative real-time PCR. Functional implications of FIZ1/NRL interaction, on NRL-and CRX-mediated activation of the Rhodopsin (Rho) and cGMPphosphodiesterase β-subunit gene (PDE6B) promoters, were examined by co-transfection assays. Immunoblot analysis revealed that FIZ1 protein levels were lowest in immature mouse neural retina (P0). FIZ1 concentration increased at least ten-fold as the neural retina matured to the adult state (P21 and later). Immunohistochemical comparison of immature post-natal and mature adult retina revealed increasing FIZ1 protein in photoreceptors, the inner plexiform layer, and the ganglion cell layer. Total retinal Fiz1 mRNA content increased as the neural retina matured. The expected increase in Rho mRNA level was also monitored as a genetic marker of photoreceptor maturation. In transient co-transfection assays of CV1 cells, FIZ1 synergized with NRL to activate transcription from the Rho and PDE6B gene promoters with some differences. In the case of the Rho promoter, FIZ1 synergized when both NRL and CRX were present. With the PDE6B promoter, FIZ1 synergized with NRL alone, and the inclusion of CRX decreased this synergy.Conclusions-These findings support previous evidence that FIZ1 is present in rodphotoreceptors. (Co-immunoprecipitation from nuclear-protein extracts with rod-specific NRL) FIZ1 expression increases in the neural retina during the retinal maturation period. Additionally, in vitro experiments demonstrate that FIZ1 has the potential to significantly increase the NRLmediated activation of photoreceptor-specific promoters. While CRX is not a strong activator of the PDE6B promoter, alone or with NRL, CRX decreased the synergy of NRL with FIZ1.

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Section: Discussionmentioning

confidence: 99%

Section: Neural Retina Fiz1 Protein Expression Increases During Photomentioning

confidence: 99%

Section: Neural Retina Fiz1 Mrna Content Increases During Photoreceptmentioning

confidence: 99%

Section: Fiz1 Protein Expression In Retinal Developmentmentioning

confidence: 99%

See 2 more Smart Citations

FIZ1 is expressed during photoreceptor maturation, and synergizes with NRL and CRX at rod-specific promoters in vitro

Mali

Zhang

Hoerauf

et al. 2007

Experimental Eye Research

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“…Nr1d1 is a member of the circadian clock (Yin et al, 2006) involved in regulating diurnal variations in gene expression. It is also known that the expression of some photoreceptor genes such as rhodopsin is under circadian regulation (Bowes et al, 1988;von Schantz et al, 1999). Thus the Nr2e3/Nr1d1 interaction may play a role in regulating the diurnal expression pattern of these genes.…”

Section: Mechanisms Of Actionmentioning

confidence: 99%

Regulation of photoreceptor gene expression by Crx-associated transcription factor network

2008

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Rod and cone photoreceptors in the mammalian retina are special types of neurons that are responsible for phototransduction, the first step of vision. Development and maintenance of photoreceptors require precisely regulated gene expression. This regulation is mediated by a network of photoreceptor transcription factors centered on Crx, an Otx-like homeodomain transcription factor. The cell type (subtype) specificity of this network is governed by factors that are preferentially expressed by rods or cones or both, including the rod-determining factors neural retina leucine zipper protein (Nrl) and the orphan nuclear receptor Nr2e3; and cone-determining factors, mostly nuclear receptor family members. The best-documented of these include thyroid hormone receptor β2 (Trβ2), retinoid related orphan receptor Rorβ, and retinoid X receptor Rxrγ. The appropriate function of this network also depends on general transcription factors and co-factors that are ubiquitously expressed, such as the Sp zinc finger transcription factors and STAGA coactivator complexes. These cell type-specific and general transcription regulators form complex interactomes; mutations that interfere with any of the interactions can cause photoreceptor development defects or degeneration. In this manuscript, we review recent progress on the roles of various photoreceptor transcription factors and interactions in photoreceptor subtype development. We also provide evidence of auto-, para-, and feedback regulation among these factors at the transcriptional level. These protein-protein and protein-promoter interactions provide precision and specificity in controlling photoreceptor subtype-specific gene expression, development and survival. Understanding these interactions may provide insights to more effective therapeutic interventions for photoreceptor diseases.

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Evidence from normal and degenerating photoreceptors that two outer segment integral membrane proteins have separate transport pathways

et al. 1997

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Detachment of the neural retina from the retinal pigment epithelium induces photoreceptor degeneration. We studied the effects of this degeneration on the localization of two photoreceptor outer segment-specific integral membrane proteins, opsin and peripherin/rds, in rod photoreceptors. Results from laser scanning confocal microscopic and electron microscopic immunolocalization demonstrate that these two proteins, normally targeted to the newly-forming discs of the outer segments, accumulate in different sub-cellular compartments during photoreceptor degeneration: opsin immunolabeling increases throughout the photoreceptor cell's plasma membrane, while peripherin/rds immunolabeling occurs within cytoplasmic vesicles. The simplest hypothesis to explain our results is that these proteins are transported in different post-Golgi transport vesicles and separately inserted into the plasma membrane. More complex mechanisms involve having the two co-transported and then opsin finds its way into the plasma membrane but peripherin/rds does not, remaining behind in vesicles. Alternatively, both insert into the plasma membrane but peripherin/rds is recycled into cytoplasmic vesicles. We believe the data most strongly supports the first possibility. Although the transport pathways for these proteins have not been fully characterized, the presence of peripherin/rds-positive vesicles adjacent to the striated rootlet suggests a transport role for this cytoskeletal element. The accumulation of these proteins in photoreceptors with degenerated outer segments may also indicate that their rate of synthesis has exceeded the combined rates of their incorporation into newly forming outer segment disc membranes and their degradation. The accumulation may also provide a mechanism for rapid recovery of the outer segment following retinal reattachment and return of the photoreceptor cell to an environment favorable to outer segment regeneration.

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Opsin, G-protein and 48-kDa protein in normal and rd mouse retinas: Developmental expression of mRNAS and proteins and light/dark cycling of mRNAs

Cited by 145 publications

References 21 publications

FIZ1 is expressed during photoreceptor maturation, and synergizes with NRL and CRX at rod-specific promoters in vitro

FIZ1 is expressed during photoreceptor maturation, and synergizes with NRL and CRX at rod-specific promoters in vitro

Regulation of photoreceptor gene expression by Crx-associated transcription factor network

Evidence from normal and degenerating photoreceptors that two outer segment integral membrane proteins have separate transport pathways

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