Visinin: A novel calcium binding protein expressed in retinal cone cells

Yamagata, Kanato; Goto, Kaoru; Kuo, Che‐Hui; Kondo, Hisatake; Miki, Naomasa

doi:10.1016/0896-6273(90)90059-o

Cited by 218 publications

(95 citation statements)

References 27 publications

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“…Since CAR antisera label both rods and cones, it appears likely that 1 ~6 and visinin are the respective antigens, although p26 may be present in both types of photoreceptors and is the sole antigen. Although two other calcium-binding proteins, calretinin and calbindin, are present in cones but not rods and may bind CAR autoantibodies, they share little homology with visinin or p:6 (Rogers, 1987;Yamagata et al, 1990). Nonetheless, the definitive identification of the cone antigen awaits the purification of these calcium binding proteins in order to determine which ones, in addition to 1 ~6, bind CAR autoantibodies.…”

Section: Discussionmentioning

confidence: 99%

“…Both visinin and the rod protein, p26, contain within their sequences the proper motifs for the binding of calcium. Concurrent investigations in several laboratories are examining the role which these calcium binding proteins might play in phototransduction, perhaps by regulating guanylate cyclase activity (Hurley, 1990;Koch, 1990;Yamagata et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

“…The two proteins share •60% identical amino acids in the 157 residues that have been sequenced in p26 and almost 90% homology if considering conservative replacements (Dayhoff et al, 1969). Three regions within the visinin sequence are clearly homologous with calmodulin and troponin C (Yamagata et al, 1990) and represent calcium binding domains of the E-F hand structure. Corresponding regions within the p~ sequence revealed ,,090% homology to visinin.…”

Section: R E S U L T Smentioning

confidence: 99%

“…An aliquot of the soluble extract was separated by SDS-PAGE, and the protein staining pattern is shown in lane A. Protein which did not bind to the column is shown in lane B, whereas bound material which could be eluted with EDTA is stained in lane ( amino acid sequence of p:6 and the homology it shares with a cone photoreceptor-specific protein, visinin (Yamagata et al, 1990). The two proteins share •60% identical amino acids in the 157 residues that have been sequenced in p26 and almost 90% homology if considering conservative replacements (Dayhoff et al, 1969).…”

Section: R E S U L T Smentioning

confidence: 99%

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A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy.

Polans

Buczyłko

Crabb

et al. 1991

The Journal of Cell Biology

251

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Abstract. Cancer-associated retinopathy (CAR), a paraneoplastic syndrome, is characterized by the degeneration of retinal photoreceptors under conditions where the tumor and its metastases have not invaded the eye. The retinopathy often is apparent before the diagnosis of cancer and may be associated with autoantibodies that react with specific sites in the retina. We have examined the sera from patients with CAR to further characterize the retinal antigen. Western blot analysis of human retinal proteins reveals a prominent band at 26 kD that is labeled by the CAR antisera. Antibodies to the 26-kD protein were affinity-purified from complex CAR antisera and used for EMimmunocytochemical localization of the protein to the nuclei, inner and outer segments of both rod and cone cells. Other antibodies obtained from the CAR sera did not label photoreceptors. Using the affinitypurified antibodies for detection, the 26-kD protein, designated p26, was purified to homogeneity from the outer segments of bovine rod photoreceptor cells by Phenyl-Sepharose and ion exchange chromatography. Partial amino acid sequence of p26 was determined by gas phase Edman degradation and revealed extensive homology with a cone-specific protein, visinin. Based upon structural relatedness, both the p26 rod protein and visinin are members of the calmodulin family and contain calcium binding domains of the E-F hand structure.variety of neurodegenerative diseases are known to be associated with different types of cancer, even though the tumor and its metastases have not invaded the nervous system (Brain and Norris, 1965;Brain and Wilkinson, 1965;

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: R E S U L T Smentioning

confidence: 99%

Section: R E S U L T Smentioning

confidence: 99%

See 2 more Smart Citations

A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy.

Polans

Buczyłko

Crabb

et al. 1991

The Journal of Cell Biology

251

View full text Add to dashboard Cite

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“…Visinin is the avian homologue of mammalian recoverin and is expressed by all types of photoreceptors in the chick retina (Yamagata et al, 1990). Calretinin is normally expressed by most if not all horizontal and ganglion cells and many types of amacrine cells in the chick retina (Ellis et al, 1991;Fischer et al, 1999).…”

Section: Resultsmentioning

confidence: 99%

NeuroD induces the expression of visinin and calretinin by proliferating cells derived from toxin‐damaged chicken retina

Fischer

Wang

Reh

2004

Developmental Dynamics

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Retinoid X receptor ? gene transcripts are expressed by a subset of early generated retinal cells and eventually restricted to photoreceptors

Hoover

Seleiro²,

Kielland

et al. 1998

J. Comp. Neurol.

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We have examined the distribution of the retinoid X receptor gamma (RXRgamma) in the developing chicken retina by using in situ hybridization and RNase protection assays. We detected RXRgamma transcripts as early as 4 days of embryonic development (d4) in central regions of the retina, spreading to more peripheral regions by d8. The first few RXRgamma-positive cells were scattered within the depth of the retinal neuroepithelium, but as they increased in number they became localized predominantly to the apical (outer, ventricular) layer. The identity of the RXRgamma-positive cells at these stages is unknown, due to the lack of cell type-specific markers. By d10, when photoreceptors and ganglion cells have been generated and begun to establish their definitive layers, RXRgamma-positive cells were virtually restricted to the photoreceptor layer, and maintained this distribution to posthatch stages. RNase protection assays were performed on whole retinae to verify the temporal pattern of in situ hybridization results and showed that between d5 and d16 there was a significant increase in the mRNA levels of the RXRgamma2 isoform. Between d16 and early posthatch stages the level of RXRgamma2 mRNA did not change significantly. Consistent with previous studies, mRNA levels of the RXRgamma1 isoform were substantially lower than mRNA levels of the RXRgamma2 isoform at all time points examined. These results demonstrate that RXRgamma mRNA is expressed in photoreceptors in the developing chicken retina and implicate RXRgamma as the earliest marker of photoreceptor differentiation documented to date.

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Visinin: A novel calcium binding protein expressed in retinal cone cells

Cited by 218 publications

References 27 publications

A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy.

A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy.

NeuroD induces the expression of visinin and calretinin by proliferating cells derived from toxin‐damaged chicken retina

Retinoid X receptor ? gene transcripts are expressed by a subset of early generated retinal cells and eventually restricted to photoreceptors

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