Recoverin in pineal organs and retinae of various vertebrate species including man

Korf, Horst‐Werner; White, Benjamin H.; Schaad, Nicolas; Klein, David C.

doi:10.1016/0006-8993(92)91452-k

Cited by 73 publications

(47 citation statements)

References 21 publications

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“…Goldfish retina contains a type of double cone and four types of single cone that can be differentiated by morphology and photopigment content (i.e., Marc and Sperling, 1976;Raymond et al, 1993). Recoverin antibodies label cones in many vertebrates (Korf et al, 1992;McGinnis et al, 1997). We found, in goldfish as well, that cones were recoverin-immunoreactive, as illustrated for the pedicles in Figure 3B.…”

Section: Light Microscopymentioning

confidence: 73%

“…A polyclonal antibody raised in rabbits against the 23-kD calcium-binding protein recoverin (Lambrecht and Koch, 1991) was kindly provided by Dr. K.-W. Koch (Institut fü r Biologische Informationsverabeitung, Jü lich, Germany). This antibody is against purified recoverin isolated from bovine photoreceptors (Lambrecht and Koch, 1992) and labels photoreceptors in a variety of vertebrate species (Korf et al, 1992;McGinnis et al, 1997).…”

Section: Immunoreagentsmentioning

confidence: 99%

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Localization of the AMPA subunit GluR2 in the outer plexiform layer of goldfish retina

Klooster

Studholme

Yazulla

2001

J of Comparative Neurology

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L-glutamate, the photoreceptor neurotransmitter, depolarizes horizontal cells and OFF bipolar cells by ionotropic AMPA-glutamate receptors. The AMPA-receptor subunit (GluR4) is localized to dendrites of OFF bipolar cells in goldfish retina. Here, we used immunohistochemical techniques to identify AMPA-receptor subunits on horizontal cell dendrites. A monoclonal antibody against rat GluR2, with high sequence homology to the recently cloned goldfish GluR2a receptor, was used for light- and electron-microscopical immunocytochemistry. Light- and dark-adapted retinas were analyzed, with no major difference in results. GluR2-immunoreactivity (IR) was restricted to a narrow band in the outer plexiform layer, in which it appeared as bright dome-shaped structures amidst numerous puncta. At the ultrastructural level, GluR2-IR was found in horizontal cell dendrites that invaginated cones and rods. Dendrites of OFF bipolar cells were not labeled. GluR2-IR was present mostly in horizontal cell dendrites that were the lateral elements of the triad, rather than in dendrites that were the central elements. In light-adapted retinas, GluR2-IR was found in many horizontal cell spinules. GluR2-IR was observed, on occasion, in a mixed rod/cone (Mb) ON bipolar cell process that innervated rod spherules. Verification of the Mb ON bipolar cell was made by protein kinase C and metabotropic mGluR1alpha immunolabeling. The presence of GluR2-IR in lateral elements suggests that lateral horizontal cell dendrites are postsynaptic to cones rather than only sites of feedback inhibition. All horizontal cell types express the GluR2 subunit, uniquely differentiating themselves from OFF bipolar cells that express the GluR4 subunit. This differentiation most likely has a major influence on the glutamate pharmacology and response kinetics of these cell types to glutamate.

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Section: Light Microscopymentioning

confidence: 73%

Section: Immunoreagentsmentioning

confidence: 99%

Localization of the AMPA subunit GluR2 in the outer plexiform layer of goldfish retina

Klooster

Studholme

Yazulla

2001

J of Comparative Neurology

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“…It remains to be determined which changes of the immunostaining pattern take place during the circadian rhythmic changes of melatonin synthesis. Another calciumbinding protein which has recently been shown to occur in a variable number of pinealocytes is recoverin (Korf et al, 1992). The function of this protein in pinealocytes is not yet clear.…”

Section: Discussionmentioning

confidence: 99%

Differential immunocytochemical localization of calretinin in the pineal gland of three mammalian species

1996

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Calcium plays an important role for signal transduction in the mammalian pineal organ. The regulation of the intracellular concentration of free calcium probably involves calcium-binding proteins of the calmodulin superfamily. In the present study, we have investigated the expression of calretinin, one member of this superfamily, in the pineal organ of hamsters, gerbils and guinea-pigs by means of immunochemical and immunocytochemical analyses with a calretinin-specific antiserum. In immunoblots this antibody recognized a single protein band of approximately 29 kDa in the brain and pineal organ of all three mammalian species. Immunocytochemical investigations of serial semithin sections of plastic-embedded pineals revealed the constant occurrence of variable numbers of calretinin-positive cells throughout all glands. In order to identify the immunopositive cells precisely, adjacent sections were exposed to antibodies against various marker proteins of pineal cell types, i.e., synaptophysin, neuron-specific enolase, protein gene product 9.5, S-antigen, vimentin and S-100. By this approach, calretinin could be localized to vimentin-positive cells in the gerbil which are generally considered as interstitial glial cells. Likewise, calretinin-positive cells in the guinea-pig probably correspond to interstitial cells, taking into account their morphology and the lack of calretinin immunoreactivity in pinealocytes. The unusual expression of calretinin in astrocyte-like cells further supports the notion that pineal glial cells are endowed with peculiar properties. In contrast to gerbil and guinea-pig, a subpopulation of pinealocytes displayed calretinin immunoreactivity in the hamster. This finding adds to the hypothesis that in pinealocytes of some species calretinin plays a role in calcium-mediated signal transduction which eventually is linked to melatonin synthesis. Our results demonstrate that calretinin is a regular constituent of pineal glands in three mammalian species, but that its cellular localisation shows interspecific variation. This variation suggests that the protein is involved in diverse calcium-mediated functions in the mammalian pineal gland.

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“…Among the Ca ϩϩ -binding proteins whose presence has been shown by immunohistochemistry in various retinal cells (ganglion and amacrine but, specifically, neither photoreceptor nor Müller cells) are CaM (Seto-Ohshima et al 1987;Pochet et al 1991), calbindin D-28k (Uesugi et al 1992), parvalbumin (Endo et al 1985), calretinin (Bastianelli et al 1995), and neurocalcin (Nakano et al 1992). Another Ca ϩϩ -binding protein, recoverin, is exceptional because it is located mainly in photoreceptor and bipolar cells (Korf et al 1992;Günhan-Agar et al 2000). The location of most Ca ϩϩ -binding proteins in ganglion cells and amacrine cells, which coincides with our localization of calcineurin, may indicate that ganglion cells and amacrine cells, but not Müller cells, are the main site of the function of calcium-binding activity in the retina.…”

Section: Discussionmentioning

confidence: 99%

Localization of Calcineurin in the Mature and Developing Retina

Nakazawa

Usuda²,

Matsui³

et al. 2001

J Histochem Cytochem.

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S U M M A R YWe studied the localization of calcineurin by immunoblotting analysis and immunohistochemistry as a first step in clarifying the role of calcineurin in the retina. Rat, bovine, and human retinal tissues were examined with subtype-nonspecific and subtypespecific antibodies for the A ␣ and A ␤ isoforms of its catalytic subunit. In mature retinas of the three species, calcineurin was localized mainly in the cell bodies of ganglion cells and the cells in the inner nuclear layer, in which amacrine cells were distinctively positive. The calcineurin A ␣ and A ␤ isoforms were differentially localized in the nucleus and the cytoplasm of the ganglion cell, respectively. Calcineurin was also present in developing rat retinas, in which the ganglion cells were consistently positive for it. The presence of calcineurin across mammalian species and regardless of age shown in the present study may reflect its importance in visual function and retinal development, although its function in the retina has not yet been clarified.

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Recoverin in pineal organs and retinae of various vertebrate species including man

Cited by 73 publications

References 21 publications

Localization of the AMPA subunit GluR2 in the outer plexiform layer of goldfish retina

Localization of the AMPA subunit GluR2 in the outer plexiform layer of goldfish retina

Differential immunocytochemical localization of calretinin in the pineal gland of three mammalian species

Localization of Calcineurin in the Mature and Developing Retina

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