Topographic specializations of catecholaminergic cells and ganglion cells and distribution of calcium binding proteins in the crepuscular rock cavy ( Kerodon rupestris ) retina

AbstractCalbindin-D28K and calretinin are homologous calcium-binding proteins localized in many neurons of the central nervous system. We have compared polyclonal antibodies against calbindin and calretinin and have shown by western blots using purified calbindin and calretinin from rat that (1) anti-calretinin does not recognize calbindin and (2) anti-calbindin presents some cross-reactivity with calretinin.In this report, we have compared by immunohistochemistry the localization of both calcium-binding proteins in the retina of monkey, pig, sheep, rat, cat, pigeon, and salamander. These results are compared with previous data for chick. There are many differences between species and not within species, but some aspects of the distribution are conserved. All species, except rat and monkey, have some cones which contain calbindin only. Most species also have some bipolar cells containing calbindin only. Calretinin is rarely seen in photoreċeptors or bipolar cells. All species have horizontal cells which contain calretinin or calbindin or both. All species have amacrine cells and ganglion cells containing one or other protein.In the cat ganglion cell layer, the calretinin antisera define a new, asymmetric, type of cell.

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Differential co-localization of nicotinic acetylcholine receptor subunits with calcium-binding proteins in retinal ganglion cells

Brain Research ◽

10.1016/s0006-8993(97)81715-5 ◽

1997 ◽

Vol 774 (1-2) ◽

pp. 250-255 ◽

Cited By ~ 10

Author(s):

Claudia M Araki ◽

Raquel S Pires ◽

Luiz R.G Britto ◽

Jon M Lindstrom ◽

Harvey J Karten ◽

...

Keyword(s):

Acetylcholine Receptor ◽

Retinal Ganglion Cells ◽

Nicotinic Acetylcholine Receptor ◽

Calcium Binding ◽

Binding Proteins ◽

Ganglion Cells ◽

Calcium Binding Proteins ◽

Retinal Ganglion ◽

Nicotinic Acetylcholine

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Calretinin in the cat retina: Colocalizations with other calcium-binding proteins, GABA and glycine

Visual Neuroscience ◽

10.1017/s0952523800011445 ◽

1997 ◽

Vol 14 (2) ◽

pp. 311-322 ◽

Cited By ~ 42

Author(s):

Dennis J. Goebel ◽

Roberta G. Pourcho

Keyword(s):

Calcium Binding ◽

Binding Proteins ◽

Ganglion Cells ◽

Amacrine Cells ◽

Photoreceptor Cells ◽

Calcium Binding Proteins ◽

Horizontal Cells ◽

Cone Photoreceptors ◽

Cat Retina ◽

Double Label

AbstractImmunocytochemical techniques were used to determine the distribution of the calcium-binding protein calretinin in the cat retina. Comparisons were made with parvalbumin and calbindin as well as with the inhibitory neurotransmitters GABA and glycine. Calretinin immunoreactivity was seen in horizontal cells and multiple subpopulations of amacrine and ganglion cells. Cone outer segments were also stained. Calbindin immunoreactivity was present in cone photoreceptors, horizontal cells, at least two subtypes of cone bipolar cell, numerous amacrine cells, and cells residing in the ganglion cell layer. Heavy staining for parvalbumin was found in both A- and B-type horizontal cells, distinct subpopulations of amacrine and ganglion cells, and a small population of cone photoreceptor cells. To confirm the identity of cone photoreceptors, comparisons were made with retinas stained for opsins specific for red/green or blue cones (Szé1 et al., 1986). The localization of parvalbumin corresponded with that of blue-type cones only whereas calretinin and calbindin staining showed the same distribution as both red/green and blue cones. Double-label immunofluorescence studies revealed colocalization of all three of the calcium-binding proteins in a number of neurons including horizontal cells and AII amacrine cells. To assess a possible transmitter-specific relationship for calretinin, double-label studies were carried out with GABA and glycine. However, the staining patterns for each of these inhibitory amino acids differed substantially from that of calretinin. The possibility remains that calretinin and other calcium-binding proteins may play a role in neurotransmission through interactions with receptors or second-messenger agents.

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