Immunohistochemical localization of calbindin‐D28K and calretinin in the lamprey retina

Abstract

Calbindin-D28K and calretinin are homologous cytosolic calcium binding proteins localized in many retinal neurons from different species. In this report, location of cells immunoreactive to both proteins was investigated in the retina of the lamprey, Lampetra fluviatilis. This organism constitutes one of the older representative vertebrates and possesses a peculiar organization, probably unique: two-thirds of the ganglion cells are in the classical amacrine cell layer and the nerve fiber layer is located in the scleral part of the inner plexiform layer. Calbindin-like immunoreactivity was demonstrated in large bipolar cells and in cell bodies located in the inner retina. Although the distinction between labelled ganglion cells and labelled amacrine cells was rendered difficult, we hypothesized that the majority of calbindin-immunoreactive cells observed in the inner retina are ganglion cells, because of the high number of labelled fibers in the nerve fiber layer. Calretinin-like immunoreactivity was detected in both large and small bipolar cells, and also in cells located in the inner retina. Since few calretinin-immunoreactive fibers were observed in the nerve fiber layer, we assume that the latter category of cells are amacrine cells. Horizontal cells were both negative for calbindin and calretin-like immunoreactivities. Calbindin and calretinin, which are present in cones from many species, could not be detected in the photoreceptor layer favouring the rod-dominated lamprey retina. Although their distribution differs from those observed in most vertebrates, the present results indicate the good conservation of both calcium binding proteins in the retina during the vertebrate evolution.

Calbindin and calretinin immunoreactivities identify different types of neurons in the adult lamprey spinal cord

“…The presence of these proteins has been demonstrated previously in the lamprey retina (Dalil-Thiney et al, 1994). These authors have also reported the coexistence of CB and CR in particular cell types such as large bipolar cells.…”

Calbindin and calretinin immunoreactivities in the retina of a chondrostean, Acipenser baeri

“…The CB distribution in sturgeon retina markedly differs from that reported immunocytochemically in adult lamprey (Dalil-Thiney et al 1994) and teleosts (goldfish: Pochet et al 1991;trout: Vecino et al 1993). In these fishes, CB immunoreactivity has been observed in bipolar, amacrine, and ganglion cells, whereas only a single type of bipolar cell is CB-ir in sturgeon.…”

“…Our results in a primitive bony fish suggest that the lack of CB observed in some teleosts (Hamano et al 1990;Friedman and Kawasaki 1997;Manso et al 1997; Díaz-Regueira and Anadón 2000) is secondary. The immunohistochemical demonstration of CR and CB in the lamprey retina (Dalil-Thiney et al 1994) supports the idea that primitive vertebrates have both proteins.…”

“…In the retina, CB and CR immunohistochemistry has been used for the characterization of various neuronal populations. In fishes, the presence of CB and/or CR immunoreactivity in retinal cells has been studied in a jawless fish (Dalil-Thiney et al 1994) and a few teleosts (modern bony fishes; Hamano et al 1990;Pochet et al 1991;Vecino et al 1993;Doldán et al 1999). To our knowledge, no data are available concerning the presence and distribution of these calcium-binding proteins in the nervous system of sturgeons, which are representatives of the most ancient living bony fishes, the chondrosteans.…”

Comparative immunolocalization of the plasma membrane calcium pump and calbindin D28K in chicken retina during embryonic development

“…The exact cellular location of these proteins varies among species and among specific cell types. Identified within one or more of these cells are calmodulin (Pochet et al, 1991), calbindin (Schreiner et al, 1985;Pochet et al, 1991;Pasteels et al, 1987;Veccino et al, 1993;Papzafiri et al, 1995;Yan, 1997;Haley et al, 1995;Dalil-Thiney et al, 1994), calretinin (Rogers, 1989;Pasteels et al, 1990;Papzafiri et al, 1995;Völgyi et al, 1997), parvalbumin (Uesugi et al, 1992;Yan, 1997), hippocalcin (Bastianelli et al, 1995) and caldendrin (Menger et al, 1999). The function of many of these proteins, except the ubiquitous calmodulin, is the subject of speculation and, in certain cases, controversial.…”