Vitamin D-Dependent Calcium-Binding Protein in the Cerebellum:
A Marker of Purkinje Cell Development

Thomasset, M.; Rabie, A.; Parkes, Owen; Desplan, Claude; Hénin, Dominique; Cuisinier-Gleizes, P

doi:10.1159/000457220

Cited by 11 publications

(4 citation statements)

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“…To this end, we used polyclonal antisera directed against PKC-I, -11, and -111 with standard immunocytochemical techniques. As it is not always possible to identify cell type in a mixed culture based on morphological criteria alone, we also employed antisera directed against calbindin-D,,, (Thomasset et al, 1984), a marker shown to recognize Purkinje cells selectively in sections of adult rat cerebellum. (Fig.…”

Section: Resultsmentioning

confidence: 99%

An electrophysiological correlate of protein kinase C isozyme distribution in cultured cerebellar neurons

Linden

Smeyne

et al. 1992

J. Neurosci.

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Protein kinase C (PKC) is a family of at least seven closely related molecules (isozymes) that vary in terms of their requirements for activation and their distribution among cells of the brain. A striking example of this differential distribution is seen in the cerebellum, where Purkinje cells express PKC-I, an isozyme that is strongly activated by both phorbol ester (PE), and low doses of cis-unsaturated fatty acid (c-UFA), while granule cells predominantly express PKC-II, an isozyme that is strongly activated by PE but not c-UFA. Both Purkinje and granule cells have large, easily recorded voltage-gated K currents. These currents are attenuated by PKC activators in several other varieties of neuron. We hypothesized that the effects of these two PKC activators would be predicted by the distribution of the relevant PKC isozyme, and that the delayed outward rectifier current, IK, would be attenuated by both PE and c-UFA in Purkinje cells, but only by PE in granule cells. This hypothesis was confirmed in perforated-patch recordings. The attenuation produced by both activators could be blocked by application of a specific PKC inhibitor, RO-31-8220, and could not be mimicked by inert forms of PE or c-UFA. To our knowledge, this study represents the first report of an electrophysiological correlate of PKC isozyme distribution.

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Section: Resultsmentioning

confidence: 99%

An electrophysiological correlate of protein kinase C isozyme distribution in cultured cerebellar neurons

Linden

Smeyne

et al. 1992

J. Neurosci.

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“…Purkinje cells in vivo have been shown to express relatively high levels of calbindin D25K, a calcium binding protein, to such an extent that antibodies recognizing calbindin have been used to identify specifically this neuronal population (Jande et al, 1981;Legrand et al, 1983;Thomasset et al, 1984;Sequier et al, 1990). It has been reported previously that the isolation of cerebellar cells from younger embryos, E16, as opposed to E18 or E21 enhances the in vitro survival of Purkinje cells (Lhrkfors et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Responses of Purkinje Cells to Neurotrophin Treatment

Lärkfors

Lindsay

Alderson

1996

Journal of Neurochemistry

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The ability of the neurotrophins nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4/5 to promote neuronal survival and phenotypic differentiation was examined in dissociated cultures from embryonic day 16 rat cerebellum. BDNF treatment increased the survival of neuron-specific enolase-immunopositive cells by 250 and 400% after 8 and 10 days in culture, respectively. A subpopulation of these neurons, the Purkinje cells, identified by calbindin staining, was increased to an equivalent extent,~-~200%, following BDNF, NT-41 5, or NT-3 treatment. The number of GABAergic neurons, identified by GABA immunoreactivity, was greatly increased by treatment with BDNF (470%) and moderately by NT-4/5 (46%), whereas NT-3 was without effect. NGF failed to increase the number of either Purkinje cells or GABAergic neurons. Addition of BDNF within 48 h of cell plating was required to obtain a maximal increase in Purkinje cell number after 8 days. In contrast, the NT-3 responses were nearly equivalent even if treatment was delayed for 96 h after plating. BDNF, NT-415, and NT-3, but not NGF, induced the rapid expression of the immediate early gene c-fos. Immunocytochemical double-labeling with antibodies to c-fos and calbindin was used to identify Purkinje cells that responded to neurotrophin treatment by induction of c-fos. After 4 days in vitro, both BDNF and NT-3 induced the formation of c-fos protein in calbindin-immunopositive neurons, whereas NT-4/5 did not. The latter results suggest that although BDNF and NT-4/5 have been shown to act through a common receptor, TrkB, it appears that the effects of BDNF and NT-4/5 are not identical.

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“…The 28K CaBP appears very early in the cerebellum, at 14 wk, and seems to increase between 14 and 24 wk of gestation. Although the vitamin D-dependence of cerebellum 28K CaBP has not been yet demonstrated (4), the appearance of 28K CaBP in the rat cerebellum is related to the Purkinje cell differentiation and the developmental increase of this protein reflects the overall maturation of Purkinje cells (9,10). Such data suggest a possible role of the protein in the development of cerebellum.…”

Section: Resultsmentioning

confidence: 99%

“…Although their exact molecular functions remain unclear, 9K CaBP in the duodenum and the placenta as well as 28K CaBP in the kidney are probably involved in calcium transfer. 28K CaBP has been proposed as a marker of Purkinje cell differentiation and development of the cerebellum (10). Vitamin D-dependence of rat intestinal 9K CaBP gene expression was documented using either a cell free translation system (1 I) or a specific cDNA probe synthesized from rat mRNA coding for 9K CaBP (12).…”

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confidence: 99%

Vitamin D-Dependent Calcium-Binding Proteins (CaBPs) in Human Fetuses: Comparative Distribution of 9K CaBP mRNA and 28K CaBP during Development

et al. 1987

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ABSTRACT. The vitamin D-dependent calcium-binding protein (CaBP) cholecalcin or calbindin, has been used as a molecular marker of 1,25-dihydroxyvitamin D3 action. Mammals possess two CaBPs: a 9,000 mol wt (9K CaBP) and a 28,000 mol wt (28K CaBP). The distinct localization of each protein in the rat has been previously described with the aid of specific radioimmunoassays developed for each CaBP. Antibodies raised against the rat 28K CaBP can be used to detect this protein in a number of mammalian species including humans. In contrast, antibodies against rat 9K CaBP do not cross react with human 9K CaBP, but human 9K CaBP mRNA can be analyzed using a cDNA probe for rat 9K CaBP mRNA. Such a cross-hybridization between the rat cDNA probe and human CaBP mRNA was demonstrated by Northern analysis. We have documented the distribution and evolution of 28K CaBP and 9K CaBP mRNA in human tissues during fetal development from 14 to 32 wk of gestation. 28K CaBP was only present in kidney and cerebellum, and not detectable in duodenum. There was a 2-fold increase of 28K CaBP in the cerebellum between 14 and 24 wk of gestation. The 9K CaBP mRNA was unevenly distributed in human fetal tissues. 9K CaBP mRNA was present in classical vitamin D target tissues such as duodenum and placenta; high levels of 9K CaBP mRNA also were found in thymus and lung. These findings suggest a role for the hormone not only in the duodenum, placenta and kidney, but during the development of specific organs such as cerebellum, lung and thymus, and in agreement with many recent studies, point to a role of vitamin D in cellular differentiation and growth. (Pediatr Res 21: 362-367, 1987) Abbreviations 1,25(OH)2D3, 1,25-dihydroxyvitamin D3 CaBP, calcium-binding protein 9K CaBP, 9,000 molecular weight calcium-binding protein 28K CaBP, 28,000 molecular weight calcium-binding protein PGFa, prostaglandin DEPC, diethylpyrocarbonate SDS, sodium dodecyl sulfateThe vitamin D-dependent CaBP, cholecalcin (1) or calbindin, is one of a group of intracellular proteins that bind calcium with an affinity constant Ka = lo6 M-' (2, 3). These proteins are the best known molecular markers of vitamin D action on target cells and have been characterized for a number of species (3). Birds have only one CaBP of 28,000 molecular weight, while two CaBPs have been described in mammals (3, 4). A small 9K CaBP having two calcium-binding sites was first located in the absorptive cells of the duodenum (5) but is also found in the placenta (6, 7). A larger 28K CaBP, similar to the chick 28K CaBP (3), possesses four calcium-binding sites and is concentrated in the distal tubules of the kidney (8) and the Purkinje cells of cerebellum (9). Although their exact molecular functions remain unclear, 9K CaBP in the duodenum and the placenta as well as 28K CaBP in the kidney are probably involved in calcium transfer. 28K CaBP has been proposed as a marker of Purkinje cell differentiation and development of the cerebellum (10). Vitamin D-dependence of rat intestinal 9K CaBP gene expression ...

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Vitamin D-Dependent Calcium-Binding Protein in the Cerebellum: A Marker of Purkinje Cell Development

Cited by 11 publications

References 0 publications

An electrophysiological correlate of protein kinase C isozyme distribution in cultured cerebellar neurons

An electrophysiological correlate of protein kinase C isozyme distribution in cultured cerebellar neurons

Characterization of the Responses of Purkinje Cells to Neurotrophin Treatment

Vitamin D-Dependent Calcium-Binding Proteins (CaBPs) in Human Fetuses: Comparative Distribution of 9K CaBP mRNA and 28K CaBP during Development

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