Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Calbindins”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 739 records · Page 41Linked to original sources
PubMed2004

Static, transient and permanent organization of GABA receptor expression in calbindin-positive interneurons in response to amygdala kindled seizures.

We tested the hypothesis that experimentally produced epilepsy (by kindling) may induce changes in GABAA receptor expression in some but not all interneuron populations. Using laser capture microdissection and quantitative polymerase chain reaction (QPCR) analysis, GABAA receptor alpha subunit expression in calbindin- (CBir) and parvalbumin- (Parvir) immunoreactive interneurons was compared between normal brains and brains in which amygdala kindled seizure responses were permanently established. Two weeks after the last seizure response, Cbir neurons in the hilus and/or perirhinal cortex up-regulated the expression of alpha2, alpha3 and alpha5 subunit mRNAs up to 900%. In contrast, no changes were found in Parvir neurons. In Cbir neurons contralateral to the amygdala kindling site alpha1 subunit mRNA expression was increased. In both Cbir and Parvir neurons, the coordinated subunit expression patterns ipsilateral (fully kindled) and contralateral (partially kindled) to the kindling site suggested that permanent and transient co-expressional relationships occur respectively. In the perirhinal cortex alpha2 protein was up-regulated in the processes but not in the cell somas of calbindin-positive neurons, whereas alpha3 subunit protein expression was up-regulated on the cell bodies of Cbir neurons in the hilus. These data indicate that different interneuron populations may selectively reorganize their GABAA subunit expression in response to seizures.

Amygdala↗
PubMed1990

Elevated 1,25-dihydroxyvitamin D3 and intestinal calbindin-D9k in the toothless rat.

The toothless (tl) rat is a nonlethal osteopetrotic mutation characterized by systemic skeletal sclerosis, growth plate morphology suggestive of rickets, and morphological evidence of reduced osteoclastic bone resorption. Vitamin D metabolites, serum calcium and phosphorus levels, and the developmental appearance of vitamin D-dependent intestinal calcium binding protein (calbindin-D9k) was studied in normal and mutant rats of tl stock from 7 to 35 days of age. 1,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] was found to be significantly elevated in mutant animals by 7 days of age (71 +/- 9 pM, tl/tl vs. 24 +/- 8 pM, +/?) and continued to increase to a peak of 428 pM at the time of weaning. This was 240% higher than normals at this period. The elevated levels of 1,25-(OH)2D3 stimulated a significant and precocious appearance of intestinal calbindin-D9k in mutants, beginning by 14 days of age and reaching their peak levels at 21 days postpartum (25.6 +/- 1.7 micrograms/mg protein, tl/tl vs. 16.4 +/- 1.5 micrograms/mg protein, +/?). The cause of the elevated circulating levels of 1,25-(OH)2D3 in tl rats is unknown but may be due to the low serum phosphorus levels present in these animals.

Aging↗
PubMed1989

The human genes for calbindin 27 and 29 kDa proteins are located on chromosomes 8 and 16, respectively.

Genomic clones coding for the brain calcium-binding protein, calbindin 29 kDa, were isolated from a human library. A fragment containing exon 2 was used as a probe to investigate the presence of the gene in human x rodent somatic cell hybrids. The gene was unambiguously assigned to chromosome 16. The closely-related calbindin 27 kDa gene was previously assigned to chromosome 8. These two genes, deriving from a common ancestor, thus appear to have been separated during vertebrate evolution.

Animals↗
PubMed1998

Immunocytochemical and In situ hybridization studies of the distribution of calbindin D9k in the bovine placenta throughout pregnancy.

The fetus must transport considerable and increasing amounts of calcium across the placental trophoblast epithelium to support growth and development and bone formation. Active calcium transport across epithelia has been shown to correlate with calbindin D9k or 28k content. This study examined the distribution of calbindin D9k (9CBP) protein and mRNA during pregnancy in the bovine placenta to determine its possible role in calcium transport in this system. The immunocytochemical results show 9CBP in an increasing percentage of interplacentomal uninucleate trophoblast cells until, at term, all show a level at least eight times that of any other placental cell. There is a similar, although smaller, rise in their 9CBP mRNA content. The mature interplacentomal binucleate cell ( approximately 5% of the total) contains no 9CBP at any stage of pregnancy. In interplacentomal uterine epithelium, 9CBP protein and mRNA decrease to zero in late pregnancy but the glands maintain constant low levels throughout. In the placentome trophoblast, uninucleate cells show insignificant amounts but binucleate cells (15-20% of the total trophoblast cells) contain considerable levels of both 9CBP protein and mRNA, as do all the uninucleate uterine epithelial cells. The placentomal binucleate cells show peak values at mid-pregnancy; the placentomal uterine epithelium shows only small changes in levels in the second half of pregnancy. Increase in fetal calcium demand in the second half of pregnancy therefore correlates with a major increase in 9CBP only in the interplacentomal trophoblast, as we have also shown in the sheep and goat, indicating an important role for this region in active calcium transport by the ruminant placenta. The 9CBP is distributed uniformly in the cytosol and nucleoplasm, supporting a role in facilitated diffusion of calcium through the cell rather than a vesicular shuttle system.

Animals↗
PubMed1988

Elevated levels of vitamin D-dependent calcium-binding protein (calbindin-D9k) in the osteosclerotic (oc) mouse.

The osteosclerotic (oc) mouse is an osteopetrotic mutation that has recently been identified as having rickets associated with its osteopetrosis. The presence of this rachitic lesion, unexplainable from a nutritional standpoint, prompted an investigation into the vitamin D endocrine system in these animals. The developmental appearance of vitamin D-dependent calcium-binding protein (calbindin-D9k) and alkaline phosphatase was studied in oc mutant and normal mice from birth to weaning, as were serum concentrations of 25-hydroxyvitamin D3 (25OHD3), 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3], calcium, and phosphorus. Intestinal and renal calbindin-D9k levels were markedly and precociously elevated (4- to 9-fold) in young suckling, but not newborn, mutant mice compared to values in normal controls. Serum 25OHD3 levels were very low to undetectable in 2-week-old mutant mice compared to normal values, while 1,25-(OH)2D3 levels were 6 times higher in mutants. The exact cause of this premature induction in mutants is unknown, but may be due to elevated circulating levels of 1,25-(OH)2D. Alkaline phosphatase activity was similar between phenotypes at all ages. These studies indicate that the rachitic lesion present in oc mutants may be the result of some inherited disorder in vitamin D metabolism in these animals. Alternatively, these data are also consistent with a normal appropriate response to hypocalcemia and hypophosphatemia resulting from decreased osteoclastic bone resorption.

Aging↗
PubMed1995

1 alpha,25(OH)2-vitamin D3 analog structure-function assessment of intestinal nuclear receptor occupancy with induction of calbindin-D28K.

1 alpha,25-dihydroxyvitamin D3 [1 alpha,25(OH)2D3] has been shown to generate biological responses via both genomic and nongenomic pathways. In previous studies concerning the mechanism of 1 alpha,25(OH)2D3-stimulated rapid intestinal transport of Ca2+, a process termed transcaltachia, we assessed the ability of seven analogs of 1 alpha,25(OH)2D3 to initiate transcaltachia in the vitamin D-replete chick and bind in vitro to the classical nuclear chick intestinal receptor for 1 alpha,25(OH)2D3 (VDR). Two groups of analogs were found, one able to stimulate transcaltachia and the other able to bind to the VDR. In the present study, we have examined both the genomic effect of these analogs in the intestine of vitamin D-deficient chicks and their in vitro binding to vitamin D binding protein. It was found that analogs known to bind effectively to the nuclear receptor in vitro could achieve a significant occupancy of the VDR in vivo and stimulated calbindin-D28K messenger RNA and protein synthesis. In contrast, those analogs that were good agonists of transcaltachia were ineffective either in occupying the VDR in vitro or in stimulating in vivo calbindin-D28K messenger RNA and protein synthesis. These differences are consistent with our hypothesis that there may be two receptors for 1,25-(OH)2D3 with differing ligand binding domains, one being the classical nuclear VDR and the second a membrane receptor associated with transcaltachia.

Animals↗
PubMed2000

The spatial relationship between the perineuronal proteoglycan network and the synaptic boutons as visualized by double staining with cationic colloidal iron method and anti-calbindin-D-28K immunohistochemistry in rat cerebellar nuclei.

The present study demonstrated the precise spatial relationship between meshes in the perineuronal proteoglycan network and the terminal boutons of synaptically associated axons. Sections from the rat cerebellum were stained with cationic colloidal iron (pH 1.0-1.5), and successively immunostained with anti-calbindin-D-28K monoclonal antibody. Cationic iron stained sulfated proteoglycans around the nerve cell of the medial cerebellar nucleus, whereas the anti-calbindin antibody labeled the Purkinje cells including their axons terminating on large neurons in the cerebellar nucleus. It was found that each synaptic bouton fits into a mesh of the perineuronal network. The individual meshes appeared to be divided by partitions faintly stained with the colloidal iron. Electron microscopy of cationic colloidal iron-stained ultrathin sections revealed that the synaptic boutons were separated from each other by the proteoglycan matrix and that each of them was further divided into two or more contact areas of presynaptic membrane by the same matrix. This suggests that individual synapses are protected against the effects of adjacent synaptic transmission, and that each of them may be subdivided by this manner of partitioning, like pads of a cat's paw.

Animals↗
PubMed1987

Immunohistochemical identification of neuron-specific enolase and calbindin in the vestibular receptors of human fetuses.

Immunohistochemical techniques were used to identify neuron-specific enolase (NSE) and calbindin in the vestibular receptors and ganglia of human fetuses at 10 weeks of gestation. NSE was found in vestibular ganglion cells and in a few sensory cells. The pattern of immunoreactivity in the sensory epithelia was characteristic of the appearance of NSE in these structures. Calbindin was found in vestibular ganglion cells and sensory cells which displayed a strong immunoreactivity. These findings are discussed with regard to synaptogenesis and they indicate that the vestibular receptors show biochemical signs of maturation consistent with the possibility of synaptic activity.

Calbindins↗
PubMed1992

Parvalbumin and calbindin immunoreactivity in the rat brain: a double-immunolabelling method.

Parvalbumin and calbindin, two calcium binding proteins in the nervous system, are present in certain neuronal subpopulations. In the present study a method for a simultaneous demonstration of the both antigens was developed, which labels parvalbumin- and calbindin-containing structures in contrasting colours. A horseradish peroxidase-conjugated second antibody was used for the visualization of the monoclonal anticalbindin antibody, whereas the biotinylated anti-parvalbumin antibody was demonstrated by means of a biotin-streptavidine-alkaline phosphatase system. The method may be useful to classify neuronal populations and to study their morphological relationship.

Animals↗
PubMed1991

A unique neuronal organization in the cat pretectum revealed by antibodies to the calcium-binding protein calbindin-D 28K.

The pretectum is an important center for visual reflexes. However, the location, boundaries, and connections of individual nuclei of the pretectum are incompletely understood. In cat, the traditionally defined nuclear boundaries have been placed in doubt by recent evidence showing that the retinal input to the pretectum forms four continuous projection zones that do not match the cytoarchitectural boundaries of individual pretectal nuclei defined by previous studies. We now show that antibodies to the calcium-binding protein calbindin-D 28K (CaBP) label clusters of neurons within the pretectum that match the zones of retinal termination. Four obvious cell clusters within the pretectum were labeled by CaBP antisera. Computer three-dimensional reconstruction of these cell clusters revealed that they form four distinct but continuous zones that run the rostrocaudal length of the pretectum in a medial-to-lateral direction. By combining anterograde HRP labeling of retinal terminals with CaBP immunocytochemistry, these CaBP-labeled cell clusters were found virtually to overlap the retinal projection zones. The CaBP-labeled neurons included both multipolar and fusiform morphologies, and most were medium- to large-sized cells. HRP retrograde transport studies showed that many CaBP-labeled neurons in the clusters projected to the LGN, while none projected to the inferior olive (IO). GABA-immunoreactive neurons were also found within the CaBP cell clusters, but these neurons were smaller than most CaBP-labeled neurons, and none were retrogradely labeled following HRP injections into the LGN or IO. Two-color antibody double-labeling experiments did not reveal any GABA neurons within the clusters that colocalized CaBP. In summary, calbindin is a precise marker of neuron clusters that overlap the retinal projection zones in the cat pretectum. Many of these CaBP neurons project to the LGN, and none contain GABA.

Animals↗
PubMed1990

Immunohistochemical localization of calbindin-D28K in the brain of a cartilaginous fish, the dogfish (Scyliorhinus canicula L.).

The occurrence and distribution of the vitamin-D-induced calcium-binding protein, calbindin-D28K, has been studied in the brain of a cartilaginous fish using immunohistochemical techniques. A strong immunoreactivity was found in the perikarya, dendrites and axons of neurons located in the nucleus interstitialis commissurae anterioris, the nucleus medialis of the left habenula, the thalamus dorsalis, the thalamus ventralis, the nucleus lobi lateralis, the nucleus interpeduncularis, the lobus vagi and the medial reticular zone. Fibre tracts associated with some of these neuronal groups, such as the fasciculus retroflexus, the stria medullaris and the commissura habenulae, also contained immunopositive fibres. Only a minor immunoreactivity could be detected in other brain areas such as the tectum mesencephali and some telencephalic zones. Interestingly, the cerebellum did not show any immunoreactivity in Purkinje cells nor in other neurons. The distribution of calbindin-D28K in the dogfish brain appears to be mainly related to the viscerosensory centres.

Animals↗
PubMed1989

Calbindins D-9kDa and -28kDa and enamel secretion in vitamin D-deficient and control rats.

The present study focuses on the ultrastructure of enamel organ cells and the immunolocalization of calbindins D-9kDa and -28kDa during enamel secretion in Vitamin D-deficient rats. Vitamin D-deficiency disturbed the deposition of the layer of inner enamel and depleted the calbindins-content of ameloblasts. These data raise the possibility of a direct action of Vitamin D on the physiology of ameloblasts through ionic calcium homeostasis.

Ameloblasts↗
PubMed1994

Distribution of calbindin D-28k-immunoreactivity in the cat brainstem.

We studied the distribution of calbindin-immunoreactive fibers and cell bodies in the cat brainstem. The densest clusters of immunoreactive perikarya were found in the inferior and superior colliculi, the inferior olive, the periaqueductal gray, the central tegmental field and the substantia nigra, whereas the central linear nucleus, the locus coeruleus, the nucleus incertus, the dorsal and ventral nuclei of the lateral lemniscus, the cuneiform nucleus, the pontine gray, the Kölliker-Fuse nucleus, the dorsal motor nucleus of the vagus and the medial nucleus of the solitary tract had the lowest density. In the lateral tegmental field, the marginal nucleus of the brachium conjunctivum, the superior central nucleus, the nucleus sagulum, the dorsal nucleus of the raphe, the interpeduncular nucleus and the retrorubral nucleus the density of immunoreactive cell bodies was moderate. A high density of immunoreactive fibers was observed in the substantia nigra, the nucleus ruber, the superior and inferior colliculi, the periaqueductal gray, the interpeduncular nucleus, the central, magnocellular and lateral tegmental fields, the marginal nucleus of the brachium conjunctivum, the postpyramidal nucleus of the raphe, the inferior olive, the internal division of the lateral reticular nucleus and the medial and lateral nuclei of the superior olive. A moderate density of calbindin-immunoreactive fibers was found in the retrorubral nucleus, the central linear nucleus, the locus coeruleus, the nucleus sagulum, the dorsal nucleus of the raphe, the cuneiform nucleus, the ventral and dorsal nuclei of the lateral lemniscus, the medial nucleus of the solitary tract, the dorsal motor nucleus of the vagus, and the cuneate nucleus. Other brainstem regions such as the area postrema, the external division of the lateral reticular nucleus, the nucleus ambiguus, the nucleus intercalatus, the nucleus incertus, the pyramidal tract and the trapezoid body had the lowest density of immunoreactive fibers.

Animals↗
PubMed1995

Calbindin D-28K-immunoreactivity in the cat diencephalon: an immunocytochemical study.

The distribution of calbindin D-28k-immunoreactive fibers and cell bodies in the cat diencephalon has been analyzed by using the avidin-biotin immunoperoxidase technique. The thalamus showed a higher density of immunoreactive cell bodies than the hypothalamus. A high density of both immunoreactive perikarya and fibers was observed in the nuclei pulvinar, geniculatum mediale and laterale, lateralis posterior and dorsalis, habenularis lateralis and medialis, posterior, subparafascicularis, submedius, centralis medialis, medialis dorsalis, ventralis postero-medialis and postero-lateralis, reticularis, centralis lateralis, rhomboidens, paracentralis, ventralis lateralis, anterior and medialis, reuniens, anterior ventralis and medialis, hypothalamus posterior, corpus mamillare, area hypothalamica dorsalis and in the hypothalami ventromedialis. Moreover, a high density of fibers containing calbindin and a moderate/low density of immunoreactive cell bodies was found in the nuclei periventricularis anterior, parataenialis, hypothalamus lateralis, mamillaris lateralis, filiformis, periventricularis hypothalami, hypothalamus anterior and in the suprachiasmaticus.

Animals↗
PubMed1998

McAB 300 antibody against calbindin D-28K is a glial marker in the teleost brain.

The monoclonal antibody McAB 300 against calbindin D-28 k demonstrated an immunostaining pattern in the teleost brain completely different to those obtained in other classes of vertebrates, or after using in the teleost brain other monoclonal and polyclonal antibodies raised against the same protein. Although calbindin D-28k is considered a neuronal marker, McAB 300 specifically stained glial cells throughout the brains of teleosts, with the only exception of some retinal amacrine and horizontal cells.

Animals↗
PubMed1998

Phenotypic characterization of septal neurons in culture: immunohistochemistry of GABA, calbindin D-28k and choline acetyltransferase, and histochemistry of acetylcholinesterase.

Phenotypes of septal neurons, dissociated from 19-day-old fetal rat brains and then cultured in a medium containing nerve growth factor for 4 weeks, were examined using gamma-aminobutyric acid (GABA), calbindin D-28k, parvalbumin and choline acetyltransferase immunohistochemistry, and acetylcholinesterase histochemistry. There were primarily four groups of neurons identified in this septal culture: the first group (12.7% of 212 neurons examined) displayed a cholinergic, but not GABAergic, phenotype and had an average diameter of 13.6 +/- 2.7 microm (mean +/- S.D.); the second group (31.6%) displayed both cholinergic and GABAergic phenotypes and had a diameter of 12.2 +/- 2.8 microm; the third group (31.0%) displayed only a GABAergic phenotype and had a diameter of 10.4 +/- 2.3 microm; and the fourth group (24.7%) displayed neither a GABAergic nor cholinergic phenotype and had a diameter of 10.4 +/- 2.1 microm. Neurons in the first two groups described were significantly larger than those in the second two groups; neurons in the third and fourth groups were the same size. Calbindin D-28k was expressed in some neurons of each group (31.3%, 18.8%, 9.6% and 15.7%, respectively). These results demonstrate that septal neurons have the ability to express a variety of phenotypes when grown in vitro. This culture will be a useful tool for studying mechanisms of phenotype expression in septal neurons.

Acetylcholinesterase↗
PubMed1992

Calbindin-D28K (CaBP28k)-like Immunoreactivity in Ascending Projections.

This study concerns the involvement of calbindin-D28K (CaBP28k)-containing neurons in ascending spinal projections to the brainstem (nucleus of the solitary tract, lateral reticular nucleus area), pontine (parabrachial area) and mesencephalic (periaqueductal grey) structures. All these central structures are important in the processing of visceroception and visceronociception and all are targets for spinal efferents from similar areas. CaBP28k controls the excitability of cells by acting on intrinsic calcium metabolism. Results refer to the caudal spinal areas where the visceroceptive regions are concentrated. Experiments were performed through a double labelling approach that combined the retrograde transport of a protein - gold complex to identify the projection cells and immunohistochemistry to identify the CaBP28k-positive cells. The caudal spinal cord is rich in both CaBP28k-containing and projection cells. Cells colocalizing the protein and the retrograde tracer were quite numerous, with a particularly high concentration in the superficial layers of the dorsal horn (laminae I and outer II) and the lateral spinal nucleus. The other spinal areas containing immunoreactive projection cells were the reticular part of the neck of the dorsal horn, the medial laminae VII and VIII, lamina X and the sacral parasympathetic nucleus. The superficial layers and the neck of the dorsal horn are targets for nociceptive, visceroceptive and thermal inputs; the sacral parasympathetic column and lamina X are involved in visceroceptive integration. A functional role for the lateral spinal nucleus has not yet been established. Quite similar results were obtained for each of the ascending pathways under study. The high incidence of CaBP28k in spinal pathways suggests that calbindin has a major role in controlling the excitability of spinal cells subserving the processing of visceroception and/or visceronociception information to supraspinal levels. The participation of CaBP28k-immunoreactive cells in spinal ascending tract cells largely outnumbers those previously reported for various neuropeptides (Leah et al., Neuroscience, 24, 195 - 207, 1988)

Journal Article↗
PubMed1998

Phenotypic characterization of septal neurons in culture: immunohistochemistry of GABA, calbindin D-28k and choline acetyltransferase, and histochemistry of acetylcholinesterase

Phenotypes of septal neurons, dissociated from 19-day-old fetal rat brains and then cultured in a medium containing nerve growth factor for 4 weeks, were examined using gamma-aminobutyric acid (GABA), calbindin D-28k, parvalbumin and choline acetyltransferase immunohistochemistry, and acetylcholinesterase histochemistry. There were primarily four groups of neurons identified in this septal culture: the first group (12.7% of 212 neurons examined) displayed a cholinergic, but not GABAergic, phenotype and had an average diameter of 13.6±2.7 μm (mean±S.D.); the second group (31.6%) displayed both cholinergic and GABAergic phenotypes and had a diameter of 12.2±2.8 μm; the third group (31.0%) displayed only a GABAergic phenotype and had a diameter of 10.4±2.3 μm; and the fourth group (24.7%) displayed neither a GABAergic nor cholinergic phenotype and had a diameter of 10.4±2.1 μm. Neurons in the first two groups described were significantly larger than those in the second two groups; neurons in the third and fourth groups were the same size. Calbindin D-28k was expressed in some neurons of each group (31.3%, 18.8%, 9.6% and 15.7%, respectively). These results demonstrate that septal neurons have the ability to express a variety of phenotypes when grown in vitro. This culture will be a useful tool for studying mechanisms of phenotype expression in septal neurons.

Journal Article↗