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 595 records · Page 33Linked to original sources

A subpopulation of large calbindin-like immunopositive neurones is present in the hippocampal formation in food-storing but not in non-storing species of bird.

The avian hippocampal formation (HP) is thought to play a role in the processing of spatial memory related to food-storing behaviour. The HP of two food-storing species (marsh tit (Parus palustris) and magpie (Pica pica)) and two non-storing species (great tit (Parus major) and jackdaw (Corvus monedula)) were compared following calbindin-like immunostaining. In the dorsal hippocampal region, both species of food-storing birds had larger calbindin-immunoreactive cells than did the two non-storing species. The fact that this association between storing behaviour and cell morphology is seen in two unrelated families of birds, the Paridae (marsh tit versus great tit) and Corvidae (magpie versus jackdaw) suggests that there may be a direct link between food-storing behaviour and the dorsal hippocampal calbindin-immunoreactive cell population.

Animals↗

Calbindin D-28K in the dopaminergic mesocortical projection of a monkey (Aotus trivirgatus).

Injections of fluorescent dyes were made in the prefrontal and motor cortex of owl monkeys and retrogradely labeled neurons in the mesencephalon were analyzed for tyrosine hydroxylase and calbindin-D28K immunostaining. Numbers of mesocortical dopaminergic neurons in the dorsal substantia nigra compacta and in the ventral tegmental area also contain calbindin-D28K. This cortically projecting calbindin-D28K containing subpopulation of the dopaminergic mesencephalic cells may be characterized by different electrophysiological properties and a lesser vulnerability to cell death.

Animals↗

Depletion and recovery of the calcium-binding proteins calbindin and parvalbumin in the pigeon optic tectum following retinal lesions.

Retinal lesions in pigeons produced a marked depletion of somata and neuropil staining for both calbindin-D28k and parvalbumin immunoreactivities in the contralateral optic tectum. Calbindin-like immunoreactivity reappeared in some tectal layers by 6 weeks postlesion, whereas paravalbumin-like immunoreactivity recovered almost completely after 5 weeks. These data indicate that the retinal input may control the expression of calbindin and parvalbumin in the pigeon optic tectum.

Animals↗

Calbindin D-28k as a marker for the associative cortical territory of the striatum in macaque.

An immunohistochemical study was made to investigate the topographic distribution of calbindin D-28k in relation to the associative and sensorimotor cortical territories in the macaque striatum. An intense calbindin-staining was found in the caudate nucleus and ventromedial putamen, i.e., in the associative striatum. In contrast, only a weak immunoreaction was found in the dorsolateral, sensorimotor, putamen. Calbindin immunoreactivity thus appears as a specific marker for the associative striatum.

Animals↗

Induction of Calbindin-D28K by 1,25-dihydroxyvitamin D3 in cultured chicken intestinal cells.

Intestinal cells from chicken embryos were grown in chemically defined, serum-free medium. The majority of cultured cells exhibits an epithelial-like morphology. As demonstrated by indirect immunofluorescence, the epithelial cells, and not the contaminating fibroblasts, express Calbindin-D28K only after 1,25-dihydroxyvitamin D3, the hormonally active form of vitamin D, is added to the culture medium. The highly sensitive reverse transcriptase-polymerase chain reaction shows that both Calbindin-D28K mRNA and the corresponding primary unprocessed transcripts (pre-mRNA) are dramatically increased in cultured intestinal cells treated with 1,25-dihydroxyvitamin D3, thus indicating that Calbindin-D28K is induced by the increased rate of transcription of the corresponding gene.

Animals↗

Neocortical neuronal subpopulations labeled by a monoclonal antibody to calbindin exhibit differential vulnerability in Alzheimer's disease.

Numerous studies have demonstrated that specific neuronal subtypes display a differential vulnerability to the pathological process in Alzheimer's disease. Large pyramidal neurons are likely to be highly vulnerable, whereas smaller neurons are more resistant to pathology. Using a monoclonal antibody to the calcium-binding protein calbindin, we observed in the human prefrontal cortex distinct populations of labeled cells. First, a subset of heavily stained interneurons was located in layers II and superficial III and in layers V-VI. Second, a subpopulation of pyramidal neurons in the mid and deep parts of layer III displayed a less intense, punctate staining pattern. The interneurons in the superficial layers were unaffected in the Alzheimer's disease cases. Interestingly, in layers V-VI, there was significant cell loss in the interneuron population, but only in the Alzheimer's disease cases with high neurofibrillary tangle densities. The calbindin-immunoreactive pyramidal neurons of layer III were dramatically affected in the disease. Moreover, there was a strong correlation between the extent of the loss of these cells and neurofibrillary tangle counts. These data suggest that calbindin is present in multiple neuronal subpopulations that exhibit a differential vulnerability in Alzheimer's disease and support the hypothesis that the degenerative process involves specific neuronal subsets with particular anatomical and molecular profiles.

Aged↗

The inferior colliculus: calbindin and parvalbumin immunoreactivity in neural grafts.

The inferior colliculus was selected as a brain stem site for study of neural grafting and identification of calcium binding proteins. Unilateral ablation sites of eight midbrain inferior colliculus in adult Long-Evans rats were implanted with E17-18 caudal tectum. After 2 to 9 months animals were sacrificed and sections reacted using antibodies for calbindin and parvalbumin. The central nucleus of normal inferior colliculus shows high density of neuronal and fiber staining for parvalbumin. Typical graft cores had similar staining distributions including discoid and stellate neuron populations. Graft cores showed low densities of reactivity for calbindin comparable to central nucleus. In surrounding graft regions there was substantive-neuronal and fiber labeling for calbindin and parvalbumin including stellate neuron populations normally found in the dorsal and lateral nuclei of inferior colliculus. These results demonstrate that the expression of calcium binding proteins in tectal grafts resembles that of inferior colliculus.

Animals↗

Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography.

In a structure of recombinant bovine calbindin D9k, determined crystallographically to 1.6 A resolution, a proline in mixed, approximately equally populated, cis and trans conformation is observed. Isomers of this kind have not been reported in structure determinations of calbindin D9k to 2.3 A resolution or in any other crystallographically determined protein structure. The cis-trans isomerization occurs at the peptide bond between Gly42 and Pro43, which is in agreement with results from two-dimensional 1H nuclear magnetic resonance spectroscopy experiments on solutions of calbindin D9k. Alternative backbone stretches have been modeled and refined by stereochemical restrained least-squares refinement for the segment Lys41 to Pro43. The final R-value was 0.188. The structural perturbations accompanying the cis-trans isomerization are found to be very localized. The largest positional differences are observed at residue Gly42, in which the alternative positions of the oxygen atom are 3.6 A apart.

Amino Acid Sequence↗

Comparison of the enhanced steady-state diffusion of calcium by calbindin-D9K and calmodulin: possible importance in intestinal calcium absorption.

The diffusion of calcium was measured using the unidirectional flux of 45Ca across an aqueous layer. The aqueous layer was bounded by two dialysis membranes and convection was eliminated by gelling the aqueous layer with agarose. The apparent self-diffusion coefficient was determined by the dependence of the tracer flux on the diffusion distance. The apparent self-diffusion coefficient increased linearly with the concentration of calbindin-D9K and calmodulin, but the effect of calmodulin was markedly less than that of calbindin-D9K. This difference is attributed to the lower association constant for calmodulin. The ion-exchange resin Chelex-100 also increased the steady-state of 45Ca, but the effect of Chelex-100 was much less efficient than the effect of calbindin-D9K. The mechanism of enhanced diffusion was attributed to an enhanced gradient of total 45Ca. These results indicate that the steady-state unidirectional calcium flux is a superposition of free calcium diffusion and bound calcium diffusion, with only a small contribution due to a 'bucket brigade' mechanism. We suggest that this phenomenon may be important in calcium absorption across the intestine.

Animals↗

Appearance during chick embryogenesis of vitamin D-dependent calcium-binding protein (calbindin-D28K).

The appearance of the vitamin D-dependent calcium-binding protein (calbindin-D28K) in embryonic chick tissues was determined using a sensitive immunohistochemical assay to elucidate the possible role of calbindin-D28K during embryogenesis. This protein first occurs in renal, cerebellar and intestinal cells during the final stages of maturation and/or differentiation. It is during this period of their development that these tissues become functional. On the basis of our observations, we suggest that the onset of cell function may be coupled with the appearance of calbindin-D28K.

Animals↗

TPA decreases 1,25(OH)2D3 binding and calbindin D-28K in renal (MDBK) cells.

The effect of the phorbol ester TPA (12-O-tetradecanoylphorbol 13-acetate) on vitamin D receptors (VDRs) was studied in MDBK cells, a normal bovine renal epithelial cell line. 24 h treatment of MDBK cells with TPA resulted in down-regulation of VDR number, with no change in the binding affinity for 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) or approximate molecular weight determined by fast protein liquid chromatography (FPLC). TPA treatment also reduced the level of calbindin D-28K, a vitamin D-dependent renal protein. 4 alpha-Phorbol 12,13-didecanoate (4 alpha-PDD), an inactive phorbol ester, did not affect either 1,25(OH)2D3 binding or calbindin D-28K levels. TPA elicited a significant decrease in membrane-associated protein kinase C (PKC) activity which coincided with the reduction in VDR number and calbindin D-28K. These data support a link between TPA, PKC activity and vitamin D actions in kidney.

Animals↗

Localization of calbindin D28 mRNA in rat tissues by in situ hybridization.

We investigated, by in situ hybridization histochemistry, the cellular localization of the mRNA encoding a vitamin D-dependent calcium-binding protein (calbindin D28) in rat brain and peripheral organs. Using a [35S]cRNA probe under high stringency conditions, specific mRNA was found in tissues well known for their calbindin D28 content, e.g. renal distal tubules, cerebellar Purkinje cells and dentate gyrus granule cells. Tissue devoid of this protein, such as liver, also lacked specific mRNA. In situ hybridization histochemistry allows the precise identification of cells expressing calbindin D28 and offers a new approach to study its regulation and possible role, e.g. in neuronal function.

Animals↗

Colocalization of calbindin and GABA in medial nucleus of the trapezoid body of the rat.

Using immunocytochemical methods, both calbindin and GABA were found to be colocalized in the somas of all the cells of the medial nucleus of the trapezoid body (NMTB) of the rat auditory system. In the lateral superior olive (LSO), calbindin was also found in the terminals but not in the cells. Some terminal labelling was found in the medial superior olive (MSO). GABA was also found in the somas of some cells in both LSO and MSO, but most of the labelling was in terminals. In the rat, calbindin appears to be more involved in a pathway that detects interaural intensity differences.

Animals↗

Detection of the 9-kDa vitamin D-dependent calbindin gene in a fruit bat (Rousettus aegyptiacus) fibroblast cell line.

1. A fibroblast cell line was established from skin and lung tissue of the fruit bat (Rousettus aegyptiacus). 2. Genomic DNA, isolated from the fibroblast cells, was restriction digested and probed for the 9-kDa calbindin gene with a 180 base-pair fragment of mouse calbindin-D9K cDNA. Genomic DNA from rats and humans was similarly probed. 3. Hybridization and thus homology was observed between the mouse probe and DNA from the rat and the fruit bat, but not the human. 4. The results are discussed in relation to the detection of calbindin-D9K in the fruit bat despite very low circulating levels of its inducer 1,25(OH)2D3.

Animals↗

Parvalbumin and calbindin-D28K immunoreactivity as developmental markers of auditory and vocal motor nuclei of the zebra finch.

The posthatch developmental profiles of parvalbumin and calbindin-D28K immunoreactivity were compared for the auditory nucleus mesencephalicus lateralis pars caudalis in the midbrain, n. ovoidalis in the thalamus, and telencephalic field L, as well as for the telencephalic vocal motor nuclei hyperstriatum ventrale pars caudalis and n. robustus archistriatalis. The two calcium-binding proteins showed specific temporal patterns of expression in each nucleus, without following an ascending or descending sequence. Calbindin-D28K immunoreactivity usually preceded parvalbumin immunoreactivity. Onset of expression, especially of parvalbumin-immunostaining, was earlier in auditory nuclei than in vocal motor nuclei. The developmental order of appearance of immunoreactivity in somata, dendrites and axons was different in various brain regions. In some structures parvalbumin or calbindin-D28K immunoreactivity occurred only transiently. The two antibodies bound to separate but spatially complementary groups of cells in the nucleus mesencephalicus lateralis pars dorsalis and n. ovoidalis, as has previously been described in visual nuclei. This pattern was maintained into adulthood. These hitherto unknown subcompartments may reflect internal functional organization in these nuclei. A transitory neostriatal zone containing parvalbumin-positive neurons and fibres was observed between the immature field L and the emerging hyperstriatum ventrale pars caudalis. Some comparative aspects are discussed as to the way in which neurons distinguished by the two Ca-binding proteins may differ in energy metabolism, activity pattern and other functional mechanisms.

Animals↗

Calbindin D-28K- and parvalbumin-reacting neurons in the hypothalamic magnocellular neurosecretory nuclei of the rat.

The distribution of calbindin D-28K- and parvalbumin-reacting neurons in the hypothalamic magnocellular neurosecretory nuclei of the rat was studied using the avidin-biotin-immunoperoxidase method and highly specific monoclonal antibodies. Incubation with anticalbindin D-28K-antiserum revealed immunoreactive neurons in the following nuclei: supraoptic, paraventricular (both in the magnocellular and parvicellular regions), circularis, fornicals and medial forebrain bundle. Incubation with parvalbumin antiserum displayed immunoreactive neurons only in the circularis nucleus. Additionally, it was possible to observe scattered calbindin and parvalbumin immunoreactive neurons (which do not form part of the nuclei considered) located in the hypothalamic area between the supraoptic and the paraventricular nuclei, especially for the calbindin D-28K antiserum.

Animals↗

Neuronal phenotypes in mouse dorsal root ganglion cell cultures: enrichment of substance P and calbindin D-28k expressing neurons in a defined medium.

The primary sensory neurons in mouse dorsal root ganglia consist of diversified subpopulations which express distinct phenotypic characteristics such as substance P or calbindin D-28k. To determine whether neuronal phenotypes are altered or not in in vitro cultures carried out in a defined synthetic medium, dissociated dorsal root ganglion cells from newborn mice were grown in the alpha-modified minimum essential medium either supplemented with 10% fetal calf serum or serum-free. About 80% of the neurons survived after 5 days of culture in both media, but only 35% or 65% were rescued after 12 days in serum-free or fetal calf serum supplemented medium, respectively. The neuronal subpopulations expressing substance P or calbindin D-28k displayed similar morphological properties in both media and a higher resistance to culture conditions than the whole neuronal cell population, especially in serum-free medium. It is therefore concluded that a defined synthetic medium offers reproducible conditions to culture dorsal root ganglion cells for at least 5 days, stimulates the expression of substance P and enriches preferentially neuronal phenotypes expressing substance P or calbindin D-28k, for a longer period of culture.

Animals↗