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At least 577 records · Page 32Linked to original sources
PubMed1997

Glial-derived neurotrophic factor rescues calbindin-D28k-immunoreactive neurons in alcohol-treated cerebellar explant cultures.

Ethanol exposure during development leads to alterations in neuronal differentiation and profound neuronal loss in multiple regions of the developing brain. Although differentiating Purkinje cells of the cerebellum are particularly vulnerable to ethanol exposure, the mechanisms that ameliorate ethanol-induced Purkinje cell loss have not been well defined. Previous research indicates that glial-derived neurotrophic factor (GDNF), a member of the transforming growth factor-beta family, promotes the survival of several neuronal populations, including cerebellar Purkinje cells. Therefore, we examined whether GDNF could attenuate ethanol-induced Purkinje cell loss in an in vitro model system using calbindin-D28k immunoreactivity as a specific marker for Purkinje cells. We found that ethanol led to a significant dose-related decline in calbindin-D28k-immunoreactive cells in explant cultures of the developing cerebellum. However, concurrent administration of GDNF led to a significant rescue of calbindin-D28k-immunoreactive cells. Therefore, our results suggest that GDNF prevents ethanol-associated Purkinje cell loss.

Animals↗
PubMed1999

Determination of the metal-binding cooperativity of wild-type and mutant calbindin D9K by electrospray ionization mass spectrometry.

Since the initial reports showing the ability of electrospray ionization mass spectrometry (ESI-MS) to study intact noncovalent biomolecular complexes, an increasing number of uses for this technique in studying biochemical systems is emerging. We have investigated the ability of ESI-MS to characterize the metal-binding properties of calcium (Ca2+) binding proteins by studying the incorporation of Ca2+ and cadmium (Cd2+) into wild-type and mutant calbindin D9K. ESI-MS showed that wild-type calbindin D9K binds two Ca2+ ions with similar affinities while the binding of two Cd2+ ions is sequential, as is the binding of the two Ca2+ or Cd2+ ions to the N56A mutant of calbindin. The binding of Ca2+ to the wild-type protein was clearly seen to be cooperative. These results demonstrate the potential efficacy of ESI-MS to discriminate between cooperative and independent site metal binding to metalloproteins.

Cadmium↗
PubMed2002

Three-dimensional cartography of functional territories in the human striatopallidal complex by using calbindin immunoreactivity.

This anatomic study presents an analysis of the distribution of calbindin immunohistochemistry in the human striatopallidal complex. Entire brains were sectioned perpendicularly to the mid-commissural line into 70-microm-thick sections. Every tenth section was immunostained for calbindin. Calbindin labeling exhibited a gradient on the basis of which three different regions were defined: poorly labeled, strongly labeled, and intermediate. Corresponding contours were traced in individual sections and reformatted as three-dimensional structures. The poorly labeled region corresponded to the dorsal part of the striatum and to the central part of the pallidum. The strongly labeled region included the ventral part of the striatum, the subcommissural part of the external pallidum but also the adjacent portion of its suscommissural part, and the anterior pole of the internal pallidum. The intermediate region was located between the poorly and strongly labeled regions. As axonal tracing and immunohistochemical studies in monkeys show a similar pattern, poorly, intermediate, and strongly labeled regions were considered as the sensorimotor, associative, and limbic territories of the human striatopallidal complex, respectively. However, the boundaries between these territories were not sharp but formed gradients of labeling, which suggests overlapping between adjacent territories. Similarly, the ventral boundary of the striatopallidal complex was blurred, suggesting a structural intermingling with the substantia innominata. This three-dimensional partitioning of the human striatopallidal complex could help to define functional targets for high-frequency stimulation with greater accuracy and help to identify new stimulation sites.

Adult↗
PubMed2004

Calbindin-containing interneurons are a target for VIP-immunoreactive synapses in rat primary somatosensory cortex.

Inhibitory interneurons in cerebral cortex are morphologically and physiologically extremely heterogeneous. This greatly interferes with an understanding of their functions. Progress has been made by classifying these neurons with the aid of molecular markers, e.g., neuropeptides or calcium-binding proteins, which are reliably expressed by certain subpopulations. We have used this approach to demonstrate an output of a subpopulation of cortical interneurons which express vasoactive intestinal polypeptide (VIP). By double immunostaining and correlated light and electron microscopy, we show that calbindin (CB)-containing interneurons located in layers II-VI of rat barrel cortex are targets of symmetric VIP-immunoreactive synapses. All CB-immunoreactive interneurons showed numerous contacts of VIP boutons on proximal and distal dendritic segments. A great majority of CB-immunoreactive interneurons (214/222) displayed such close appositions with VIP boutons on their soma as well. Quantification revealed that the number of VIP-immunoreactive boutons on CB-immunoreactive somata and dendrites of specified order is comparable for the different cortical layers. In conclusion, all calbindin-containing cortical interneurons seem to be under direct influence of other GABAergic interneurons expressing the peptide VIP. An indirect functional consequence of this may be disinhibition of pyramidal cells, which are considered the major target of calbindin interneurons. However, since the examined types of interneurons are intricately embedded in networks of yet different interneurons, the outcome of these multiple inhibitory interactions is likely to be less simplistic. It may be related to the timing of pyramidal cell discharge within and across layers of cortical columns.

Animals↗
PubMed1991

Calbindin-like immunoreactivity in the central auditory system of the mustached bat, Pteronotus parnelli.

With the aid of a polyclonal antibody specific for Calbindin D-28k, we studied the distribution of this calcium-binding protein in the central auditory system of the mustached bat, Pteronotus parnelli. Components of the cochlear nucleus (CN) that were calbindin-positive (cabp(+] included the root of the auditory nerve, multipolar and globular bushy cells in the anteroventral CN, multipolar and octopus cells in the posteroventral CN, and small and medium-size cells in the dorsal CN. Not stained were spherical bushy cells of the anteroventral CN and pyramidal/fusiform cells in the dorsal CN. In the superior olivary complex, labeled cells were found in the lateral and medial nuclei of the trapezoid body, the ventral and ventromedial periolivary nuclei, and the anterolateral periolivary nucleus. No cellular labeling was seen in the lateral superior olive. In the medial superior olive, only marginal cells were cabp(+). Labeled fibers could be seen surrounding the gosts of unlabeled cells in both the latter nuclei. Most cells in the intermediate nucleus and the columnar division of the ventral nucleus of the lateral lemniscus were cabp(+). However, the dorsal nucleus was cabp(-). A group of cabp(+) cells was also seen in the paralemniscal zone. The inferior colliculus had a relatively low density of cabp(+) cells. Labeled cells were more common in the caudal half of the central nucleus, and in the external nucleus and dorsal cortex. In the auditory thalamus, nearly every cell in the medial geniculate body was cabp(+), but those in the suprageniculate nucleus and in the posterior group did not stain. Small cells in the intermediate layer and giant cells in the deep layers of the superior colliculus were densely cabp(+). In the pons, cabp(+) cells and neuropil could be seen in the medial and lateral pontine nuclei (pontine gray). In conclusion, calbindin-like immunoreactivity was found in most of the brainstem auditory system, as well as in regions associated with acoustic orientation or control of vocalization. However, except for a minority of cells of the medial superior olive, it is conspicuously absent from the nuclei receiving binaural input below the level of the inferior colliculus.

Animals↗
PubMed1995

Hypothalamic Leu-enkephalin-immunoreactive fibers terminate on calbindin-containing somatospiny cells in the lateral septal area of the rat.

Correlated light and electron microscopic double-immunostaining experiments for Leu-enkephalin and calbindin were employed to determine the postsynaptic targets in the septal complex of Leu-enkephalin fibers. Chronic surgical isolation of the septal complex from its hypothalamic afferents and retrograde tracer studies using wheat germ agglutinin-conjugated horseradish peroxidase, both followed by an immunostaining for Leu-enkephalin, were performed to elucidate the location of the origin of these axon terminals. Furthermore, a colocalization study for glutamic acid decarboxylase and Leu-enkephalin was carried out on hypothalamic sections to determine their possible coexistence in cells projecting to the lateral septum. These studies revealed that 1) Leu-enkephalin-immunoreactive axons form pericellular baskets around a population of lateral septal area neurons; 2) they establish exclusively asymmetric synaptic contacts on their soma and initial dendritic segments; 3) 10% of the lateral septal area calbindin-containing cells, which are all of the gamma-aminobutyric acid (GABA)-ergic somatospiny type, are innervated by Leu-enkephalin-immunoreactive baskets; 4) only 40% of the Leu-enkephalin target neurons are calbindin immunopositive; 5) the septopetal Leu-enkephalin fibers derive from neurons located in the ipsilateral perifornical area and anterior hypothalamus; and 6) none of their cells of origin cocontains the inhibitory transmitter GABA. These observations indicate that hypothalamic Leu-enkephalin-containing neurons are non-GABAergic excitatory cells. Hence, they can effectively stimulate a population of lateral septal area neurons, including the somatospiny cells, which are all GABAergic. Therefore, after stimulatory Leu-enkephalin action, these neurons can inhibit their postsynaptic targets, including other projective lateral septal neurons.

Animals↗
PubMed1993

Effect of 1,25,28-trihydroxyvitamin D2 and 1,24,25-trihydroxyvitamin D3 on intestinal calbindin-D9K mRNA and protein: is there a correlation with intestinal calcium transport?

Although analogs and metabolites of vitamin D have been tested for their calciotropic activity, very little information has been available concerning the effects of these compounds on gene expression. In this study one analog of vitamin D, 1,25,28-trihydroxyvitamin D2 [1,25,28-(OH)3D2], and one metabolite, 1,24,25-trihydroxyvitamin D3 [1,24,25-(OH)3D3], were tested for their effect on intestinal calbindin-D9K mRNA and protein as well as for their effect on intestinal calcium absorption and bone calcium mobilization. These compounds were also evaluated for their ability to compete for rat intestinal 1,25-(OH)2D3 receptor sites and to induce differentiation of human leukemia (HL-60) cells as indicated by reduction of nitro blue tetrazolium. In vivo studies involved intrajugular injection of 12.5 ng 1,25-(OH)2D3 or test compound to vitamin D-deficient rats and sacrifice after 18 h. 1,25,28-Trihydroxyvitamin D2 had no effect on intestinal calcium absorption, bone calcium mobilization, or intestinal calbindin-D9K protein and mRNA. Competitive binding to 1,25-(OH)2D3 receptors was 0.8% of that observed using 1,25-(OH)2D3. However, 20- and 40-fold higher doses of 1,25,28-(OH)3D2 (250 and 500 ng) resulted in significant inductions in calbindin-D9K protein and mRNA (3.5 to 7.4-fold), although doses as high as 800 ng were found to have no effect on intestinal calcium absorption or bone calcium mobilization.(ABSTRACT TRUNCATED AT 250 WORDS)

25-Hydroxyvitamin D 2↗
PubMed1994

Immunohistochemical distribution of calbindin D-28k and parvalbumin in the head of the caudate nucleus and substantia nigra of the cat.

The heterogeneous anatomy of both the dorsal striatum at the level of the head of the caudate nucleus and of the substantia nigra of cats was analyzed immunohistochemically using two calcium-binding proteins, namely, calbindin D-28k and parvalbumin. The striatal histochemical markers nicotinamide-adenine dinucleotide phosphate diaphorase and acetylcholinesterase were revealed in sections adjacent to those used for the immunohistochemical procedure. The distribution of both the calbindin D-28k and the parvalbumin immunoreactivities is heterogeneous in dorsal, ventral, lateral, and medial areas of the head of the caudate nucleus and is in register with the striosome/matrix pattern displayed by the histochemical markers. These calcium-binding proteins preferentially are located in the matrix compartment of the rostral caudate nucleus. Moreover, in some areas of the rostral two-thirds of the substantia nigra, calbindin D-28k and parvalbumin immunoreactivities appear to follow a complementary pattern that is quite different from the mesencephalic distribution of these two calcium-binding proteins.

Acetylcholinesterase↗
PubMed1996

1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100 beta.

The homodimeric S100 protein calcyclin has been studied in the apo state by two-dimensional 1H NMR spectroscopy. Using a combination of scalar correlation and NOE experiments, sequence-specific 1H NMR assignments were obtained for all but one backbone and > 90% of the side-chain resonances. To our knowledge, the 2 x 90 residue (20 kDa) calcyclin dimer is the largest protein system for which such complete assignments have been made by purely homonuclear methods. Sequential and medium-range NOEs and slowly exchanging backbone amide protons identified directly the four helices and the short antiparallel beta-type interaction between the two binding loops that comprise each subunit of the dimer. Further analysis of NOEs enabled the unambiguous assignment of 556 intrasubunit distance constraints, 24 intrasubunit hydrogen bonding constraints, and 2 x 26 intersubunit distance constraints. The conformation of the monomer subunit was refined by distance geometry and restrained molecular dynamics calculations using the intrasubunit constraints only. Calculation of the dimer structure starting from this conformational ensemble has been reported elsewhere. The extent of structural homology among the apo calcyclin subunit, the monomer subunit of apo S100 beta, and monomeric apo calbindin D9k has been examined in detail by comparing 1H NMR chemical shifts and secondary structures. This analysis was extended to a comprehensive comparison of the three-dimensional structures of the calcyclin monomer subunit and calbindin D9k, which revealed greater similarity in the packing of their hydrophobic cores than was anticipated previously. Together, these results support the hypothesis that all members of the S100 family have similar core structures and similar modes of dimerization. Analysis of the amphiphilicity of Helix IV is used to explain why calbindin D9k is monomeric, but full-length S100 proteins form homodimers.

Amino Acid Sequence↗
PubMed1997

Parvalbumin- and calbindin D-28k-immunoreactive innervation of orofacial tissues in the rat.

Parvalbumin- and calbindin D-28k-immunoreactive (-ir) innervation was examined in orofacial tissues of the rat. Labial and facial skins were devoid of the calcium-binding protein (CaBP)-ir nerve endings, while the infraorbital and mental nerves contained numerous parvalbumin-ir axons. Labial and gingival mucosae were also devoid of the CaBP-ir nerve endings. The buccal mucosa and incisive papilla contained both encapsulated and unencapsulated endings, while the hard palate mucosa excluding the incisive papilla contained only unencapsulated endings. Encapsulated endings were found just beneath the epithelium or attached to the cartilaginous core of the incisive papilla. Unencapsulated endings in the lamina propria were subdivided into two types: simple (unramified) and complex (ramified). Neurites of simple endings were straight, curved, or coiled, while those of complex endings exhibited a bush-like appearance due to the ramification. In addition, palatal rugae contained intraepithelial endings. The unencapsulated complex endings in palatal rugae coexpressed parvalbumin- and calbindin D-28k-irs, whereas other endings were immunoreactive for parvalbumin alone. The pterygopalatine ganglion contained calbindin D-28k-ir pericellular fibers but not the ir cell bodies. A subpopulation of trigeminal ganglion neurons coexpressed both CaBPs. CaBP-ir encapsulated and unencapsulated endings in the oral mucosa probably include low-threshold mechanoreceptors, while parvalbumin-ir intraepithelial endings in the palatal mucosa may be involved in nociception.

Animals↗
PubMed1993

Two-dimensional 1H nuclear magnetic resonance studies of the half-saturated (Ca2+)1 state of calbindin D9k. Further implications for the molecular basis of cooperative Ca2+ binding.

Calbindin D9k exhibits cooperative binding of two calcium ions, hence study of the half-saturated states of the protein is critical to understanding the binding process. However, the half-saturated states are not significantly populated under equilibrium conditions. To circumvent this problem, an absolutely conserved glutamic acid residue in the C-terminal binding site (site II) has been mutated to glutamine (E65Q), causing a substantial reduction in calcium affinity and permitting detailed two-dimensional 1H NMR analysis of calbindin D9k with a calcium ion bound only in the N-terminal EF-hand. Complete 1H resonance assignments have been obtained for (Ca2+)1 E65Q, as well as near complete assignments for the apo and (Ca2+)2 states. A value of 1.1(+/- 0.2) x 10(3) M-1 has been determined for the calcium binding constant in site II, from an analysis of the chemical shift changes in response to titration with calcium. The elements of secondary structure and global folding patterns were identified from nuclear Overhauser effects, backbone spin-spin coupling constants and the exchange rates of backbone amide protons. Although the mutation has only very small effects on the secondary structure and global fold of the protein, it so drastically lowers affinity for Ca2+ in the C-terminal site that (Ca2+)2 E65Q does not correspond to a standard (Ca2+)2 state. From the analysis of the half-saturated state, it is apparent that some reorganization of the structure and changes in the internal dynamics of calbindin D9k does occur for each step of the apo-->(Ca2+)1(I)-->(Ca2+)2 binding pathway. When the first ion is bound to the N-terminal EF-hand, that half of the molecule adopts a conformation and dynamic state similar to the fully calcium-loaded protein state, whereas only minor changes occur in the C-terminal EF-hand. It is only upon binding of the second calcium ion that the C-terminal EF-hand switches over to the fully calcium-loaded state. Together with the results from our earlier study of the apo-->(Ca2+)1(II)-->(Ca2+)2 binding pathway, these findings indicate that changes in protein conformation and dynamics associated with Ca2+ binding contribute to the observed positive cooperativity, and that the molecular details of the cooperative binding events are different for the two binding pathways.

Amides↗
PubMed1990

Calmodulin and calbindin in pancreatic islet cells.

The process of insulin release evoked by D-glucose and other nutrient secretagogues is triggered by an increase in cytosolic Ca2+ activity. However, some other insulinotropic agents may stimulate insulin release at a close-to-basal concentration of cytosolic ionized calcium. The control of cytosolic Ca2+ concentration depends not solely on the rate of Ca2+ entry into the cell through voltage-sensitive channels and Ca2+ exit via Na(+)-Ca2+ countertransport or active Ca2+ pumping, but also on the subcellular distribution of Ca2+, as dependent, for instance, on both Ca2(+)-ATPase activity and inositol 1,4,5-triphosphate-sensitive release in microsomes and calcium accumulation in mitochondria. Calmodulin and calbindin were both identified in pancreatic islet cells. Activation of adenylate cyclase by calcium-calmodulin may account for the increased production of cyclic AMP in islets stimulated by nutrient secretagogues. Calbindin is present in both normal and tumoral islet cells, and might participate to the alteration of islet function encountered in vitamin D-deprived or repleted rats. However, no target enzyme for calbindin was yet identified in islet cells. Independently of the role of calcium-binding regulatory proteins, the mitochondrial accumulation of calcium may account in part at least, for the preferential stimulation of mitochondrial oxidative events in the process of nutrient-stimulated insulin release.

Animals↗
PubMed1988

Localization of 28 kDa calbindin in human odontoblasts.

The presence of 28 kDa calbindin in human odontoblasts was studied by use of specific antibodies raised against chick duodenal 28 kDa calbindin, in immunofluorescence, immuno-peroxidase, and electron-microscopic labelling experiments. The calbindin-like protein was detected mainly in the cytoplasm of odontoblast cell bodies, in their processes and occasionally in their nuclei. Correspondingly, at the ultrastructural level, immunoreactive material was associated with the cytosol, microfilaments and cilia. These findings suggest that human odontoblasts express a 28 kDa vitamin D-dependent calcium-binding protein, unlike those of rats and mice in which ameloblasts are the only cells immunoreactive for the protein.

Animals↗
PubMed1988

Pineal-retinal molecular relationships; immunocytochemical evidence of calbindin-27 kDa in pineal transducers.

Calbindin-27 kDa immunocytochemical localization was studied concurrently in the pineal organ and retina from human as well as representatives of all vertebrate classes. Calbindin immunoreactivity was demonstrated in retinal cones (but not in rods) and in pineal transducers (cone-like and modified photoreceptor cells, pinealocytes) of a majority of amniotes. In contrast, no labelling was observed in anamniotes, except in retinal cones of the toad. Labelling was distributed through all cellular compartments (outer and inner segments, perikarya, pedicles or processes) of pineal transducers and retinal cones. Intra- and interspecific variations of calbindin contents are discussed.

Animals↗
PubMed1990

Expression of calbindin D-28K-like immunoreactivity in human SK-N-SH and SH-SY-5Y neuroblastoma cells.

Calbindin D-28K is a calcium-binding protein first isolated from avian intestines, and more recently shown to be present in a number of other vertebrate species and in other tissues, including CNS neurones. Using immunocytochemical techniques and Western blotting, we have shown that a calbindin D-28K-like protein is expressed in two related human neuroblastoma cell lines, SK-N-SH and SH-SY-5Y. To our knowledge these are the first immortal neuronal cell lines shown to express calbindin D-28K.

Blotting, Western↗
PubMed1991

Parvalbumin- and calbindin-containing neurons in the monkey medial geniculate complex: differential distribution and cortical layer specific projections.

Neuronal immunoreactivity for the calcium binding proteins, parvalbumin and calbindin, has been examined immunohistochemically in the monkey medial geniculate complex. Neurons containing one or other of these proteins were present in most (but not all) regions of the complex and were differentially distributed; parvalbumin immunoreactive neurons tended to form densely packed clusters in the ventral nucleus and rather loose arrangements in the anterodorsal and posterodorsal nuclei, whereas most calbindin neurons were scattered, with concentrations in the caudal end of the posterodorsal and in the magnocellular nuclei. In fluorescent tracer experiments combined with immunohistochemistry, it was found that parvalbumin and calbindin neurons project to layer IV and to layer I, respectively, of the primary auditory cortex. These results suggest the presence of parallel and chemically differentiated geniculocortical pathways which make different contributions to the neuronal circuitry of the auditory cortex.

Animals↗
PubMed1991

Differential sensitivity of calbindin and parvalbumin immunoreactive cells in the striatum to excitotoxins.

The neurotoxic effects of ibotenic acid, quinolinic acid and kainic acid on cells in the rat striatum were investigated using immunocytochemistry with antibodies to the calcium binding proteins, calbindin and parvalbumin. The results showed that both ibotenic acid and quinolinic acid affected calbindin and parvalbumin cells to the same extent. However, parvalbumin immunopositive neurons were more sensitive than calbindin immunopositive neurons to the neurotoxic effects of kainic acid. Although the reason for this increased sensitivity of parvalbumin striatal neurons to kainic acid is unclear, these results suggest that the neurotoxicity produced by kainic acid is different to that occurring with quinolinic acid and ibotenic acid.

Animals↗
PubMed1992

Calbindin immunoreactivity in normal human temporal neocortex.

Calbindin immunoreactivity in the temporal neocortex was examined in 4 subjects with no neurological, metabolic or malignant disease. The brains were obtained between 1 and 4 h after death and rapidly fixed by perfusion with 4% paraformaldehyde through the carotid arteries, cut into slabs, cryoprotected and stored at -80 degrees C. Sections of the whole left temporal lobe obtained with a freezing microtome were processed free-floating with a well known monoclonal antibody against calbindin according to the peroxidase-antiperoxidase (PAP) method. Calbindin-immunoreactive (CaBP-ir) neurons were found to be local-circuit neurons (interneurons) mainly distributed in the upper cortical layers (layers I, II and III), and were categorized as small multipolar neurons with ascending dendrites ramifying in the molecular layer, small bitufted cells, pyramid-like cells in layer II, horizontal neurons in the molecular layer, multipolar neurons with long descending dendrites, and large double-bouquet cells, some of them exhibiting a very long dendrite with claw-shaped terminals in layer V. Less than 10% of all CaBP-ir neurons were localized in the remaining cortical layers. Pyramidal cells were only very weakly or not stained at all. In addition, CaBP-ir fibres formed a dense plexus in the molecular layer, and vertical bundles 8-10 microns thick and 500-600 microns long, separated by blank spaces 20-40 microns wide were distributed in layers III and V/VI.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗