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PubMed1990

Calbindin D-28k Protein and mRNA Localization in the Rat Brain.

After the discovery of calretinin, a protein with high sequence homology to calbindin D-28k, the validity of immunohistochemical results obtained using polyclonal antibodies for this protein, was in question. In order to validate the previous results on the localization of calbindin D-28k in the brain, we localized the protein by highly specific monoclonal antibodies and revealed its mRNA histochemically by in situ hybridization. In general there was good agreement between the results obtained using these two different techniques and those reported in previous publications. The concordance was particularly impressive for the cerebral cortex, basal ganglia, basal nucleus of Meynert, hippocampus, thalamus, cerebellum and superior colliculus. In the amygdala and hypothalamus the low spatial resolution of in situ hybridization did not allow precise definition of some nuclei displaying a positive reaction for the protein. In the rhombencephalon, cells of the parabrachial nuclei and the dorsal raphe nucleus expressed calbindin D-28k. Neurons in the dorsal horn of the spinal cord and some horizontal cells of the retina were tagged with both methods. The only discrepancy was the presence of immunoreactive ependymal cells, whereas mRNA never occurred in cells lining the ventricles. Thus, the combined approach has established the widespread distribution of cells expressing calbindin D-28k in the rat brain.

Journal Article↗
PubMed1996

Shell and core in monkey and human nucleus accumbens identified with antibodies to calbindin-D28k.

The neurochemical division of the rodent nucleus accumbens into shell and core is now a widely accepted concept. However, such divisions in the primate nucleus accumbens have yet to be fully clarified and described. In the present study, the forebrains of three primates--marmoset, rhesus monkey, and human--and a Wistar rat, were immunoreacted with antibodies directed against calbindin-D28k. The patterns of immunoreactivity in the primates' ventral striatum were mapped and compared to that of rat. Calbindin staining was uneven in all species and there was no evidence of a bicompartmental organization, i.e., striosome/patch and matrix, in central parts of the nucleus. Nucleus accumbens in primates, as in rat, could be divided immunohistochemically into a crescent-shaped outer shell--medially, ventrally and laterally--and an inner core. In general, medial parts of the shell stained less intensely for calbindin than did lateral parts. However, interspecific variation in the intensity of the immunoreactive staining and the mediolateral extent of the shell was obvious. The core, which immunostained unevenly, was consistently more intensely immunoreactive than either medial or lateral shell in all species except the marmoset. These results suggest that the neurochemical subdivisions of shell and core established for nucleus accumbens of rodents are also present in primates. However, further work is needed to establish whether these territories are homologous and, if so, the full extent of that homology.

Animals↗
PubMed1996

Presence of calbindin D28K and GAD67 mRNAs in both orthotopic and ectopic Purkinje cells of staggerer mice suggests that staggerer acts after the onset of cytodifferentiation.

We used in situ hybridization to study the expression of GAD67 and calbindin D28K mRNAs in developing mouse cerebellar Purkinje cells. Both genes are expressed prenatally; calbindin D28K mRNAs can be detected in Purkinje cells of embryonic day (E) 15 mice, whereas GAD67 mRNAs first appear slightly later, in E16 mice. The stunted Purkinje cells of staggerer (sg/sg) mutant mice maintain calbindin D28K and GAD67 expression. Our data suggest that the sg/sg mutation does not interfere with the transcriptional activation of these two genes, and might therefore act after the induction of specific gene expression in developing Purkinje cells.

Animals↗
PubMed1994

Control of calbindin-D28K expression in developing mouse kidney.

Calbindin-D28K, a cytoplasmic calcium-binding protein located in restricted regions of mature metanephric kidneys, is expressed in a complex manner by kidneys developing in culture. In developing collecting duct, it is present in all regions and is independent of 1,25-dihydroxy-vitamin D3 [1,25(OH)2D3]. In developing nephrons, its expression is restricted to the most distal end of the growing tubule, commences during differentiation of specialized tubule segments, and depends completely on the presence of 1,25(OH)2D3. The Wolffian ducts of mesonephric kidneys also express calbindin independently of 1,25(OH)2D3, as do the Wolffian duct-derived connecting tubules, but mesonephric nephrons show no expression of the molecule. By displaying separate tissue-specific controls for calbindin expression, cultured kidney rudiments offer a very accessible system for investigation of the control mechanisms involved.

Animals↗
PubMed1994

Calmodulin immunoreactivity in the chicken pineal gland: comparison with calbindin-D28k, calretinin, and S100.

Calmodulin distribution in the chicken pineal organ was investigated by immunohistochemistry. Calmodulin immunoreactivity was detected in ependymocytes in the follicular zone and in interstitial cells in the parafollicular zone. No calmodulin immunoreactivity was detected in pinealocytes. Lack of calmodulin immunoreactivity in pinealocytes raises questions about its proposed function in melatonin synthesis as suggested by pharmacological studies using calmodulin antagonists. The calmodulin distribution was comparable to that of S100, a glial cell marker. Two other markers, calbindin-D28k and calretinin, which in neuroanatomical studies give excellent cytoarchitectonic staining, in the chick pineal permitted the detection of two subclasses of pinealocytes. One was darkly stained by calbindin-D28k and rare. The other was very abundant and calretinin positive. In the parafollicular zone, calbindin-D28k and/or calretinin antibodies allowed us to visualize cells presenting a neuron-like morphology. Calretinin immunoreactivity was detected in nearly all pinealocytes in which hydroxy-indol-O-methyl transferase was also located. Comparison between the lack of calmodulin and the presence of calretinin, belonging to the same calcium-binding protein family, in chick pinealocytes raises the hypothesis about a possible role of calretinin in melatonin synthesis.

Animals↗
PubMed2001

Chemical organization of the macaque monkey olfactory bulb: II. Calretinin, calbindin D-28k, parvalbumin, and neurocalcin immunoreactivity.

The distribution and morphologic features of calcium-binding protein- (calbindin D-28k, calretinin, neurocalcin, and parvalbumin) immunoreactive elements were studied in the macaque monkey olfactory bulb by using specific antibodies and the avidin-biotin-immunoperoxidase method. A characteristic laminar pattern of stained elements was observed for each marker. Scarce superficial short-axon cells and superficial stellate cells demonstrated calbindin D-28k immunoreactivity in the outer layers, whereas a moderate number of calbindin D-28k-immunoreactive granule cells and scarce deep short-axon cells were observed in the inner layers. Calretinin-staining demonstrated abundant periglomerular cells and granule cells and a scarce number of other interneuronal populations. Most neurocalcin-immunopositive elements were external and medial tufted cells and periglomerular cells, although other scarcer interneuronal populations were also immunostained. A few superficial and deep short-axon cells as well as small interneurons in the external plexiform layer were the only elements immunoreactive to parvalbumin. The distribution of the immunoreactive elements in the olfactory bulb of the macaque monkey showed a high similarity to that reported in the human, whereas it demonstrated a different and simpler pattern to what has been reported in the olfactory bulb of macrosmatic animals. It suggests more homogeneous calcium-mediated cell responses after stimulation that could be correlated to the lower capability to modulate olfactory signals in microsmatic animals. In addition, these results indicate that experimental models in rodents do not provide an accurate estimation of calcium-binding protein-immunoreactive neuronal populations in the primate olfactory system.

Animals↗
PubMed1995

Correlation of anoxic neuronal responses and calbindin-D28k localization in stratum pyramidale of rat hippocampus.

Immunohistochemical staining for the calcium-binding protein calbindin-D28k (CaBP) was combined with Lucifer Yellow (LY) identification and intracellular recording of changes in membrane parameters of pyramidal neurons in CA2, CA1, and the subiculum of rat hippocampal slices during brief exposure (4.0 +/- 0.19 min) to N2. Anoxia evoked either a depolarization or hyperpolarization of membrane potential (VM) (+21.5 +/- 2.79 mV above VM = -70.5 +/- 1.50 mV, n = 30 and -7.2 +/- 0.72 mV below VM = -68.2 +/- 1.34 mV, n = 24, respectively) and a fall in membrane resistance of approximately 20%. Differences in the response could be correlated with the presence or absence of CaBP and the localization of neurons in different layers of stratum pyramidale and sectors of the hippocampus. For neurons immunopositive for calbindin (CaBP(+)), depolarization was observed more frequently (83%) than hyperpolarization (17%); in contrast, 44% of responses of calbindin-negative (CaBP(-)) neurons were depolarizing and 56% were hyperpolarizing. Depolarizations of CaBP(+) neurons were more gradual in slope, and more rapidly reached a plateau in comparison with those recorded in CaBP(-) neurons. Responses of neurons in the superficial layer of stratum pyramidale (in which 79% of CaBP(+) pyramidal neurons were situated) were mainly depolarizing (91%), while for those in the deep layer (which contained 89% of the CaBP(-) cells) such responses were observed less often (45%). Depolarization was also more common than hyperpolarization for cells located in CA2/CA1c/CA1b (63%) than in the CA1a/subicular region (37%). The depolarizing response of the majority of pyramidal neurons which are CaBP(+), superficial, and closer to CA3 may reflect an efficient buffering of intracellular Ca2+, which maintains a low [Ca2+]i, steep gradient for Ca2+ influx and may facilitate the movement of Ca2+ away from points of entry. The neurons which are CaBP(-), deep, and closer to subiculum and in which N2 evokes hyperpolarization, on the other hand, may have a sustained elevation/accumulation of cytosolic Ca2+ which could activate K+ conductance, inhibit Ca2+ influx, and stabilize the membrane potential. These experiments provide a functional correlate for CaBP and suggest that it may have a significant role in Ca2+ homeostasis and the determination of selective neuronal vulnerability.

Animals↗
PubMed1994

Cellular distribution of calbindin D28K mRNAs in the adult mouse brain.

We have determined the cellular distribution of calbindin D28K mRNAs throughout the mouse brain by in situ hybridization. While these studies identified neuronal populations similar to those previously identified in rat brain by immunohistochemistry, some discrepancies exist. These may derive from species differences or from the immunological cross-reactivity of calbindin D28K antiserum with other proteins. We note an intriguing association between the distribution of neurons containing calbindin D28K mRNA and those reported by others to contain the inositol 1,4,5-triphosphate (InsP3) receptor.

Animals↗
PubMed1994

Deafferentation removes calretinin immunopositive terminals, but does not induce degeneration of calbindin D-28k and parvalbumin expressing neurons in the hippocampus of adult rats.

Unilateral combined transections of the fimbriafornix and angular bundle in adult Fischer 344 rats were used to study the effects of deafferentation on hippocampal expression of calretinin, calbindin D-28k, and parvalbumin. Reflecting the widespread degeneration of synaptic contacts, immunostaining for glial fibrillary acidic protein 6 days after the lesions was increased in lacunosum-molecular and oriens layers of CA1, 2, and 3 in ipsi- and contralateral hippocampus and in the ipsilateral dentate gyrus outer molecular layer. At 21 days the immunoreactivity had decreased to control levels except for a still slightly increased signal in the oriens layer of CA1-3. At 6 and 21 days after the combined lesions the numbers of hippocampal neurons containing calretinin, parvalbumin, and calbindin D-28k was unaltered. The combined lesions abolished calretinin containing terminals in the dentate gyrus inner molecular layer on the deafferentated side. This could be reproduced by single unilateral fimbria-fornix transections, suggesting that the axons of these calretinin positive terminals project to the hippocampus through the fimbria-fornix. The most likely origin of the calretinin positive terminals are neurons in the supramammillary hypothalamic nucleus. Our findings demonstrate that the extensive lesion-induced synaptic rearrangements in the adult hippocampus do not induce degeneration of hippocampal neurons expressing calretinin, calbindin D-28k, and parvalbumin, but do remove calretinin containing terminals which reach their targets in the hippocampus through the fimbria-fornix.

Animals↗
PubMed2000

Distribution of calbindin, parvalbumin, and calretinin immunoreactivity in the reticular thalamic nucleus of the marmoset: evidence for a medial leaflet of incertal neurons.

The placement of the reticular thalamic nucleus (RTN) between the dorsal thalamus and the cortex and the inhibitory nature of reticulothalamic projections has led to suggestions that it "gates" the flow of sensory information to the cortex. The New World diurnal monkey, the marmoset, Callithrix jacchus is emerging as an important "model primate" for the study of sensory processing. We have examined the distribution of Nissl-stained somata and calbindin, parvalbumin, and calretinin immunoreactivity in the ventral thalamus for comparison with other species. Cells were labeled using standard immunohistochemistry, ExtraAvidin-HRP, and diaminobenzidine reaction products. The RTN is constituted by a largely homogeneous population of parvalbumin immunoreactive cells with respect to size and orientation. Calbindin and calretinin immunoreactive cells were only found along the medial edge of the RTN adjacent to the external medullary lamina of the dorsal thalamus and laterally near the ventral RTN. These cells were considered to be part of the zona incerta (ZI). The marmoset ZI could be subdivided into dorsal and ventral regions on the basis of its immunoreactivity to calcium binding proteins. Both the ZI and nucleus subthalamicus Luysi contained scattered calbindin and calretinin immunoreactive cells with well-defined dendritic processes. These cells were clearly different to cells in the dorsal thalamus. Parvalbumin immunoreactive cells in RTN, ZI, and subthalamic nucleus were on average larger than neurons positive for the other calcium binding proteins. Future studies reporting the afferent and efferent projections to the RTN must view their results in terms of the close apposition of RTN and ZI somata.

Animals↗
PubMed1999

Expression and purification of human calbindin D28k.

Calbindin D28k is a protein abundant in the mammalian central nervous system and in epithelial tissue involved in Ca2+ transport. Human calbindin D28k was cloned into a Pet3a vector and expressed in Escherichia coli. The protein was purified in three steps: (i) heat precipitation of bacterial proteins, (ii) ion-exchange chromatography on a DEAE-cellulose column in the presence of calcium, and (iii) ion-exchange chromatography on a DEAE-Sephacel column in the presence of EDTA. The protein was then supplemented with calcium and dialyzed against neutral water. The final yield was 20-50 mg of pure, homogeneous calcium-loaded calbindin D28k per liter of bacterial culture. The identity and purity of the protein were confirmed by immunoblotting, SDS-polyacrylamide gel electrophoresis, and agarose gel electrophoresis in the absence and presence of calcium and 1H NMR spectroscopy. The entire expression and purification protocol takes only 3 days and is easy to scale up and down. It was designed to minimize degradation and deamidation.

Amino Acid Sequence↗
PubMed1995

Transient co-localization of calretinin, parvalbumin, and calbindin-D28K in developing visual cortex of monkey.

This paper reports a double-labelling immunocytochemical study of the three calcium-binding proteins calretinin, parvalbumin, and calbindin-D28k in developing and adult Macaca primary visual cortex. In adult visual cortex, each protein marks a subset of GABAergic neurons with a characteristic laminar distribution and virtually no co-localization was found between these three proteins, suggesting that each calcium-binding protein may serve as a marker for one or more cortical subcircuits. The immature visual cortex, immunostained using identical techniques was then analysed to determine if each calcium-binding protein could serve as a developmental marker for these circuits. The Cajal-Retzius cells of layer 1 contained all three proteins during development. Calbindin-D28k and calretinin were co-localized starting at Fd (foetal day) 45 and after Fd125, parvalbumin also was present in the same Cajal-Retzius cells. All three proteins continued to be expressed until the Cajal-Retzius disappeared postnatally. In layers 2-6 calbindin-D28k and calretinin were never co-localized. In contrast, parvalbumin and calretinin were found in neurons of deep layer 3 from Fd 155 to postnatal (P6) weeks with a few persisting even later. Before birth almost all PV+ neurons in layers 4-6 were CaB+, but by P3 weeks only a few PV+/CaB+ neurons remained in layer 4C and these completely disappeared by P6 weeks. Co-localization in layer 4 neurons overlaps the period of ocular dominance segregation, suggesting that the onset of cortical maturity coincides with segregation of calcium-binding proteins within the GABA interneurons.

Animals↗
PubMed1992

In vitro enzyme activation with calbindin-D28k, the vitamin D-dependent 28 kDa calcium binding protein.

Purified porcine erythrocyte membrane Ca(2+)-ATPase and 3':5'-cyclic nucleotide phosphodiesterase were stimulated in a dose-dependent, saturable manner with the vitamin D-dependent calcium binding protein from rat kidney, calbindin-D28k (CaBP-D28k). The concentration of CaBP-D28k required for half-maximal activation (K0.5 act.) of the Ca(2+)-ATPase was 28 nM compared to 2.2 nM for calmodulin (CaM), with maximal activation equivalent upon addition of either excess CaM or CaBP-D28k. 3':5'-Cyclic nucleotide phosphodiesterase (PDE) also showed equivalent maximum saturable activation by calbindin (K0.5 act. = 90 nM) or calmodulin (K0.5 act. = 1.2 nM). CaBP-D28k was shown to effectively compete with CaM-Sepharose for PDE binding. Immunoprecipitation with CaBP-D28k antiserum completely inhibited calbindin-mediated activation of PDE but had no effect on calmodulin's ability to activate PDE. While the physiological significance of these results remains to be established, they do suggest that CaBP-D28k can activate enzymes and may be a regulator of yet to be identified target enzymes in certain tissues.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1993

Transient expression of calretinin during development of chick cerebellum. Comparison with calbindin-D28k.

Calcium ions play a critical role in neural development. Insights into the ontogeny of Ca2+ homeostasis were gained by investigating the developmental expression of two E-F hand calcium-binding proteins. Calretinin and calbindin were monitored through their immunoreactivity in the developing chick cerebellum (from E6 to E20). Calbindin was detected from E13 and in Purkinje cells only. Intensity of labelling increased with Purkinje cell development. Calretinin presented a transitory immunoreactivity between E11 and E20 in the internal granular cell layer. This cell layer contains cells which will differentiate into Golgi and granular cells which are calretinin-negative in adult chick cerebellum. Calretinin immunoreactivity presented a peak (both in number of cells and in intensity) at E15 and fell dramatically after E20 while calbindin immunoreactivity was restricted to the Purkinje cells and increased with the development of these cells.

Animals↗
PubMed1994

Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or the 72 kDa heat-shock protein in three models of acute CNS injury.

Changes at the level of gene expression are becoming an increasingly recognized component of the neuronal response to injury. We used Northern analysis and three in vivo models of central nervous system (CNS) injury in the rat to determine whether injury alters the expression of certain gene products related to cellular homeostasis. The three models included kainate (KA)-induced seizures, global ischemia, and lateral fluid percussion injury to the cerebral cortex. Animals were sacrificed at various times after injury, and total RNA was isolated from specific brain regions. Northern blots were hybridized with probes for calbindin-D28K, the 78 and 94 kDa glucose-regulated proteins (grp78, grp94), the inducible 72 kDa heat-shock protein (hsp72), and a control probe for the 18S ribosomal subunit. Results showed that mRNA for calbindin-D28K, grp78, and hsp72 increased in the hippocampus following seizures. Peak expression occurred 6-12 h after administration of KA, and returned towards baseline in most cases by 24 h. Changes in all four transcripts were seen in the hippocampus or cortex following global ischemia, although the return to baseline tended to exceed 24 h for the grps. In the trauma model, mRNA for hsp72 was increased in the cortex ipsilateral to the impact 12 h after injury. These results expand the repertoire of known changes in mRNA expression following CNS injury. The increases in hsp72 and grps indicate the occurrence of a generalized stress response. Furthermore, given the evidence that grp78 and grp94 are induced by calcium ionophores in vitro, and the potential role of calbindin-D28K in buffering cytoplasmic calcium, the changes observed in this study may represent a cellular response to perturbed calcium homeostasis that is known to occur in acute CNS injury.

Animals↗
PubMed1993

Relative loss of the striatal striosome compartment, defined by calbindin-D28k immunostaining, following developmental hypoxic-ischemic injury.

The striatum is especially vulnerable to hypoxic-ischemic injury, both in adulthood and during development. Striatal injury is likely to play a major role in the chronic abnormalities of motor control which occur as a consequence of developmental hypoxia-ischemia. Previous studies have shown that two striatal neuron phenotypes, cholinergic and NADPH-diaphorase-positive, are resistant to developmental hypoxia-ischemia, but little is otherwise known of patterns of vulnerability among other striatal neurons. In particular, there has been no data available about patterns of vulnerability within the major striatal neuron group, the medium-sized neurons. Since a major anatomical and functional organization of these neurons is in their localization to either the striosome or the matrix compartments, we have examined the effect of developmental hypoxia-ischemia on these compartments using a quantitative morphologic analysis of immunostaining for the calcium-binding protein calbindin-D28k. We have found that there is a predominant loss of the striosome compartment; in the presence of a mean loss of 33% of total striatal area, there was a 49% decrease in striosomal area. There was also a 41% reduction in the number of striosomes, and a small (14%) but significant decrease in the mean area of individual striosomes. The striosome loss was uniform in the rostrocaudal dimension. At a cellular level, the density of calbindin-positive neurons, expressed as number per unit area, was preserved. While there are several possible explanations for the selective loss of the striosome compartment, one hypothesis is that the lower level of calbindin within these neurons makes them more vulnerable to increases in intracellular calcium, which has been postulated to play a role in hypoxic-ischemic injury. The predominant loss of the striosome compartment following hypoxic-ischemic injury may lead to an imbalance with the functionally distinct matrix system. Such an imbalance may contribute to the abnormalities of motor control observed after this form of injury.

Age Factors↗
PubMed1996

Distribution of neurofilament protein and calcium-binding proteins parvalbumin, calbindin, and calretinin in the canine hippocampus.

Neurofilament protein and calcium-binding proteins parvalbumin, calbindin, and calretinin are present in morphologically distinct neuronal subpopulations in the mammalian cerebral cortex. Immunohistochemical studies of the hippocampal formation and neocortex have demonstrated that while neurofilament protein and calbindin are localized in subsets of pyramidal neurons, the three calcium-binding proteins are useful markers to differentiate non-overlapping populations of interneurons. To date, most studies have been performed in rodents and primates. In the present analysis, we analyzed the distribution of these proteins in the canine hippocampus. Neurofilament protein was present in large multipolar neurons in the hilus and in pyramidal neurons in the CA3 field, whereas pyramidal neurons in the CA1 field and subiculum were less intensely immunoreactive. Parvalbumin immunoreactivity was observed in large multipolar neurons in the hilus and throughout the CA3-CA1 fields, in a few pyramidal-shaped neurons in the CA1 field and subiculum, and had a distinct neuropil staining pattern in the granule cell layer and stratum pyramidale of the Ammon's horn. Calbindin immunoreactivity displayed a strong labeling of the granule cells and mossy fibers and was also observed in a population of moderately immunoreactive neurons in the CA1 field and subiculum. Calretinin immunoreactivity was relatively weaker overall. The inner molecular layer in the dentate gyrus had a distinct band of labeling, the stratum lacunosum/moleculare contained a punctate neuropil staining, and there were a few small multipolar neurons in the hilus, CA3-CA1 fields, and subiculum. Comparison of the staining patterns observed in the dog hippocampus with those in human, macaque monkeys and rats revealed that although there are some subregional differences among these taxa, the dog may constitute a valuable large animal model for the study of certain neurological conditions that affect humans, in spite of the phylogenetic distance between carnivores and primates.

Animals↗
PubMed2004

Altered hippocampal expression of calbindin-D-28k and calretinin in GABA(B(1))-deficient mice.

Balb/c GABA(B(1))(-/-) mice develop complex epileptiform activity, including spontaneous and audiogenic generalized seizures, 6-8 weeks after birth. The neuronal systems involved in these epilepsies have not been identified yet. Because the hippocampus is critically involved in epileptiform activity, we now investigated whether this brain region exhibits seizure-related alterations. Using semi-quantitative immunohistochemistry, we studied the temporal and cellular hippocampal expression pattern of two seizure-sensitive calcium-binding proteins, calbindin-D-28k and calretinin, in GABA(B(1))(-/-) mice. One month after birth, before the onset of overt epileptiform activity, wild-type (WT) and GABA(B(1))(-/-) mice exhibit comparable expression profiles for the two calcium-binding proteins. Three months after birth, once the epileptic phenotype is established, we observe clear alterations in the expression of calcium-binding proteins in the dentate gyrus area. GABA(B(1))(-/-) mice exhibit a 50% decline in the staining intensity of calbindin-D-28k expressing neurons and a 70% increase in the number of calretinin-positive neurons when compared to WT littermates. Six months after birth, the down-regulation of calbindin-D-28k protein is even more pronounced, while the calretinin expression in GABA(B(1))(-/-) mice reverts to the pattern seen in WT littermates. Our data demonstrate that the absence of functional GABA(B) receptors causes epileptiform activity through a mechanism that crucially involves dentate gyrus granule cells, and that this pathological activity is accompanied by adaptive changes.

Animals↗