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PubMed1994

Induction of calbindin-D 28K gene and protein expression by physiological stimuli but not in calcium-mediated degeneration in rat PC12 pheochromocytoma cells.

To understand the role of calbindin-D 28K in neuronal degeneration, we examined its expression in differentiated PC12 cells in response to calcium intoxication, using the ionophore A23187 treatment, that results in cell degeneration and death. We first established that calbindin-D 28K is expressed in PC12 cells. The amounts of calbindin-D 28K mRNA and protein were increased by the differentiation factors, NGF and retinoic acid, but not by vitamin D3. Calbindin-D 28K expression was also significantly up-regulated by stimuli (depolarization, low concentrations of Ca2+ ionophore A23187) which increase intracellular calcium levels within the physiological range. In contrast, the calbindin-D 28K mRNA and protein concentrations were not modulated by high concentrations of A23187, which resulted in cell degeneration and death. Experiments with the antisense oligonucleotides showed that, although the calbindin-D 28K protein levels were decreased significantly, the progression of degenerative changes induced by calcium via A23187, was not altered.

Animals↗
PubMed1995

Calbindin-D28K facilitates cytosolic calcium diffusion without interfering with calcium signaling.

The role of calbindin-D28K, in transcellular Ca2+ transport and Ca2+ signaling in rabbit cortical collecting system was investigated. Rabbit kidney connecting tubules and cortical collecting ducts, hereafter referred to as cortical collecting system, were isolated by immunodissection and cultured to confluence on permeable filters and glass coverslips. Calbindin-D28K was present in the cytosol of principal cells, but was absent from the intercalated cells. 1,25(OH)2D3 (48 h, 10(-7) M) significantly increased cellular calbindin-D28K levels (194 +/- 15%) and stimulated transcellular Ca2+ transport (41 +/- 3%). This stimulatory effect could be fully mimicked by the endogenous Ca2+ chelator, BAPTA (30 microM BAPTA/AM), which suggests that the presence of Ca2+ chelators alone is sufficient to enhance transcellular Ca2+ transport. Stimulation of Ca2+ transport was not accompanied by a rise in [Ca2+]i. Isosmotic replacement of extracellular Na+ ([Na+]o) for N-methylglucamine (NMG) generated oscillations in [Ca2+]i in individual cells of the monolayer. The functional parameters of these oscillations such as frequency of spiking, resting [Ca2+]i, increase in [Ca2+]i and percentage of responding cells, were not affected by the level of calbindin-D28K. In contrast, loading the cells with BAPTA abruptly stopped these [Ca2+]i oscillations. This suggests that the kinetics of Ca2+ binding by calbindin-D28K are slow relative to the initiation of the [Ca2+]i rise, so that calbindin-D28K, unlike BAPTA, is unable to reduce [Ca2+]i rapidly enough to prevent the initiation of Ca(2+)-induced Ca2+ release.

Animals↗
PubMed1992

Localization of calbindin D28K-like immunoreactivity in fish gill: a light microscopic and immunoelectron histochemical study.

The presence of calbindin D28K in fish (Heteropneustes fossilis) gill was studied by use of specific antibodies raised against chick duodenal 28 kDa calbindin in immunoperoxidase and electron-microscopic labelling experiments. Immunoreactivity for calbindin D28K, which has been observed in the intestine of a number of avian and mammalian species, is reported for the first time in the gill. It was primarily located in neuroendocrine (NE) cells. Some immunoreactivity was also located in the glycocalyx of the non-endocrine cells, i.e., the pavement cells, which have ultrastructural characteristics quite different from those of endocrine cells. The calbindin-immunopositive NE cells were ascertained in both gill filamental and lamellar epithelium. All the NE cells contained secretory granules as the most distinctive feature of these cells. Ultrastructurally, two types of NE cells were distinguished according to the morphology of their secretory granules. The calbindin immunoreactivity in the NE cells was stimulated when the calcium concentration of the ambient water was reduced. The present findings suggest that NE cells exert some as yet unidentified function related to calcium-mediated processes involving the expression of calbindin.

Animals↗
PubMed1992

Reduction of vitamin D hormone receptor mRNA levels in Alzheimer as compared to Huntington hippocampus: correlation with calbindin-28k mRNA levels.

Receptors for vitamin D hormone (VDR) and the calcium binding protein, calbindin-28k, have been localized in many tissues, including brain. In brain, VDR and calbindin-28k were reported to colocalize in hippocampal CA1 cells. We have shown that mRNA pool size for calbindin-28k was reduced, on average, by 35% in Alzheimer hippocampal CA1 cells, as compared to Huntington control (manuscript in preparation). In the present study, in situ hybridization with tritiated antisense RNA probes was used to examine VDR expression in paired Alzheimer and Huntington brain tissue. Message levels for VDR were reduced, on average, by 34% and 31%, respectively, in Alzheimer hippocampal CA1 and CA2 pyramidal cells, as compared to Huntington control. However, VDR message levels were not significantly different from control in Alzheimer temporal cortex or cerebellum. There was no correlation between VDR message levels and brain weight, autopsy interval, patient age or the extent of neurofibrillary degeneration. Instead, VDR mRNA pool size in hippocampal CA1 cells correlated significantly with calbindin-28k message levels (r = 0.52, P less than 0.001). Decreased message levels for VDR and calbindin-28k in these cells were due to an increased percentage of cells expressing lower message levels for these proteins. These results show that in Alzheimer hippocampal CA1 cells, VDR mRNA pool size is downregulated and that this downregulation may play a role in the reduction of calbindin-28k expression.

Alzheimer Disease↗
PubMed1992

Noncytoplasmic and filamentous appearance of calbindin-D28k and tubulin in double, indirect immunofluorescent staining of embryonic chick tissue.

Double indirect immunofluorescent labeling of embryonic chick tissue was undertaken for the vitamin D-induced calcium binding protein, calbindin-D28k, and microtubules. Immunoreactivities for both calbindin-D28k and tubulin were found to exhibit a filamentous staining pattern in mesonephros, metanephros, intestine, and brain. In the intestine, staining was absent at 19 days, while immunolabeling of tubulin became evident at 20 days, and both antigens were present in 21-day tissue. In intestinal epithelium, as well as in 10-day metanephros, it was strikingly evident that cells either stained for both antigens or were negative for both calbindin-D28k and tubulin. In 11-12-day metanephros, an increased number of cells with both immunoreactivities were found. In 15-17-day brain, tubulin was evident within all cells but stained most intensely in Purkinje cells which were also positive for calbindin-D28k. Mesonephros from 4-5-day embryos revealed immunolabeling of both tubulin and the calcium binding protein. A statistical analysis of the various cell types revealed that the vast majority contained either both antigens or neither of the immunoreactivities. Of the more than 600 cells scored, none were found to be positive for calbindin-D28k, while at the same time negative for tubulin. It is concluded that calbindin-D28k exhibits a noncytoplasmic distribution in all tissues tested and that the filamentous appearance may reflect localization of the antigen in tubulo-vesicular organelles associated with cytoskeleton.

Animals↗
PubMed1993

Calbindin D-28K distribution in the retina of the developing trout (Salmo fario L.).

The appearance of calbindin D-28K, a calcium-binding protein, during development of the trout retina was studied by immunohistochemistry. The first calbindin immunoreactive cells appear in the inner nuclear layer at the equator of the embryonic retina at the stage 227 degrees C (around embryonic day 15). Just before hatching, stage 440 degrees C (around embryonic day 30) cells located in the ganglion cell layer and inner nuclear layer, expressed calbindin. This pattern of immunoreactivity was conserved in post-embryonic retinae (alevins 15 days old). In adult retinae the ganglion cells showed a faint immunoreaction; the amacrine cells are markedly fewer and their immunoreaction declined; and the bipolar cells expressed calbindin for the first time. The results obtained in the present work attending to the expression of calbindin, generally conforms with the vitreal to scleral progression of differentiation of the teleost retina. Ganglion, amacrine and bipolar cells undergo further maturation after beginning calbindin expression.

Animals↗
PubMed1991

Calbindin-D-28k-like immunoreactive structures in the olfactory bulb and anterior olfactory nucleus of the human adult: distribution and cell typology--partial complementarity with parvalbumin.

Calbindin-D-28k and parvalbumin are calcium-binding proteins. The laminar distribution and morphological features of calbindin-D-28k-like immunoreactive structures were studied in 60-microns-thick sections of the human olfactory bulb. Except for the olfactory nerve layer, immunoreactive neurons were present in all layers of the olfactory bulb. They reached highest densities in the external plexiform layer and internal granule cell layer. Considerable numbers of calbindin-like nerve cells were also found in the olfactory tract and in distal portions of the anterior olfactory nucleus. When comparing the distribution of calbindin-positive structures to that of parvalbumin-positive ones a partially complementary distribution pattern was found. Calbindin-like immunoreactive portions of the anterior olfactory nucleus and olfactory tract were mirrored by immunonegative areas in adjacent sections stained for parvalbumin. Using the combined pigment-Nissl procedure we observed the presence of lipofuscin deposits in nearly 80% of all the calbindin-immunoreactive neurons analysed. Moreover, analysis of their lipofuscin deposits rendered the further differentiation of morphologically similar neuronal subpopulations possible. In contrast, all parvalbumin-like immunoreactive neurons remained free of lipofuscin granules.

Adult↗
PubMed2006

Calbindin D9k is not required for 1,25-dihydroxyvitamin D3-mediated Ca2+ absorption in small intestine.

The exact role of calbindin D9k in vitamin D-mediated calcium absorption has been debated but remains unsettled. In 129/OlaHsd mice, calbindin D9k was found highest in duodenum (36-50%) and kidney (24-34%) followed by stomach, lung and uterus. Age does not affect the relative distribution of calbindin D9k but it does decline with age in duodenum of both male and female 129/Ola mice. Recently, we produced a null calbindin D9k mutant 129/OlaHsd mouse; this mouse proved to be indistinguishable from the wild-type in phenotype and in a serum calcium level regardless of age or gender. We have now examined directly whether the mutant mouse can absorb calcium from the intestine in response to the active form of vitamin D. The calbindin D9k null mutant mouse is fully able to absorb calcium from the intestine in response to 1,25-dihydroxyvitamin D3. It is, therefore, clear that calbindin D9k is not required for vitamin D-induced intestinal calcium absorption.

Absorption↗
PubMed2005

Reduced density of calbindin-immunoreactive interneurons in the planum temporale in schizophrenia.

Reduced density of calbindin-containing interneurons in the prefrontal cortex in schizophrenia has been reported (Beasley et al 2002; Biol Psych 52:708-715). Calbindin is a calcium-binding protein (CBP) present in a subpopulation of GABAergic neurons restricted mainly to layer II of the cortex. A paraffin-embedded, 10-mum-thick section from the planum temporale (PT) of each hemisphere was prepared from 12 patients with schizophrenia and 12 controls. Calbindin-containing cells were stained using an antibody (D-28K). Counting frames were superimposed to sample within layer II of the PT. A bilateral reduction (20%) in calbindin cell density was found in patients (controlling for fixation time). Furthermore, mean calbindin cell cross-sectional area was increased in female patients and reduced in male patients. Reduced CBP expression (reducing the excitability of interneurons) or reduced number of CBP-containing cells may cause disinhibition of pyramidal cells. The majority of calbindin-containing cells in the mature brain are double-bouquet cells with vertically oriented dendrites and axon bundles. By exercising inhibitory modulation of pyramidal cells in a columnar arrangement, they make possible cohesive vertical inhibition of minicolumns. Loss of columnar inhibition may result in reduced minicolumnar segregation and altered cell size may reflect altered minicolumn size.

Adult↗
PubMed2005

Distribution of GABA, calbindin and nitric oxide synthase in the developing chick entopallium.

The distribution of GABA, calbindin and neuronal nitric oxide synthase (nNOS) was analyzed in the developing avian entopallium. The study was carried out in chick embryos from embryonic day (E)8 to hatching postnatal day (P)0, using immunohistochemical methods. At E8, GABA-positive cells were observed in pallial regions. Neither calbindin nor nNOS-immunoreactive cells were observed. At E10, the number of GABA neurons in the prospective entopallium increased and also nNOS cells were observed. Lightly stained nNOS neurons predominated over intensely stained ones. Calbindin immunoreactivity was not observed in the entopallium. At E12, the entopallial complex appeared as the pallial region displaying the highest density of GABA neurons. Also the whole entopallium displayed an intensely stained calbindin neuropil with many embedded stained cells. From E12 on, there was a decrease in the expression of nNOS. At E14-16, both GABA and calbindin-immunoreactive neurons were numerous and homogeneously distributed within the entopallium. The whole entopallium displayed a moderately stained neuropil. From E18 to P0, GABA and nNOS immunoreactivities remained similar to previous stages. At these stages, calbindin immunoreactivity within the entopallium consisted of a moderately stained central region bordered dorsally by a pale stained region. These two areas could correspond to the entopallial core and the perientopallial belt, respectively.

Age Factors↗
PubMed2005

Subpallial origin of part of the calbindin-positive neurons of the claustral complex and piriform cortex.

The aim of the present study was to investigate whether part of the calbindin-positive neurons of the claustral complex and piriform cortex originate in the subpallium. To that end, we prepared organotypic cultures of embryonic telencephalic slices, and applied the cell tracker CMTMR to the ventricular/subventricular zone of the lateral or medial ganglionic eminence. Following 48 h of incubation, we observed a number of CMTMR-labeled cells (showing red fluorescence) of subpallial origin in the claustral complex and piriform cortex. To know whether some of these cells of subpallial origin were calbindin-positive, we performed immunofluorescence for calbindin using an Alexa 488-conjugated secondary antiserum (green fluorescence). Our results showed that some of the CMTMR-labeled cells of subpallial origin in the claustral complex and piriform cortex are calbindin-positive (and possibly GABAergic). The subpallial origin of part of these cells was confirmed by observation of double labeled neurons in the claustral complex that expressed both Lhx6 mRNA (a marker of cells derived from the medial ganglionic eminence) and calbindin. Future studies will be required to analyze the existence of a subpopulation of non-GABAergic calbindin cells in the claustral complex and piriform cortex, and to know their origin.

Animals↗
PubMed2004

Ontogeny of two calcium-binding proteins (calbindin D-28K and parvalbumin) in the human inferior olivary complex and their distribution in the adults.

The inferior olivary complex (IOC) is a prominent nuclear relay system of the medulla oblongata. Anatomically, it is connected to the cerebellum for coordination of motor activities. Calbindin D-28K (CALB) and parvalbumin (PV) are cytosolic calcium-binding proteins (CBP) that play a role in Ca2+ homeostasis. We examined their ontogeny and distribution in the fetal, postnatal and adult human IOC by immunohistochemistry. At 11-12 weeks of gestation (wg), calbindin immunoreactivity was present in the principal olive and the medial accessory olive, it was absent in the dorsal olive. Parvalbumin immunoreactivity developed at 16-17 wg in the ventral lamella and the lateral bulge of the principal olive only. Calbindin expression gradually increased from 20 to 37 wg, whilst by contrast, parvalbumin expression was moderate. By 37 wg, all three IOC subnuclei were immunopositive for both proteins. In a 3-month-old infant, parvalbumin was intensely developed in the olivary axons. In the adults (40- to 59-year-old), calbindin was distributed in most neurons, and olivocerebellar fibres, whereas parvalbumin was present in some neurons and few fibres. Parvalbumin expressed till 51 years, and disappeared by 59 years of age. Calbindin immunoreactivity in the olivary axons was declined at 70 years of age. The data suggest a differential distribution and requirement of these proteins in the human IOC maturation. It may be that the IOC utilizes mainly calbindin for Ca2+ buffering. The loss of parvalbumin with ageing might influence the excitability of the spared IOC neurons.

Adult↗
PubMed2003

Calbindin expression in the hamster suprachiasmatic nucleus depends on day-length.

The mammalian circadian clock located in the suprachiasmatic nucleus (SCN) of the hypothalamus controls many physiological and behavioral rhythms. The SCN is compartmentalized in two functionally distinct subregions: a dorsomedial subregion that rhythmically expresses clock genes, and a ventrolateral subregion which, in contrast, mainly expresses clock genes at a constant level. In the golden hamster, this ventrolateral part of the SCN contains a subpopulation of neurons expressing calbindin D28k. This subpopulation has recently been implicated in the control of locomotor rhythmicity. Because both the pattern and level of locomotor activity are affected by day-length, we investigated whether photoperiod also affects calbindin expression. We show that calbindin expression is negatively correlated to the day-length. The number of calbindin immunopositive neurons and calbindin mRNA levels were markedly increased in hamsters exposed to short photoperiods (light/dark cycle [LD] 6:18 and LD10:14) when compared with hamster exposed to long photoperiods (LD18:6 and LD14:10). This suggests that calbindin neurons are involved in the encoding of seasonal information by the SCN.

Animals↗
PubMed2004

Non-serotonergic dorsal and median raphe projection onto parvalbumin- and calbindin-containing neurons in hippocampus and septum.

The median raphe nucleus is involved in controlling and maintaining hippocampal activity through its projection to inhibitory neurons in medial septum and hippocampus. It has been shown that anterogradely axonal-traced fibers originating in the median raphe nucleus project onto calbindin-containing neurons in hippocampus and parvalbumin-containing neurons in medial septum. Parallel immunohistochemistry studies showing serotonin fibers contacting calbindin- and parvalbumin-positive neurons have led to the assumption that raphe fibers projecting on these types of neurons are mainly serotonergic. However, in both dorsal and median raphe nucleus there is a large amount of non-serotonergic neurons which also are projecting neurons, indicating that a part of the raphe fibers projecting to hippocampus and septum may be non-serotonergic. Our aim was to determine whether there is a non-serotonergic projection from the raphe nucleus onto calbindin- and parvalbumin-containing neurons in hippocampus and septum. Biotin dextran amine was used as the anterograde neuronal tracer and injected into either dorsal or median raphe nucleus. By use of triple immunofluorescence-labeling we analyzed the serotonergic content of the biotin dextran amine-labeled fibers contacting parvalbumin- and calbindin-positive neurons. Surprisingly, we found a significant non-serotonergic projection from both dorsal and median raphe nuclei onto calbindin- and parvalbumin-containing interneurons in septum and hippocampus, with a preference in hippocampus for projecting onto calbindin-positive neurons. These results indicate that the raphe nuclei may exert their control on hippocampal and septal activity not only through a serotonergic projection, but also through a significant non-serotonergic pathway.

Animals↗
PubMed2003

The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.

Calbindin D(28K) is a six-EF-hand calcium-binding protein found in the brain, peripheral nervous system, kidney, and intestine. There is a paucity of information on the effects of calcium binding on calbindin D(28K) structure. To further examine the mechanism and structural consequences of calcium binding to calbindin D(28K) we performed detailed complementary heteronuclear NMR and microelectrospray mass spectrometry investigations of the calcium-induced conformational changes of calbindin D(28K). The combined use of these two powerful analytical techniques clearly and very rapidly demonstrates the following: (i). apo-calbindin D(28K) has an ordered structure which changes to a notably different ordered conformation upon Ca(2+) loading, (ii). calcium binding is a sequential process and not a simultaneous event, and (iii). EF-hands 1, 3, 4, and 5 take up Ca(2+), whereas EF-hands 2 and 6 do not. Our results support the opinion that calbindin D(28K) has characteristics of both a calcium sensor and a buffer.

Apoproteins↗
PubMed1998

The cyclosporine A-induced decrease in rat renal calbindin-D28kDa protein as a consequence of a decrease in its mRNA.

Cyclosporine A (CsA) is a potent immunosuppressant with the drawback of renal side-effects. We recently reported that relatively high doses of CsA markedly decreased the calcium-binding protein calbindin-D28kDa in kidneys of male Wistar rats, and showed that this decrease could be associated with some of the drug-induced adverse renal effects. To investigate the events leading to this decrease, the calbindin-D28kDa mRNA level in kidneys of rats treated with 15 or 50 mg/kg/day CsA for 12 days was analysed by reverse transcription followed by polymerase chain reaction. At both doses, a marked dose-dependent decrease in the calbindin-D28kDa mRNA level was found, one very similar to the decrease measured in the calbindin-D28kDa protein abundance. Thus, the CsA-mediated down-regulation of the renal calbindin-D28kDa protein is most likely the result of a decrease in the calbindin-D28kDa mRNA level.

Animals↗
PubMed2002

Spontaneous recurrent seizures after pilocarpine-induced status epilepticus activate calbindin-immunoreactive hilar cells of the rat dentate gyrus.

Although it is now established that neurogenesis of dentate gyrus granule cells increases after experimental seizures, little is currently known about the function of the new granule cells. One question is whether they become integrated into the network around them. Recent experiments that focused on the newly born granule cells in the hilus showed that indeed the new cells appear to become synchronized with host hippocampal neurons [Scharfman et al. (2000) J. Neurosci. 20, 6144-6158]. To address this issue further, we asked whether the new hilar granule cells were active during spontaneous limbic seizures that follow status epilepticus induced by pilocarpine injection. Thus, we perfused rats after spontaneous seizures and stained sections using antibodies to c-fos, a marker of neural activity, and calbindin, a marker of the newly born hilar granule cells [Scharfman et al. (2000) J. Neurosci. 20, 6144-6158]. We asked whether calbindin-immunoreactive hilar neurons were also c-fos-immunoreactive.C-fos was highly expressed in calbindin-immunoreactive hilar neurons. Approximately 23% of hilar cells that expressed c-fos were double-labeled for calbindin. In addition, other types of hilar neurons, i.e. those expressing parvalbumin or neuropeptide Y, also expressed c-fos. Yet other hippocampal neurons, including granule cells and pyramidal cells, had weak expression of c-fos at the latency after the seizure that hilar neuron expression occurred. In controls, there was very little c-fos or calbindin expression in the hilus.These results indicate that calbindin-immunoreactive hilar cells are activated by spontaneous seizures. Based on the evidence that many of these cells are likely to be newly born, the data indicate that new cells can become functionally integrated into limbic circuits involved in recurrent seizure generation. Furthermore, they appear to do so in a manner similar to many neighboring hilar neurons, apparently assimilating into the local environment. Finally, the results show that a number of hilar cell types are activated during chronic recurrent seizures in the pilocarpine model, a surprising result given that many hilar neurons are thought to be damaged soon after pilocarpine-induced status epilepticus.

Animals↗
PubMed2002

Synaptic reorganization of calbindin-positive neurons in the human hippocampal CA1 region in temporal lobe epilepsy.

The distribution, morphology, synaptic coverage and postsynaptic targets of calbindin-containing interneurons and afferent pathways have been analyzed in the control and epileptic CA1 region of the human hippocampus. Numerous calbindin-positive interneurons are preserved even in the strongly sclerotic CA1 region. The morphology of individual cells is altered: the cell body and dendrites become spiny, the radially oriented dendrites disappear, and are replaced by a large number of curved, distorted dendrites. Even in the non-sclerotic epileptic samples, where pyramidal cells are present and calbindin-immunoreactive interneurons seem to be unchanged, some modifications could be observed at the electron microscopic level: they received more inhibitory synaptic input, and the calbindin-positive excitatory afferents - presumably derived from the CA1, the CA2 and/or the dentate gyrus - are sprouted. In the strongly sclerotic tissue, with the death of pyramidal cells, calbindin-positive terminals (belonging to interneurons and the remaining excitatory afferents) change their targets. Our data suggest that an intense synaptic reorganization takes place in the epileptic CA1 region, even in the non-sclerotic tissue, before the death of considerable numbers of pyramidal cells. Calbindin-positive interneurons participate in this reorganization: they show plastic changes in response to epilepsy. The enhanced inhibition of inhibitory interneurons may result in the disinhibition of pyramidal cells or in an abnormal synchrony in the output region of the hippocampus.

Adult↗