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PubMed1994

Vulnerability to excitotoxic stimuli of cultured rat hippocampal neurons containing the calcium-binding proteins calretinin and calbindin D28K.

Rat embryonic hippocampal neurons cultured on astrocyte feeder-layers were sensitive to different excitotoxic stimuli after 10-12 DIV. Almost all neurons (approximately 95%) died within 20 h after a transient exposure for 10 min to 50 microM glutamate, a continuous exposure to either 25 microM NMDA or 250 microM kainate or after a 15-min deprivation of glucose and oxygen. Dizocilpine at 10 microM protected neurons against the glutamate- and NMDA-mediated toxicity as well as against 30 min glucose and oxygen deprivation. However, it failed to protect against kainate toxicity and prolonged glucose/oxygen deprivation (60 min). An additional treatment with CNQX (100 microM) protected neurons even under the latter two conditions. This indicates that the vast majority of neurons was sensitive to different excitotoxic stimuli acting through different types of glutamate receptors leading to calcium overload of the cells which might be the common denominator of triggering cell death under these conditions. Expression of calcium-binding proteins, such as calbindin D28K or calretinin, might increase the intracellular calcium buffer capacity of neurons, thus, rendering them more resistant to calcium overload. Therefore, we analysed whether neurons expressing these calcium-binding proteins would survive these toxic stimuli. Indeed, a small population of the neurons (3-5%) survived, including a subpopulation of calretinin-positive but not calbindin D28K-positive neurons. This implies that the expression of calcium-binding proteins per se does not render neurons more resistant towards these excitotoxic stimuli. Moreover, most of the surviving calretinin-positive neurons showed morphological damage as indicated by loss of neurites. When cytotoxicity due to calcium overload was induced by an exposure of the cells to the calcium ionophore 4-bromo-A23187 rather than by activation of glutamate receptors, calretinin-positive cells were found not to be significantly more resistant than the vast majority of neurons. This may indicate that the lower sensitivity of a subpopulation of calretinin-positive neurons to excitotoxic stimuli may be due to a lower expression of glutamate receptors.

6-Cyano-7-nitroquinoxaline-2,3-dione↗
PubMed1995

Region-specific alterations of calbindin-D28k immunoreactivity in the rat hippocampus following adrenalectomy and corticosterone treatment.

The aim of this study was (i) to compare the immunocytochemical distribution of the calcium-binding protein calbindin-D28k (CB) in the hippocampus of rats with the pattern of neurodegeneration following adrenalectomy (ADX) using silver impregnation, and (ii) to investigate the CB-immunoreactivity in the hippocampus following 3 weeks corticosterone treatment. 24 h following ADX no degenerative changes, nor alterations in CB-immunoreactivity were found in the hippocampus. Both 3 and 21 days following ADX neurodegeneration in the dentate gyrus could be observed which was accompanied with a loss of CB-immunoreactive (CB-ir) cells in that parts of the dentate gyrus suffering neuronal degeneration. Additionally we observed a marked loss of CB-ir in the CA1 area both 3 and 21 days following ADX. Three weeks daily corticosterone treatment (10 mg/day) induced a marked increase of CB-ir exclusively in the CA1 pyramidal cell layer. We conclude that (i) there is a close relationship between the loss of CB-immunoreactive cells in the DG and the neuronal degeneration in the dentate gyrus following ADX, and (ii) corticosterone appears to be involved in the regulation of calbindin-D28k in the CA1 pyramidal cell layer.

Adrenalectomy↗
PubMed1996

Partial coexistence of neuropeptide Y and calbindin D28k in the trigeminal ganglion following peripheral axotomy of the inferior alveolar nerve in the rat.

Immunohistochemistry was applied to examine the correlation between neuropeptide Y (NPY) and the two calcium binding proteins (CaBPs) parvalbumin (PV) and calbindin D28k (CB) in the trigeminal ganglion following peripheral axotomy of the inferior alveolar nerve (IAN) in the rat. Five days following transection and application of FluoroGold (FG) to the cut end of the IAN, approximately 14.8% (80/539) and 18.6% (90/483) of FG-labeled IAN neurons in the trigeminal ganglion showed PV-like immunoreactivity (-LI) and CB-LI, respectively. The mean +/- S.D. area of FG-labeled PV-like immunoreactive (-IR) cells (FG/PV-IR cells) and FG/CB-IR cells were 835.9 +/- 303.1 mu m2 and 712.7 +/- 246.0 mu m2, respectively. FG/PV-IR cells were significantly larger than FG/CB-IR cells. Fourteen days following peripheral axotomy of the IAN, NPY-LI appeared in the medium- to large-sized cells. Double immunostaining revealed that approximately 3.3% (52/1569) of NPY-IR cells in the axotomized trigeminal ganglion displayed PV-LI, while approximately 26.7% (371/1392) of NPY-IR cells displayed CB-LI. The mean +/- S.D. cross-sectional areas of PV-IR and CB-IR trigeminal ganglion cells displaying NPY-LI were 819.5 +/- 265.6 mu m2 and 766.5 +/- 279.7 mu m2, respectively. There were no significant differences in the cross-sectional areas either between NPY/PV-IR cells and NPY/CB-IR cells, or between FG/PV-IR cells and NPY/PV-IR cells, or between FG/CB-IR cells and NPY/CB-IR cells. The present results indicate that injury-evoked medium- to large-sized NPY neurons were a different population from large-sized PV neurons, and NPY was partly co-localized with CB.

Animals↗
PubMed1996

The presence of calbindin in rat cortical neurons protects in vitro from oxydative stress.

Free radicals are highly reactive chemicals containing an unpaired electron and are normally produced by the cellular metabolism. The oxydative stress is defined as a lack of balance between the production of free radicals and the activity of antioxydant metabolites. It induces cellular damages to lipids, proteins and membranes. Abnormal calcium metabolism can be a consequence of oxydative stress leading to increased intracellular concentrations. Calbindin D28K is a calcium binding protein which could have a neuroprotective action against various cellular insults. In this study rat cortical cell cultures were exposed during various times and at different concentrations to the couple Xanthine/Xanthine oxydase (XA/XO), which produces the superoxyde radical O2-.. Neuronal survival revealed that XA/XO is toxic for cortical cell cultures. The Calbindin D28K immunocytochemical study shows that the percentages of Calbindin positive cells are greater in surviving neurons following the XA/XO exposure compared to controls. There is a time-dependent and a dose-dependent relation between the number of surviving neurons and the percentage of Calbindin positive neurons. These results suggest that the presence of cytosolic neuronal Calbindin D28k is associated with a greater resistance to oxydative stress.

Animals↗
PubMed1985

Involvement of spot 35 protein, a cerebellar protein, in modulation of Purkinje cell activity of the rat cerebellum.

Spot 35 protein, applied iontophoretically, produced inhibition of spontaneous Purkinje cell activity in most cells and augmented the NE- or 5-HT-induced inhibition of spontaneous discharges whereas it hardly affected the inhibitory response of Purkinje cells to GABA, taurine, and beta-alanine, and the excitatory response to glutamate. It is suggested that spot 35 protein may be involved in normal physiological operation of the cerebellum through modulation of the NE or 5-HT system.

Action Potentials↗
PubMed1992

Calbindin D-28k and parvalbumin immunohistochemistry in developing rat retina.

The developmental profiles of two calcium-binding proteins, calbindin-D28k (CaBP) and parvalbumin (PV), were investigated immunohistochemically in the developing rat retina. CaBP-immunoreactivity appeared first on embryonic day 17 in the horizontal, amacrine and ganglion cells; on embryonic day 21 in the inner plexiform layer; and on post-natal day 6 in the outer plexiform layer. The reaction intensity had increased to its maximum level by post-natal day 10. PV-immunoreactivity was first noted on embryonic day 19 in the amacrine and ganglion cells and reached its maximum on post-natal day 10. Two distinct subpopulations of amacrine cells were clearly recognized after post-natal day 6; one was positive for CaBP and the other for PV. Some morphological differences were noted between the two.

Animals↗
PubMed1985

The developmental changes of mRNA levels for a cerebellar protein (spot 35 protein) in rat brains.

Our previous papers described a protein called spot 35 found in the cerebellar cytosol of adult rats by two-dimensional gel electrophoresis and localized in the Purkinje cells by immunohistochemical methods. Here we describe the biosynthesis of this spot 35 protein using a reticulocyte lysate cell-free system containing rat cerebellar mRNA. The developmental changes of mRNA-dependent protein biosynthesis were also examined. During postnatal 10-30 days, a rapid increase of mRNA levels for spot 35 protein was observed. The application of the new 45Ca-binding assay procedure revealed that this protein is a Ca-binding protein.

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↗
PubMed1991

Intestinal and renal calcium-binding protein in rats with experimental short bowel syndrome.

Intestinal calcium-binding protein (calbindin-D9K) and renal calcium-binding protein (calbindin-D28K) levels were measured by enzyme-linked immunoadsorbent assays in rats with short bowel syndrome induced by resection of about 85% of the small intestine. Rats with short bowel syndrome had significantly lower mucosal concentrations of calbindin-D9K (P less than 0.001) and a parallel reduction of both intestinal calcium absorption (P less than 0.001) and p-1,25-dihydroxyvitamin D (P less than 0.01) in spite of a general hypertrophy of the duodenal mucosa. Interestingly, the renal concentration of calbindin-D28K was significantly elevated (P less than 0.05) in rats with short bowel syndrome, a change apparently related to factors independent of vitamin D.

Animals↗
PubMed1992

Vitamin D and mineral deficiencies increase the plasma membrane calcium pump of chicken intestine.

The basolateral membrane of the enterocyte was previously shown to contain an adenosine triphosphate-dependent calcium pump. Using immunological procedures, the localization of the Ca2+ pump in chick intestine, and the effect of dietary variables on the concentration of the pump, were studied. A monoclonal antibody produced against the human erythrocyte calcium pump was shown to cross-react with a chick intestinal Ca2+ pump epitope. The most intense staining of intestinal tissue, as determined immunohistochemically, occurred at the basolateral membrane of the duodenum, jejunum, ileum, and colon, with minor staining elsewhere. By the Western blotting procedure, vitamin D repletion of vitamin D-deficient chicks was shown to significantly increase the concentration of the Ca2+ pump epitope of duodenal, jejunal, and ileal mucosa by a factor of 2-3. Chicks were also fed diets deficient in calcium or phosphorus, a situation known to result in the stimulation of the synthesis of calbindin-D28k and an enhancement of the efficiency of Ca2+ absorption. Adaptation of the chicks to these deficient diets was verified by an increase in intestinal levels of calbindin-D28k, and is now shown to increase the Ca2+ pump epitope. From these immunological studies, it seems apparent that dietary variables that enhance intestinal Ca2+ absorption also increase the amount of the intestinal basolateral Ca2+ pump.

Animals↗
PubMed1993

Calretinin and calbindin-D28k immunoreactivity in the human gastrointestinal tract.

BACKGROUND: Calretinin and calbindin-D28k are similar Ca(2+)-binding proteins previously described in specific central neurons and other cells. METHODS: The immunocytochemical distribution of these two proteins was studied in the human gastrointestinal tract. RESULTS: In gastric and small intestinal endocrine cells, calbindin-D28k immunoreactivity was confirmed, but calretinin immunoreactivity was not found. Nerve cell bodies in both submucous and myenteric ganglia were immunoreactive for calbindin (13% and 38% of total cells, respectively) or calretinin (23% and 21%), some containing both proteins. In nerve processes, calretinin was generally more abundant than calbindin and was found particularly around blood vessels. Calretinin co-localized with immunoreactive vasoactive intestinal peptide, neuropeptide Y, galanin, or substance P in submucous ganglion cells and with substance P in myenteric cells. Calbindin-D28k colocalized with fewer peptides, specifically vasoactive intestinal peptide or galanin in submucous cells. By 8 weeks of fetal development, discrete neuronal localizations for both proteins and for calbindin-D28k in endocrine cells were apparent. CONCLUSIONS: In the enteric neuroendocrine system, calretinin and calbindin-D28k are useful markers that may help elucidate Ca(2+)-mediated functions in health and disease.

Adult↗
PubMed1993

Calbindin D28K expression in transfected mouse NIH3T3 cells.

Calbindin D28K (formerly known as vitamin D-dependent calcium binding protein and referred to here as calbindin) is found in a wide variety of tissues, but only in certain cells within those tissues. Apart from its ability to bind calcium, nothing is known about its function in these cells. To investigate its role we have transfected the chick calbindin cDNA into mouse NIH3T3 fibroblasts and established a new cell line where calbindin is permanently expressed. Immunofluorescence studies show that calbindin is distributed throughout the cytoplasm, and treatment of the cells with cycloheximide shows that it has a relatively long half-life within the cell. Measurements of intracellular calcium concentration using Fura-2 suggest that the presence of calbindin within the cells does not affect the increase in intracellular calcium levels which occurs in response to serum stimulation or the rate at which these return to the basal level, but that it may act as a buffer for the entry of extracellular calcium.

3T3 Cells↗
PubMed1994

A comparative study of the calcium-binding proteins calbindin-D28K, calretinin, calmodulin and parvalbumin in the rat spinal cord.

Comparison of the immunocytochemical localizations revealed distinct patterns of differential distribution and overlapping of calbindin-D28K (CB-D28K), calretinin (CR), calmodulin (CM) and parvalbumin (PV) in the rat spinal cord. In some areas, one of the four calcium-binding proteins (CBPs) appears to be predominant, for example, CB-D28K in lamina I and ependymal cells, PV at the inner part of laminae II, CR in laminae V and VI and CM in motoneurons of lamina IX. In other regions of the spinal cord, more than one CBPs was abundant. CB-D28K and CR were similarly distributed in lamina II and the lateral spinal and cervical nucleus; CM and PV were similarly abundant in the ventromedial dorsal horn, internal basilar and central cervical nucleus; CR and PV were similarly abundant in the ventromedial dorsal horn, internal basilar and central cervical nucleus; CR and PV were similarly heterogeneous in the gracile fasciculus from caudal to rostral spinal cord. In the sacral dorsal gray commissure, the distribution patterns of CR and PV were clearly complementary. The unilateral ganglionectomies resulted in a substantial reduction of CBP-like immunoreactivity (CBP-LI) in the dorsal columns and a reduction of CM- and PV-LI in the ventromedial dorsal horn. In the motor system, only CM labeled large motoneurons in lamina IX and CB-D28K lightly stained pyramidal tract. The apparent absence of CM-LI in the superficial dorsal horn is contradictory to the presence of a CM-dependent nitric oxide synthase in the region. These data indicate that most CBP-LI in the dorsal column pathway had primary afferent origin, while the superficial dorsal horn exhibited intrinsic CBP immunoreactivity. The differential and selective localizations of CBPs in the spinal cord suggest a role for these proteins in spinal nociceptive processing, visceral regulation and dorsal column sensory pathways.

Animals↗
PubMed1995

A simple method for quantifying changes in neuronal populations in primary cultures of dissociated rat brain.

A simple method which allows easy quantification of neuronal and glial sub-populations in primary neuronal tissue culture is described. The method takes advantage of the fact that the staining of neuronal and glia nuclei with Hoechst 33258 is distinctive and characteristic of the cell type. Double-staining experiments show that only cells with nuclear staining characteristic of neurones are immunopositive for neuronal markers. There is no obvious difference between neurones from different regions of the brain nor any apparent differences in nuclear staining of neurones of different sizes. This method is particularly useful for the quantification of neurones in cultures where neurones are growing on glial beds or where the neurones are growing in clusters. Further, it eliminates the need to double-stain cultures with neuronal markers in order to calculate neuronal sub-populations. We have used this technique to examine the effect of time in vitro on the proportion of calbindin D28K-positive neurones in striatal cultures. We show that with increasing time in culture, there is a significant increase in the percentage of neurones which express calbindin D28K. This supports the suggestion that calbindin D28K may be important for promoting the survival of neurones in which it is expressed.

Animals↗
PubMed1996

Triple immunofluorescence labelling of parvalbumin, calbindin-D28k and calretinin in rat and monkey brain.

This study presents novel techniques for the concomitant cytochemical detection of the calcium-binding proteins parvalbumin, calbindin-D28k and calretinin which are frequently used neuronal markers. For the triple immunofluorescence labelling of such antigens in rat and monkey brain--with emphasis on the cortex--we developed four different protocols which revealed obviously identical distribution patterns in consecutive sections. These methods included the simultaneous use of purified monoclonal antibodies directed against parvalbumin and calbindin--D28k--haptenized with biotin or digoxigenin--and subsequent visualization with fluorochromated hapten-recognizing immunoreagents. For the combined visualization of the calcium-binding proteins we applied the bright red fluorescent carbocyanine Cy3, blue fluorescent 7-amino-4-methylcoumarin-3-acetic acid (AMCA) and as green fluorophore either fluorescein or the newly introduced carbocyanine Cy2. The latter showed a higher fluorescence intensity and more resistance against photobleaching than fluorescein. In addition to clearly distinguished distribution patterns of the calcium-binding proteins, neurons co-expressing parvalbumin and calbindin-D28k in the parietal and piriform cortex of rat were demonstrated. The elaborated methods might stimulate the further detailed investigation of spatial and functional relationships between structures immunopositive for selected neuroanatomical markers.

Animals↗
PubMed1991

Transient appearance of immunoreactivity for Ca-binding protein (spot 35-calbindin) in small principal neurons in the superior cervical ganglion of pre-weanling rats.

Immunoreactivity for rat cerebellar calbindin, termed spot 35-calbindin, is transiently expressed largely in numerous small principal neurons of the superior cervical ganglion in pre-weanling rats and disappears by the fourth postnatal week. Preganglionic denervation results in a slower rate of disappearance of the immunoreactivity in ganglion neurons. This finding suggests that small principal neurons in the superior cervical ganglion may exert some yet to be determined Ca-mediated functions that are not shared with larger neurons at the pre-weanling stage.

Animals↗
PubMed1986

An immunohistochemical study on the ontogeny of cells immunoreactive for spot 35 protein, a novel Purkinje cell-specific protein, in the rat cerebellum.

A time course study on the appearance and distribution of cells immunoreactive for spot 35 protein, a novel cerebellar Purkinje cell-specific protein, was conducted in the developing cerebella of fetal and early postnatal rats by PAP immunohistochemistry. Spot 35-immunoreactive cells were first noted in the cerebellar anlage on the 17th embryonic day, appearing as large cellular aggregations in the mantle layer and a small number of elongated cells dispersed between the cell aggregations and the ependymal layer. As the development proceeded, the spot 35-immunoreactive cells gradually accumulated beneath the external granular layer. At birth, they were arranged compactly in 4-5 irregular rows to form a primitive Purkinje cell layer. During their subsequent development, immunostaining for spot 35 protein demonstrated the rearrangement of the Purkinje cells into a single row and the maturation of their somata, axons and dendrites. All these findings indicate that spot 35 protein is a specific marker for the cerebellar Purkinje cells, from their migrating stage throughout the course of their maturation. The present study further describes the transitory lamellar arrangement of spot 35-immunoreactive Purkinje cells located horizontally at a short distance away from the ependymal layer of the cerebellum on the 17th embryonic day.

Animals↗
PubMed1991

Postnatal development of calbindin and parvalbumin immunoreactivity in the thalamus of the rat.

The maturation of the calcium binding proteins calbindin-D28k (CB) and parvalbumin (PV) during the first 3 postnatal weeks was studied in the rat thalamus using immunohistochemistry. These two proteins display a non-homogeneous distribution in the adult thalamus. In the rat, CB is mainly localized in the neurons and neuropil of the thalamic midline, intralaminar, and ventromedial nuclei, as well as in the posterior complex. At birth, CB-immunoreactive cell bodies were evident in thalamic midline structures, and especially in the nucleus reuniens. The number of thalamic CB-positive cell bodies, as well as the intensity of the neuropil immunostaining, increased progressively in the first postnatal weeks. This quantitative increase was first apparent in the midline structures and then in the other thalamic territories which are CB-positive in adulthood, and followed a mediolateral gradient. The mature pattern was achieved by the end of the third postnatal week. In the adult rat thalamus the neurons of the reticular nucleus display PV-immunostaining and PV-positive fibers densely innervate most of the dorsal thalamic domains. PV-immunoreactivity was clearly evident at birth in the cell bodies of the reticular nucleus. The density of PV-containing fibers increased progressively after birth in the dorsal thalamus, with a lateromedial gradient. At the end of the third postnatal week the ventroposterior (VP) complex appeared heavily innervated by PV-positive fibers, whose density in more medial structures was still lower than in the adult thalamus. A transient hyperinnervation of PV-immunoreactive fibers, displaying a dishomogenous organization in distinct segments, was observed in VP, and especially in the ventroposteromedial nucleus, during the second postnatal week. Altogether these findings indicate that the maturation of CB and PV requires postnatally a relatively prolonged period of time. The possible involvement of these proteins in different functional aspects of thalamic neuronal maturation is discussed.

Animals↗