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PubMed1994

Induction of enhanced postnatal expression of immunoreactive calbindin-D28k in rat forebrain by the calcium antagonist nimodipine.

The early postnatal development of immunoreactive calbindin-D28k (CaB-ir) containing neuronal systems in hippocampus and parietal cortex was studied in offspring of Wistar rats chronically treated with either the Ca(2+)-channel antagonist nimodipine or placebo food. The drug was applied to the mother animals during the last week of gestation and continued until the end of the experiment. The CaB-ir was investigated in the period of the highest rate of hippocampal and cortical fiber growth at postnatal days (PD), 5, 7, 10 and 20. In the dorsal hippocampus from PD5 to 20, the dentate granule cells and their mossy fiber connection expressed increasing CaB-ir in a topographically organized manner. In the parietal cortex at PD5, 7 and 10 interneurons and a few pyramidal cells gradually appeared immunoreactive for CaB with progressively increasing intensity and approached their adult-like pattern at PD20. Chronic nimodipine treatment resulted in a transient and markedly enhanced ir-CaB expression up to the age of PD10, which was quantified by cell counts and image analysis. Nimodipine induced a more than twofold increase in the number of CaB-ir neurons in the cortex at PD5-PD10. The developmental enhancement in the hippocampus appeared slightly earlier mainly at PD5 and 7. The findings indicate that the antihypoxic effect of nimodipine, previously found in the perinatal age, may be associated with an increased Ca2+ buffering capacity of neurons due to an enhanced expression of ir-CaB during the early postnatal period.

Animals↗
PubMed1994

Expression of calcium-binding proteins in the neurotrophin-3-dependent subpopulation of rat embryonic dorsal root ganglion cells in culture.

In this study we have examined the calcium-binding protein expression in rat embryonic (E16) dorsal root ganglia (DRG) neurons in vitro in the presence of neurotrophin-3 (NT-3). A comparison was made with the expression of calcium-binding proteins in DRG subpopulations that depended in vitro on nerve growth factor (NGF) or brain-derived neurotrophic factor (BDNF). Our results show that NT-3 promotes the survival of a DRG subpopulation of which over 75% expresses parvalbumin (PV). The majority of these PV-positive NT-3-dependent DRG neurons were large 'type A' neurons. Expression of calbindin-D28k (CaBP) and calretinin (Calr) in the NT-3-dependent DRG population was seen in smaller fractions (between 12 and 17%) of the surviving DRG neurons and in both type A and B neurons. The preferential expression of PV in NT-3-dependent type A neurons is unique in comparison to the expression of PV and the other calcium-binding proteins in DRG neurons surviving in vitro in the presence of NGF or BDNF.

Animals↗
PubMed1992

Ontogeny of the distribution and colocalization of calbindin D28K within neural and endocrine cells of the gastrointestinal tract of fetal and neonatal sheep.

Using immunocytochemical techniques we have demonstrated that Calbindin D28K (CaBP) is present in the gastrointestinal tract of ovine fetuses early in development (by day 45). At day 45, CaBP was limited to neuronal elements in the developing intestine. By day 100, CaBP immunoreactivity was abundant in both epithelial endocrine cells and nerves of the submucous and myenteric ganglia. The location of CaBP containing cells and fibers was similar in duodenal sections taken from day 100 and term (145 days), as well as those taken from 24-48 h postnatal lambs. CaBP is colocalized in endocrine cells containing gastrin, glucagon, somatostatin and neurotensin, but not glucose dependent insulinotrophic peptide (GIP). Furthermore, it is extensively colocalized in nerve fibers and cells containing neurotensin but not somatostatin or vasoactive intestinal peptide. The colocalization of CaBP within various endocrine and nerve cells does not change in fetal sheep over the last one-third of gestation and there is no difference between fetal and neonatal sheep.

Animals↗
PubMed1994

Calmodulin, calbindin-D28K and calretinin in rat and chicken pineal glands: immunocytochemical and immunoblotting analysis.

In pineal gland, melatonin is synthesized in pinealocytes. Pharmacological studies using calmodulin antagonists suggested that melatonin synthesis was regulated through calmodulin. However, immunohistochemical studies showed that calmodulin could only be detected in pineal glial cells, and not in pinealocytes. To further investigate this discrepancy, we have tried to detect calmodulin not seen by immunohistochemical methods. We have used rat and chicken pineal homogenate supernatants and Triton X-100-treated pellets denatured by sodium dodecyl sulfate, subjected to electrophoresis and immunoblotting using anti-calmodulin antibodies. Two different IgG (#465 and #860) purified from anti-calmodulin sera were used. In rat pineal homogenate supernatants, calmodulin could be detected by immunoblotting using both antibodies. Some calmodulin could also be detected in the Triton-treated pellet fractions, but no additional cross-reacting bands were detected. However, in both chicken pineal homogenate supernatants and Triton-extracted pellets, in addition to a calmodulin immunoreactive band, two other proteins with approximate molecular masses (M(r)) of 56 kDa and 60 kDa were detected using anti-calmodulin #465. For comparison, similar immunoblot experiments were performed for detection of calbindin-D28K and calretinin, two other calcium binding proteins expressed in different pineal cell populations. Interestingly, Triton extraction of chicken pineal pellets revealed additional bands cross-reacting with each antibody. Anti-calbindin-D28K cross-reacted strongly with a M(r) = 68 kDa protein and weakly with a M(r) = 56 kDa protein. Anti-calretinin cross-reacted strongly with a M(r) = 93 kDa protein and weakly with a M(r) = 56 kDa protein.

Animals↗
PubMed1996

Calcium-binding proteins in primate basal ganglia.

This paper describes the distribution of the calcium-binding proteins calbindin-D28k. Parvalbumin and calretinin in primate basal ganglia. The data derive from immunocytochemical studies undertaken in squirrel monkeys (Saimiri sciureus) and in normal human individuals. In the striatum, calbindin labels medium-sized spiny projection neurons whereas parvalbumin and calretinin mark two separate classes of aspiny interneurons. The striatal matrix compartment is markedly enriched with calbindin while striatal patches (striosomes) display a calretinin-rich neuropil. In the pallidum, virtually all neurons contain parvalbumin but none express calbindin. Calretinin occurs only in a small subpopulation of both large and small pallidal neurons. In the subthalamic nucleus, there exists a multitude of parvalbumun-positive cells and fibers but the number of calretinin and calbindin-positive neuronal elements is small. In the substantia nigra/ventral tegmental area complex, calbindin and calretinin occur principally in dopaminergic neurons of the dorsal tier of the pars compacta and in those of the ventral tegmental area. Parvalbumin is strictly confined to the GABAergic neurons of the pars reticulata and lateralis. Calbindin-rich fibers abound in the pars reticulata and lateralis, while calretinin-positive axons are confined to the pars compacta. These results indicate that calbindin and parvalbumin are distributed according to a strikingly complementary pattern in primate basal ganglia. Calretinin is less ubiquitous but occurs in all basal ganglia components where it labels distinct subsets of neurons. Such highly specific patterns of distribution indicate that calbindin, parvalbumin and calretinin may work in synergy within primate basal ganglia.

Animals↗
PubMed1992

Calbindin-D28K-containing neurons in animal models of neurodegeneration: possible protection from excitotoxicity.

Brain levels of the calcium binding protein Calbindin-D28K (CaBP28K) and CaBP28K mRNA were measured for various animal models of neurodegenerative diseases (MPTP-treated C57BL/6J mice and Sprague-Dawley rats receiving striatal/intraperitoneal kainic acid or quinolinic acid into the nucleus basalis magnocellularis). Brain areas were tested (radioimmunoassay, Western blot, slot blot, and Northern blot) for levels of CaBP28K and CaBP28K mRNA. The various models did not exhibit any changes in protein or mRNA levels from the controls, suggesting that CaBP28K-containing neurons were not lost after exposure to these neurotoxins. Immunocytochemical characterization of the substantia nigra of the MPTP-treated mice revealed that there was significant dopaminergic cell loss in this brain area after MPTP treatment. The majority of dopaminergic neurons that degenerated did not contain CaBP28K. The small percentage of surviving neurons were CaBP28K-positive. These results suggest that the presence of CaBP28K may protect neurons from calcium-mediated neurotoxicity.

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↗
PubMed1995

Calbindin D28k mRNA in hippocampus, superior temporal gyrus and cerebellum: comparison between control and Alzheimer disease subjects.

To further investigate the role of calbindin D28k in Alzheimer's disease (AD); hippocampus, superior temporal gyrus and cerebellum from control and AD cases were examined by quantitative in situ hybridization. We report here a decrease in CaBD28k mRNA in the CA2 region of AD hippocampus compared to control subjects. There were no significant differences between AD and control subjects in the other regions studied.

Aged↗
PubMed1995

Quantitative measurement of neuronal calbindin-D28k by radioimmunocytochemistry.

The calcium-binding protein calbindin-D28k (CaBP) has been localized in high concentration in several neuronal populations within the CNS and is believed to act as an intracellular calcium buffer. There has been much interest and speculation concerning its potential neuroprotective function. A radioimmunocytochemistry (RIC) technique for the cellular quantitation of protein has been applied to quantitative measurement of neuronal CaBP in vivo and in vitro. The method permits cellular comparison of CaBP content within tissue sections or cells in culture. Through the use of specific primary antibody, 35S-labeled secondary antibody, and photographic emulsion, RIC combines the simplicity of standard immunocytochemical procedures with the sophistication and power of in situ hybridization, autoradiography, and image analysis. CaBP levels are expressed as mean +/- S.E.M. silver grains/cell. CaBP content has been measured and compared in mouse cerebellar Purkinje cells (56.5 +/- 6.9 grains/cell), granule cells of the hippocampal dentate gyrus (10.3 +/- 2.1 grains/cell), midline ventral tegmental neurons (11.6 +/- 2.9 grains/cell), and human SH-SY-5Y neuroblastoma cells in culture (5.1 +/- 0.9 grains/cell). As measured by RIC, mouse cerebellar Purkinje cells contain approximately 5-fold more CaBP than granule cells of the hippocampal dentate gyrus/midline ventral tegmental neurons and 10-fold more CaBP than cultured human SH-SY-5Y neuroblastoma cells. Assay reproducibility was demonstrated by comparison of adjacent sections which yielded a 3-9% intra-assay variability. Results were validated and confirmed by comparison to previous radioimmunoassay studies which indicated similar ratios of CaBP levels between brain regions/cell types.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1996

Isolation, characterization and in vivo analysis of the murine calbindin-D28K upstream regulatory region.

The genomic locus containing the murine calbindin-D28K gene has been isolated and partially characterized. Genomic cloning revealed an exon/intron chromosomal structure very similar to the avian gene previously described. The ability of the calbindin-D28K upstream region to direct cell-specific expression was tested in vivo. Varying lengths of upstream sequence were used to drive expression of lacZ in transgenic mice. Characterization of 23 transgenic mouse lines revealed that even as much as 3.0 kb of upstream sequence was unable to direct expression independently of integration site effects, suggesting the absence of important elements. Despite the small number of expressing transgenic lines and the great variability, there was a tendency of cell specificity of transgene expression exhibited in distinct brain regions. In the cerebellum, Purkinje cell-specific expression was observed with the shortest (1.0 kb) upstream sequence tested. Specificity of transgene expression in Purkinje cells was abolished with longer portions of upstream sequence. The same observation was made for transgene expression in granule cells of the dentate gyrus, while the opposite effect was observed for expression in CA1 hippocampal cells. The absence of any transgenic lines exhibiting appropriate transgene expression in the kidney suggested that the VDREs described previously for the murine calbindin gene are not sufficient to direct kidney expression in vivo. It is concluded that 3.0 kb of calbindin upstream sequence includes the regulatory elements dictating a portion of cell-specificity in the CNS of transgenic mice, albeit lacking regions that allow expression independently of chromosomal effects.

Animals↗
PubMed1989

Low levels of intestinal calbindin-D28K in X-linked hypophosphatemic mice.

Using our radioimmunoassay for chick intestinal calbindin-D28K, a protein homologous to that in the chick intestine on the basis of immuno-crossreactivity, molecular weight and charge properties was identified in mouse intestinal mucosa. No such protein, however, was found in the kidney, cerebellum, cerebrum, liver or myocardium of the mice. In X-linked hypophosphatemic mice (Hyp mice) maintained on a standard diet containing vitamin D, the basal level of intestinal calbindin-D28K was much lower (average 65.13 +/- 7.39%) than that in breeding pairs of normal mice maintained under the same conditions. Although the mean intestinal level of calbindin-D28K was as low as 118.23 +/- 20.08 (SD) ng/mg protein in vitamin D-deficient mice (-D), the level of this protein was markedly increased to the control level (198.68 +/- 9.98 vs. 198.49 +/- 14.29 ng/mg protein of control) (P less than 0.001) in response to the administration of vitamin D3 (1000 I.U. s.c. for 10 days) (+D). These results indicate that calbindin-D28K, biochemically indistinguishable from the chick intestinal calbindin-D28K, is present in the mouse intestine, and that the lower amount of this protein in the Hyp mouse intestine may, at least in part, be responsible for the resistance to the effects of vitamin D.

Animals↗
PubMedDate not supplied

Distribution and co-localization of calbindin D28k with VIP and neuropeptide Y but not somatostatin, galanin and substance P in the enteric nervous system of the rat.

Calbindin D28k, previously demonstrated in the mammalian central nervous system, has been localized to discrete neurons in the enteric nervous system of the rat. Calbindin D28k is present in cell bodies in both the myenteric and submucous plexi and in interganglionic nerve fibers in all regions of the gastrointestinal tract. Immunoreactive nerve fibers were also detected in the mucosal region, although none were observed in the pyloric sphincter, circular or longitudinal muscle layers. The highest concentration of immunoreactivity was present in the submucosal plexus and mucosa of the colon. Western blot analysis of the protein detected by the antiserum confirmed that it comigrated with purified calbindin D28k and the single immunoreactive band seen in extracts from rat brain. The colocalization of calbindin D28k with components of the peptidergic innervation was also investigated. Of the peptides studied the neurons containing both vasoactive intestinal polypeptide and neuropeptide Y in the submucous plexus were seen to exhibit calbindin D28k immunoreactivity. The neurons containing somatostatin, galanin and substance P did not demonstrate co-localization. In the stomach, calbindin D28k was detected within a small number of epithelial cells which were found to correspond to a sub-population of the somatostatin-immunoreactive endocrine cells.

Animals↗
PubMed1990

Calbindin D28k in mammalian intestinal absorptive cells: immunohistochemical evidence.

Calbindin D28k and D9k are two cytosolic calcium-binding proteins abundant in intestinal absorptive cells which appear to play a role in calcium translocation. Until today, calbindin D28k was found in avian and reptilian absorptive cells but not in mammalian ones. We have described the presence of calbindin D28k-immunoreactivity in intestinal absorptive cells of pig and jerboa (Jaculus jaculus). Pig calbindin D28k-immunoreactive absorptive cells were prominent in duodenum, they were scattered along the villi and nearly absent in the crypts. Jerboa labelled absorptive cells were located along the colonic mucosal surface. No calbindin D28k could be detected in mouse, rat and goat absorptive cells. Topography of calbindin D28k absorptive cells was compared with calbindin D9k distribution. Our results confirmed the data of the literature showing a gradient of labelling increasing from the crypt to the top of the villus and no positive endocrine cell. Young (48 h old) pigs did not expressed calbindin D28k in absorptive cells although calbindin D9k was detected. Calbindin D28K was also observed in endocrine cells which were numerous in pig and goat duodenum and very rare in mouse and jerboa. Western blot experiments confirmed the presence of calbindin D28k in the adult pig intestine, in the jerboa colon and the absence of cross-reactivity between calbindin D28k antibody and calbindin D9k.

Animals↗
PubMed1990

Cerebral cortical calbindin D28K and parvalbumin neurones in Down's syndrome.

Anti-calbindin D28K (CaBP) and anti-parvalbumin (PVA) antibodies were used to study the number and size of neurones containing these two calcium binding proteins in post-mortem brains from 7 neurologically normal controls and from 4 elderly patients with clinically diagnosed Down's syndrome (DS) and whose brains contained numerous senile plaques and neurofibrillary tangles. The possible co-existence of these two calcium binding proteins in human cerebral cortex was also examined. In the controls, CaBP immunoreactive neurones were mainly non-pyramidal neurones although some pyramidal neurones were also CaBP immunoreactive. All the PVA immunoreactive neurones were non-pyramidal cells. CaBP and PVA did not apparently co-exist with each other in cortical neurones. When compared with the neurologically normal controls, the number and size of CaBP and PVA immunoreactive neurones were significantly reduced in the cortex of patients with DS. These findings show that CaBP and PVA containing cortical neurones are affected in elderly persons with DS.

Aged↗
PubMed1992

Pyramidal neurons are immunoreactive for calbindin D28k in the CA1 subfield of the human hippocampus.

The calcium binding protein calbindin D28k (CaBP) is localized in the granule cells of the dentate gyrus, in pyramidal neurons of the CA1 and CA2 subfields of the Ammon's horn as well as in distinct groups of local circuit neurons in both parts of the human hippocampal formation. Immunostaining was performed on human brain perfused 2 h after death. The localization of CaBP in the human was found to be similar to that in the monkey hippocampus suggesting that there is no species difference in the cellular localization of CaBP among different primates.

Animals↗
PubMed1993

Distribution of calcium binding protein mRNAs in rat cerebellar cortex.

The distribution of three calcium binding protein mRNAs in the rat cerebellar cortex was investigated using alkaline phosphatase labelled specific antisense oligodeoxynucleotide probes. Calbindin D28k mRNA was detected in the Purkinje cells, parvalbumin mRNA was located in the Purkinje cells and also in basket/stellate cells of the molecular layer. Calretinin in contrast was found only in the granule cell layer. Use of multiple alkaline phosphatase (AP)-labelled oligodeoxynucleotides resulted in an increase in signal strength and reduced detection time with no increase in background staining indicating the utility of these enzyme labelled probes for non-isotopic in situ.

Animals↗
PubMed1993

Selective loss of calbindin D28K-immunoreactive neurons in the cortical layer II in brains of Alzheimer's disease: a morphometric study.

To investigate the relationship between neuronal death and intracellular calcium homeostasis in brains from patients with Alzheimer's disease (AD), we quantitatively analyzed morphological changes of calbindin-immunoreactive neurons. Neuronal counts were made in the autopsy brains from 6 control and 6 AD patients. Calbindin-immunoreactive neurons were mainly distributed in cortical layer II and were selectively lost in the AD brains. Further, the number of calbindin-immunoreactive neurons showed a negative correlation with age in the control group. These findings strongly suggest that age-related reduction of calbindin-immunoreactive neurons may be exaggerated in AD brains and change in calcium homeostasis may be involved in the pathogenesis of AD.

Age Factors↗
PubMed1994

Neostriatal mosaic and type II Ca2+/calmodulin-dependent protein kinase: an immunohistochemical study on the adult rat striatum.

The present immunohistochemical study is concerned with the expression of type II Ca2+/calmodulin-dependent protein kinase (CaM-kinase II), which is supposed to play an essential role in the intracellular Ca2+ signal transduction, in the striatum of adult rats. CaM-kinase II immunoreactivity was differentially concentrated in irregularly shaped compartments within the nucleus in a mosaic-like fashion. The compartment of heightened CaM-kinase II-immunolabeling corresponded to the extrastriosomal matrix visualized by calbindin-D28k-immunostaining. Light microscopic observation showed neurons immunoreactive for CaM-kinase II to be less densely distributed in the striosomes than in the matrix compartment. The present data suggest that these two striatal compartments may differ in an intracellular Ca(2+)-signaling process associated with protein phosphorylation.

Animals↗