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PubMed1988

Molecular structure of the chicken vitamin D-induced calbindin-D28K gene reveals eleven exons, six Ca2+-binding domains, and numerous promoter regulatory elements.

The seco-steroid hormone 1,25-dihydroxyvitamin D3 is known to induce the expression of a calcium binding protein termed calbindin-D28K in a variety of target tissues. In order to comprehend the mechanism of induction we have cloned and sequenced the chicken calbindin-D28K gene. The gene spans some 18.5 kilobases (kb) of chromosomal DNA from the putative Cap site to the polyadenylation site of the 2.8 kb mRNA. It is split into 11 coding exons by 10 intervening sequences. The promoter region of this gene is markedly G + C-rich (60-80%) extending from -225 to +400. Within this region we find 70 CpG dinucleotides, four G-C boxes, and numerous known promoter regulatory signals. These putative regulatory signals include a TATA box (ATAAATA) at -30 and a CAT box (CCAAT) at -326. Ten additional variant CAT boxes are found in the upstream promoter region (-218 to -770) of this gene. Furthermore we have identified a glucocorticoid-like responsive element at -410 (TCTACACACTGTTCC) and this element overlaps a metal responsive element (TGCACTC) and a variant CAT box (CCAAAT) and juxtaposes an enhancer-like core element (AAATGGT) on its 3'-side. In addition, the calbindin-D28K promoter is composed of a variety of simple repeated sequences, some of which are components of putative regulatory signals. All splice junctions were found to conform to the GT-AG rule. A consensus sequence of the 5'-splice junction reads AG/GTAAG-TTATA. A consensus sequence of the 3'-splice site consists of two elements: a pyrimidine track (mainly T) followed by ACAG/G-T. A two-dimensional model of calbindin-D28K was constructed which projects the existence of 6 alpha-helix-loop-alpha-helix regions characteristic of calcium binding domains. The 3'-end of the gene consists of a single large (2039 base pair) uninterrupted exon, an organizational feature common to other members of the calcium binding protein gene family which include calmodulin, parvalbumin, Spec I, myosin light chains, etc. Another feature common to the gene family is the presence of the repeated sequence ATTT or TTTA located in the 3'-untranslated exons. These simple repeat sequences could be involved in regulating mRNA degradation by serving as a ribonuclease recognition signal.

Amino Acid Sequence↗
PubMed1992

1,25-Dihydroxyvitamin D and not calcium is the major regulator of calbindin-D 9-kDa mRNA levels in vivo.

A possible role of calcium in vivo on intestinal calbindin-D 9-kDa mRNA levels has been studied in rats. In vitamin D-deficient rats, a marked increase in dietary calcium has a small but significant effect on calbindin-D 9-kDa mRNA levels, despite a dramatic increase in serum calcium concentration that clearly resulted from increased intestinal absorption of calcium. On the other hand, vitamin D under all circumstances increased calbindin-D 9-kDa mRNA levels, with the greatest levels found in animals on a low calcium diet where little or no calcium is available for absorption. These results strongly support the idea that 1,25-dihydroxyvitamin D is directly responsible for the induction of calbindin-D 9-kDa.

Animals↗
PubMed1999

Calbindin-D28k in cortical regions of the lizard Psammodromus algirus.

The morphology, distribution, and ultrastructural features of calbindin-D28k-immunoreactive neurons and fibers in the cortical regions of the lizard Psammodromus algirus, considered homologues to the mammalian hippocampal formation, were analyzed by using the peroxidase anti-peroxidase technique at the light and electron microscopic level. On the basis of staining properties and localization, two distinct populations of calbindin-D28k-immunoreactive neurons were observed in both the medial and dorsal cortices. Those located in the cell layer, namely principal neurons, were weakly immunostained, whereas a number of Golgi-like stained neurons were observed in plexiform layers. Double immunocytochemistry showed that all calbindin immunoreactive neurons in the deep plexiform layers were also gamma-aminobutyric acid immunoreactive. We consider them as a population of nonprincipal neurons different from those containing the calcium-binding proteins parvalbumin and calretinin. Two types of immunoreactive Boutons were revealed by electron microscopy on the basis of the synaptic specialization: Boutons making asymmetrical synapses were generally smaller in size and contacted on small dendritic profiles or cell bodies, whereas larger boutons established symmetrical synapses mainly on dendritic shafts. We propose that the first type of boutons arises from principal neurons and that the second type arises from nonprincipal ones. Finally, the staining pattern, localization, and the circuit in which nonprincipal calbindin-immunoreactive neurons and other neurochemically defined neurons could be involved in cortical regions of Psammodromus are compared with those of mammalian hippocampus.

Animals↗
PubMed1992

Decreased abundance of alkaline phosphatase and calbindin-D9K mRNAs in the intestine of the spontaneously hypertensive rat.

Alkaline phosphatase activity and calbindin-D9K immunoreactivity are decreased in the intestines of spontaneously hypertensive rats (SHRs). To investigate the potential role of altered gene expression in these decreases, we measured, by Northern blot analyses, the abundances of alkaline phosphatase and calbindin-D9K mRNAs in the proximal regions of the small intestines of 14-week-old SHR and control Wistar-Kyoto (WKY) rats. Alternate 4-cm segments of intestine were used for measurements of the proteins (0-4 cm, 8-12 cm, and 16-20 cm from pylorus, segments A1, B1, and C1, respectively) and mRNAs (4-8 cm, 12-16 cm, and 20-24 cm, segments A2, B2, and C2). Calbindin-D9K (immunoassay) was decreased in SHR vs WKY rats by 27%, 64%, and 67% in segments A1, B1, and C1, respectively (P < 0.01); its mRNA was decreased to a similar extent (69%, 82%, and 80%, respectively; P < 0.002 by analysis of variance). Alkaline phosphatase activity was decreased in SHRs by 58%, 54%, and 51% in segments A1, B1, and C1, respectively (P < 0.01); the abundance of its 3.0-kb mRNA was decreased to a similar extent: 57%, 80%, and 69% in segments A2, B2, and C2, respectively (P < 0.02). The mean decreases of the 2.7-kb mRNA of alkaline phosphatase were statistically significant (P < 0.02) but smaller (38%, 40%, and 35%). The mean abundance of vitamin D receptor mRNA in the same animals was decreased slightly in SHR vs WKY rats (3%, 36%, and 20% in segments A2, B2, and C2, respectively), but the difference in the values was not statistically significant. Decreases in alkaline phosphatase activity and calbindin-D9K immunoreactivity may reflect decreased mRNA abundance and not decreased enzyme-specific activity or increased protein degradation.

Alkaline Phosphatase↗
PubMed2003

Transcriptional regulation of the mouse calbindin-D9k gene by the ovarian sex hormone.

Calbindin-D9k levels in the rat uterus are under the control of estrogen. We found that the putative estrogen response element (ERE) failed to bind to the estrogen receptor from the mouse uterus. We therefore isolated mouse genomic clones of the calbindin-D9K gene and analyzed their expression in the mouse uterus. The promoter region of the gene contained several putative steroid hormone receptor binding sites. To characterize these elements, we constructed several promoter-reporter plasmids, and transiently transfected them into T47D breast cancer cells that express both estrogen and progesterone receptors. Luciferase activity was expressed from a promoter region containing the putative progesterone response element (PRE) and expression was stimulated by progesterone. In the uterus of oophorectomized mice, the calbindin-D9k gene was up-regulated by progesterone, but not by estrogen. These results suggest that the mouse uterine calbindin-D9k gene is expressed under the control of a PRE.

Animals↗
PubMed1991

An estrogen-responsive element mediates the transcriptional regulation of calbindin D-9K gene in rat uterus.

The rat calbindin (molecular mass 9 kDa) gene sequence revealed the presence of an imperfect palindromic estrogen-responsive-like element (ERE) located at position +51 from the transcriptional initiation site. This element has the sequence AGGTCAGGGTGATCT which differs by one nucleotide from the vitellogenin ERE palindromic sequence AGGTCACTGTGACCT. The activity of this element to induce transcription in response to estrogen and the ability to bind estrogen receptor was investigated. This sequence confers estrogen-dependent transcriptional activity when cloned upstream from the tkp-CAT construct in pBLCAT2 plasmid and transfected into T47D cells, similar to the vitellogenin gene ERE activity but to a lesser extent. This element binds to the estrogen receptor in vitro as assessed by gel retardation assay similar to the vitellogenin gene ERE. No such binding was detected when a mutant sequence AGATCACTGTGATCT was used. The specificity of the complex was confirmed using polyclonal antibodies, ER712 raised against the estrogen receptor. Furthermore, competition assays showed that both sequences were able to compete for binding to the estrogen receptor. The in vivo transcriptional regulation of the calbindin D-9K gene by estrogen was also investigated in the rat. Female animals maintained on a vitamin D-sufficient or a vitamin D-deficient diet were ovariectomized, housed for 3 weeks, and then injected with 17 beta-estradiol (0.5 micrograms/kg body weight/day). Slot blot analysis of total RNA showed a marked increased in calbindin D-9K mRNA levels in the uterus but not in the intestine by 26 and 50 h post-injection. These results demonstrate that the calbindin D-9K gene is transcriptionally regulated by estrogen in the uterus mediated by an estrogen-responsive element identified in the gene.

Animals↗
PubMed1994

Induction of a calbindin-D9K-like protein in avian muscle cells by 1,25-dihydroxy-vitamin D3.

1,25-dihydroxy-vitamin D3 induces the synthesis of a 9 kDa calcium binding protein in chick embryo myoblasts. This work revealed comigration of the myoblast protein with rat calbindin-D9K in SDS-polyacrylamide gels. Western-blot analysis with a specific calbindin-D9K antibody showed the presence of an immunoreactive protein of 9 kDa in chick tissues. In addition, higher levels of myoblast mRNA hybridizing to a specific cDNA probe for rat calbindin-D9K were detected in response to 1,25-dihydroxy-vitamin D3. Northern hybridization analysis showed that the increase was related to a single 550 nucleotide mRNA species. These results provide the first evidence on the presence of calbindin-D9K or a closely related protein in avian tissues and its inducible expression in muscle by 1,25-dihydroxy-vitamin D3.

Animals↗
PubMedDate not supplied

Calbindin D-28k immunoreactivity in the temporal neocortex in patients with Alzheimer's disease.

Calbindin D-28k immunoreactivity in the temporal isocortex was examined in seven patients with Alzheimer's disease (AD) and in six controls. In normal brains, calbindin D-28k-immunoreactive cells were bitufted neurons, multipolar cells with ascending dendrites and large double-bouquet cells mainly located in layers II and III. Immunoreactive fibres were seen in the molecular layer and in vertical bundles in layers III and V/VI. Calbindin D-28k immunoreactivity was reduced in patients with AD, although with differences from one patient to another. Immunoreactivity was decreased in the plexus of the molecular layer and in the vertical bundles in the cellular layers in every case. Most patients had, also, decreased immunoreactivity in the dendritic arbors. The number of calbindin D-28k-immunoreactive cells was significantly decreased in three of five patients with moderate or severe dementia, and was normal in two cases with mild dementia.

Aged↗
PubMed1996

Developmental expression and vitamin D regulation of calbindin-D28K in chick embryonic yolk sac endoderm.

The yolk is an important calcium source for the developing chick embryo. The epithelial yolk sac endodermal cells lie in direct contact with the yolk and are the principal nutrient-transporting cell type. We previously reported that vitamin D treatment stimulated yolk calcium mobilization and that the vitamin D-dependent Ca2+-binding protein, calbindin-D28K, is present in the yolk sac. We report here the developmental expression and regulation of calbindin-D28K in the yolk sac. Calbindin-D28K is expressed as early as incubation d 3 and is found exclusively within the cytoplasm of endodermal cells. Comparative protein and mRNA analyses of yolk sac and dissociated yolk sac endodermal cells as a function of development and treatment with calcitriol (1,25-dihydroxyvitamin D3) in vitro and in vivo showed a development-specific and vitamin D-inducible expression of calbindin-D28K. Northern analysis revealed the expression of vitamin D receptor mRNA in the yolk sac, beginning as early as d 3, strongly indicating that the extraembryonic yolk sac is an early vitamin D target tissue. Cultured yolk sac endodermal cells should serve as a useful in vitro cell model for analyzing the cellular and molecular mechanisms of vitamin D action.

Animals↗
PubMed1995

Ontogeny of calbindin-D28K and calretinin in developing chick kidney.

The ontogeny of two calcium-binding proteins (calbindin-D28k and calretinin) was studied by immunohistochemical techniques in developing chick kidney. This study showed the presence of calbindin on the 5th incubation day and calretinin on the 7th incubation day in mesonephric distal and connecting tubules, and in the medial wall of the Wolffian duct. At later stages, immunostaining for these two proteins, in particular for calretinin, was also demonstrated in some metanephric proximal tubules. Glomeruli and Bowman's capsules were negative both in the mesonephros and metanephros. The presence of calretinin in the developing kidney has thus been demonstrated for the first time. The early expression of calbindin and calretinin in mesonephric distal tubules suggests their role in regulating the final excretion of calcium. The different patterns of immunoreactivity of the walls of the Wolffian duct can be correlated with their different histogenetic and histological features.

Animals↗
PubMed1992

Immunohistochemical markers in rat cortex: co-localization of calretinin and calbindin-D28k with neuropeptides and GABA.

Calretinin and calbindin-D28k are two calcium-binding proteins which are present in separate populations of interneurons in cerebral cortex and hippocampus. To identify these cells with the populations expressing different transmitters, two-colour immunofluorescence was done with antibodies against the calcium-binding proteins plus antibodies against vasoactive intestinal peptide (VIP), somatostatin (SRIF), or gamma-aminobutyric acid (GABA). In neocortex, calretinin is partially co-localized with VIP (especially in the deeper layers) and is not co-localized with SRIF. Calbindin is largely co-localized with SRIF, and not with VIP. Both calretinin and calbindin are partially co-localized with GABA. In piriform and entorhinal cortex, the patterns resemble those in neocortex. In hippocampus, preliminary data indicate greater heterogeneity, especially in the ventral part; at least a few double-positive cells are present for every combination of calcium-binding protein and neuropeptide. These results expand the known diversity of local-circuit neurons in cortical regions.

Animals↗
PubMed1993

Immunohistochemical localization of calretinin-, calbindin-D28k- and parvalbumin-containing cells in the hypothalamic paraventricular and supraoptic nuclei of the rat.

The localization of three calcium-binding proteins, calretinin, calbindin-D28k and parvalbumin, in the hypothalamic paraventricular and supraoptic nuclei of the rat was immunohistochemically examined on adjacent sections and their distribution patterns were compared. Overlap between the distribution of calretinin-immunoreactive cells and that of calbindin-D28k-immunostained cells was found in the rostrodorsal part of the supraoptic nucleus, and the caudoventral part of this nucleus contained predominantly calbindin-D28k-stained cells. Cells of the medial and lateral magnocellular subdivisions of the paraventricular nucleus were almost devoid of the calcium-binding proteins examined. No parvalbumin-immunostained cells were observed in either nucleus. This study provides a further characterization of cell bodies in the hypothalamic paraventricular and supraoptic nuclei.

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↗
PubMed1993

Mouse fetal trisomy 13 and hypotrophy of the spinal cord: effect on calbindin-D28k and calretinin expressed by neurons of the spinal cord and dorsal root ganglia.

Trisomy 13 was detected in 10% of mouse embryos obtained from pregnant females which were doubly heterozygous for Robertsonian chromosomes involving chromosome 13. The developing dorsal root ganglia and spinal cords were examined in trisomy 13 and littermate control mice between days 12 and 18 of gestation (E12-18). The overall size of the dorsal root ganglia and number of ganglion cells within a given ganglion were not altered, but the number of neurons immunoreactive for calbindin and calretinin was reduced. The trisomic spinal cord was reduced in size with neurons lying in a tightly compact distribution in the gray matter. In trisomic fetuses, the extent of the neuropil of the spinal cord was reduced, and may represent a diminished field of interneuronal connectivity, due to reduced arborization of dendritic processes of the neurons present, particularly of calbindin-immunostained neurons. Furthermore, the subpopulation of calretinin-immunoreactive neurons and axons was also reduced in developing trisomic gray and white matter, respectively. Thus, overexpression of genes on mouse chromosome 13 exerts a deleterious effect on the development of neuropil, affecting both dendritic and axonal arborization in the trisomy 13 mouse. The defect of calbindin or calretinin expression by subsets of dorsal root ganglion or spinal cord neurons may result from deficient cell-to-cell interactions with targets which are hypoplastic.

Animals↗
PubMed1994

Distribution of calretinin, calbindin-D28k, and parvalbumin in the rat thalamus.

The localization of three calcium-binding proteins, calretinin, calbindin-D28k, and parvalbumin, in the rat thalamus was immunohistochemically examined. a) Some thalamic regions revealed cells almost exclusively containing one of the calcium-binding proteins. For example, almost only calretinin-stained cells were found in the central medial and paraventricular nuclei. Calbindin-D28k-stained cells were mostly found in the centrolateral, interanteromedial, anteromedial, and posterior nuclei. Only parvalbumin-positive cells were found in the central part of the reticular nucleus. b) Other regions expressed overlap between the distributions of two cell components composed of different calcium-binding proteins. For example, both calretinin-stained cells and calbindin-D28k-labeled cells were found in the lateroposterior, intermediodorsal, rhomboid, and reuniens nuclei. c) Other regions showed no cells stained for any of the calcium-binding proteins. For example, generally no calcium-binding protein was detected in neurons of the anterodorsal, anteroventral, ventrolateral, ventral posterolateral, ventral posteromedial, or gelatinosus nuclei, or of the central part of the mediodorsal nucleus. These three proteins serve as useful marker for localizing subpopulations of neurons within the thalamus.

Animals↗
PubMed1995

Calbindin-D28k, calretinin, and S-100 immunoreactivities in rat pineal gland during postnatal development.

Profound morphological modifications occur during postnatal development of the rat pineal gland. We have immunohistochemically followed those events from postnatal day 1 to 20 by using three cytoarchitectonic markers (S-100, calbindin-D28k, and calretinin) that belong to the calmodulin/troponin C calcium-binding protein family. In the developing rat pineal, anticalbindin-D28k antibody labels three cell types: immature and mature astrocytes and perivascular type II pinealocytes. During development, calbindin-D28k positive cells migrate from the base of the pineal stalk into the superficial part of the pineal. Calbindin-D28k, usually used as a neuronal marker in the central nervous system, recognizes in rat pineal precursor astrocytes 5 days before S-100 and labels a subpopulation somewhat different from S-100 positive astrocytes. Calretinin immunoreactivity appeared in the postero-superior part of the pineal and was abundant until postnatal day 5, then its density dramatically felt to leave, after postnatal day 20, an occasional population of cells whose morphology is compatible with neuron-like cells.

Animals↗
PubMed1986

Immunohistochemical localization of calbindin-D28k during the development of the rabbit nephron.

Specific antibodies raised against a 28-kilodalton chick intestinal calcium-binding protein (calbindin-D28k) were used to localize the protein immunocytochemically in the developing rabbit kidney. Kidneys taken from rabbits between the 13th embryonic and 17th postnatal day were examined. Calbindin-D28k was observed in the mesonephric duct and the ureteral bud on the 13th embryonic day. During subsequent involution of the mesonephros, the ampullae of the metanephric ureteral buds contained calbindin-D28k. The protein was gradually lost from the ureters and the deep interstitial collecting ducts. Calbindin-D28k was never present in the renal vesicles derived from the nephrogenic blastema, but it was present in the connecting tubule segments during formation of the arcades. The last finding supports the belief that the connecting tubule is derived from the ureteral bud.

Animals↗
PubMed1986

Analysis of the mRNA coding for the chick vitamin D-induced calbindin and its regulation by 1,25-dihydroxyvitamin D3.

We have used specific cloned cDNA probes generated from the mRNA coding for the vitamin D-induced 28,000-Da chick intestinal calcium binding protein (calbindin) to study the hormonal regulation of the expression of this mRNA by 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3]. The calbindin-mRNA has been analyzed in chicken intestinal poly(A)+ mRNA samples as well as other chicken tissues by "Northern" blot analysis. There exists a predominant mRNA species of approximately 2000 nucleotides and two minor cross-hybridizing species that are nearly equivalent in proportion; their sizes are approximately 2600 and 3100 nucleotides. All three mRNA species are nonexistent in the chick intestine in the absence of vitamin D3 intake. However, all three mRNA species begin to accumulate at the same time in the chick intestine following the administration of the hormonally active metabolite of vitamin D3, 1,25-(OH)2D3. This response in the intestine is very similar to other steroid hormone-regulated gene products. All three mRNA species exist in the cell cytoplasm and are present on soluble polysome complexes, suggesting that all three are engaged in protein synthesis. Examination of other chick tissues (both vitamin D-deficient and -replete) reveals a close association between mRNA expression and previously observed calbindin expression. Each tissue is unique in the steady-state level of expression of the calbindin-mRNAs.

Animals↗