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PubMed1995

Calbindin-D 28k immunoreactivity in the cerebellum of spinocerebellar degeneration.

We studied immunoreactivity for calbindin-D 28k (CaBP), an intracellular calcium-binding protein, in the cerebellum of control subjects and of patients with spinocerebellar degeneration (SCD) including sporadic olivopontocerebellar atrophy and familial cortical cerebellar atrophy. In the cerebellum, CaBP immunoreactivity was seen exclusively in the Purkinje cell in both SCD and control groups. However, the number of CaBP-immunoreactive Purkinje cells was significantly reduced in SCD. CaBP immunohistochemistry also disclosed abnormal morphological changes of Purkinje cells, which was not visualized on conventional strains or not clearly demonstrated on immunohistochemistry for neurofilaments. Moreover, reduced CaBP immunoreactivity was observed even in some remaining Purkinje cells of SCD suggesting that loss of CaBP precedes neuronal loss of Purkinje cell. We conclude that CaBP is a useful marker for Purkinje cell degeneration, and that reduced CaBP expression might have some association with the mechanism of the Purkinje cell degeneration in SCD.

Aged↗
PubMed1992

Age-related morphological and morphometrical changes in parvalbumin- and calbindin-immunoreactive neurons in the rat hippocampal formation.

Parvalbumin (PV)- and calbindin (CaBP)-immunostaining in the hippocampal formation of 3-, 11- and 28-month-old Wistar rats was studied using monoclonal antibodies. A quantitative analysis of the densities, cross-sectional areas, length and number of processes of PV-immunoreactive neurons in the hippocampal dentata and CA1 areas of the three age groups was employed. Marked age-related changes in the morphological appearance and in the quantitative parameters characterizing the PV-immunoreactive neurons in both hippocampal regions were observed. The intensity of CaBP-immunostaining of the hippocampal principle cells and interneurons remained the same but the immunoreactive fibers were structurally altered in aging.

Aging↗
PubMed1994

Modulation of the excitability of avian peripheral nerves by vitamin D: relation to calbindin-D28k, calcium status and lipid composition.

Calbindin-D28k (CaBP), previously localized in some of the cell bodies of ganglia of the avian intestinal (Remark's) nerve, was shown to be vitamin D-dependent. In the present studies, the effect of vitamin D3 on electrophysiological properties of this nerve was examined in vitro. Electrical stimulation of the nerve yielded a compound action potential with two primary components, Peaks I and II. Peak II, suppressed by hexamethonium bromide or Ca(2+)-free buffer, is synaptically mediated. The transit time between the two peaks was unaffected by vitamin D3. The apparent conduction velocity, defined as [(activation time + transit time)/nerve length], was increased by vitamin D-deficiency and decreased by vitamin D3 repletion, the latter decrease due entirely to an increase in activation time. Activation time after vitamin D-repletion was correlated with an increase in CaBP and plasma Ca2+ levels. However, normalization of plasma Ca2+ by supplementation of vitamin D-deficient diets with excess calcium (2.5 and 4.0%) also resulted in an increase in activation time, without affecting neuronal CaBP levels. Vitamin D3 also decreased the conduction velocity and increased CaBP of the vagus nerve and, by lipid analysis, was shown to increase and decrease its phosphatidylcholine and phosphatidylethanolamine content, respectively, and to decrease its phospholipid/cholesterol ratio. Modulation of peripheral nerve activity by vitamin D3 is related to calcium status and perhaps to changes in lipid composition. The functional role of CaBP in the behaviour of this complex nerve remains unknown.

Animals↗
PubMedDate not supplied

Calbindin, tyrosine hydroxylase and opioid-like immunoreactivity in the intestinal nerve of Remak of the domestic fowl.

Four classes of neurons were identified in both juxta-jejunal and juxta-rectal ganglia of Remak's nerve of the domestic fowl using double-labeling immunohistochemistry. Neurons immunoreactive (IR) for tyrosine hydroxylase (TH) formed a mutually exclusive subpopulation from neurons displaying calbindin (CaBP)-IR. Between 48-72% of juxta-jejunal neurons labeled for TH whereas 36-57% of juxta-rectal neurons displayed TH-IR. CaBP-IR was present in 18-40% of juxta-jejunal neurons; this increased to 31-46% in juxta-rectal neurons. The majority of CaBP-IR neurons (78-85%) also displayed opioid (beta-EP)-IR. Within each ganglion a small percentage of neurons (4-18%) were non-IR with any of the three antibodies. This is the first report of an immunohistochemically identified subpopulation of non-catecholaminergic neurons within the juxta-jejunal ganglia of Remak's nerve. It is proposed that these perikarya are a major source of the CaBP-IR and opioid-IR nerve fibers found in the chicken gut.

Animals↗
PubMed1996

Calbindin and parvalbumin immunoreactivity in the developing and adult human retina.

We report the expression and pattern of two calcium-binding proteins (CBPs), calbindin (CALB) and parvalbumin (PV), in the fetal (13-25 weeks of gestation), postnatal (5 months) and adult human retina, as studied by immunohistochemistry. Both CBPs appear prenatally in different neurones as well as in the nerve fibre, inner and outer plexiform layers. The cones do not show immunoreactivity for both CBPs up to 25 weeks, the last fetal stage studied; however, they are immunopositive in the postnatal and adult retina. Of the two CBPs, CALB appears first, followed by PV. The immunoreactivity for both CALB and PV in the fetal retina follows a centroperipheral gradient and vitreal to scleral pattern of retinal differentiation. The CALB immunoreactivity shows a gradual increase in intensity with age. A spurt in intensity of PV immunoreactivity in the 24-25 week fetal retina and increased intensity in the 60 year normal adult retina when compared to the light-deprived retina of a 34-year-old staphyloma patient suggests an activity-dependent functional role for PV.

Adult↗
PubMed1996

The distribution of two calcium binding proteins, calbindin D-28K and parvalbumin, in the entorhinal cortex of the adult mouse.

The immunohistochemical localization of two specific calcium binding proteins, parvalbumin (PV) and calbindin D-28K (CB), were examined in the entorhinal cortex (EC) of the adult mouse. The PV and CB immunoreactivities exhibited a conspicuous regional and laminar distribution in the EC. The overall immunostaining pattern of PV and CB appeared to be complementary in the EC, especially in the medial entorhinal area (MEA). In the dorsal MEA, although layer 2 showed intense PV and CB immunostaining, the PV immunoreactivity was denser in layers 3, 5 and 6a than in layers 4 and 6b, whereas the CB immunoreactivity was denser in layers 4 and 6b than in layers 3, 5 and 6a. Moreover, we recognized the dorsoventral gradation of the PV and CB staining that is, in the dorsal to ventral direction, the intensity of the PV immunostaining in layers 2, 3, 5 and 6a gradually decreased whereas that of the CB immunostaining in those layers gradually increased. In addition, a similar dorsoventral gradation was also observed in the number of PV immunoreactive (PV-IR) and CB-IR neurons in layer 3. In layer 2 of the MEA, the CB-IR neurons were clustered, while displaying a patch-like pattern which could not be recognized in either Nissl staining or PV staining. In contrast, layer 2 of the LEA was separated into two sublayers, the superficial sublayer 2a and the deeper sublayer 2b; both of these sublayers consisted of cell clusters recognized by Nissl staining. These sublayers showed a prominent difference in their CB immunoreactivity; the cells in the layer 2a clusters were CB negative, whereas the cells in the layer 2b clusters were CB-IR. Furthermore, we also recognized a particular region at the most medial part of the MEA, where layer 2 was different from the other portion of the MEA regarding CB immunoreactivity and the cells containing another calcium binding protein, calretinin, were clustered in layer 3. Both the adjacent section technique and the fluorescent double-staining technique clearly revealed that a relatively large number of presumable interneurons contained both PV and CB immunoreactivities. Furthermore, the three neuron groups that were immunoreactive for both PV and CB, immunoreactive for PV alone and immunoreactive for CB alone were heterogeneous in their structural features such as shape and size, and no particular difference was found in their structural features among these three groups.

Age Factors↗
PubMed1991

Substance P and calbindin D-28k-immunoreactivity in primary sensory neurons of chick embryos: differential neuronal birthdates and transient co-localization.

During the ontogenesis of dorsal root ganglia (DRG), the immunoreactivity to substance P (SP) and calbindin D-28k (CaBP) appears in chickens at embryonic day 5 (E5) and E10 respectively. To establish the birthdates of primary sensory neurons expressing SP or CaBP, chick embryos were given repetitive intra-amniotic injections of [3H]-thymidine. The neuroblasts giving rise to SP-expressing neurons were labeled up to E6 while those generating CaBP-immunoreactive neurons stopped to incorporate [3H]-thymidine before E5.5. This finding indicates that neurons exhibiting distinct phenotypes may originate from neuroblasts which arrest to proliferate at close but distinct stages of development. To determine whether SP and CaBP are co-expressed or not in DRG neurons, chick embryos at E12, E18, and chickens two weeks after hatching were perfused and fixed to detect simultaneously SP- and CaBP-immunoreactivity in DRG sections. The results showed that SP and CaBP were transiently co-expressed by a subset of neurons at E12. Later, however, the SP-immunoreactivity was gradually lost by these ganglion cells, so that the SP- and CaBP-immunoreaction defined two distinct neuronal subpopulations after hatching. In conclusion, most CaBP-immunoreactive DRG cells derive from a subset of neurons in which SP and CaBP are transiently co-localized.

Animals↗
PubMed1987

Expression of calbindin-D28K mRNA as a function of altered serum calcium and phosphorus levels in vitamin D-replete chick intestine.

The availability of specific cDNA probes to the chick intestinal calbindin-D28K (CaBP) mRNA has allowed us to assess the regulation of this mRNA in response to 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) administration. It has previously been demonstrated that dietary calcium and phosphorus can effect alterations in the steady-state intestinal levels of chick CaBP. We have examined whether or not perturbations in dietary calcium and phosphorus have an effect on the expression of the intestinal mRNA coding for CaBP in the vitamin D-replete chick. We found altered protein levels of CaBP as expected; however there was surprisingly no difference in steady-state CaBP mRNA levels between the different dietary groups. These data suggest that calcium and phosphorus regulation of CaBP occurs at a post-transcriptional level. In addition, we have examined what effect dietary manipulations of calcium and phosphorus levels have on the response of the vitamin D-replete intestine to 1,25(OH)2D3 administration as assessed by CaBP mRNA changes. Administration of 1,25(OH)2D3 to vitamin D-replete chicks maintained on normal calcium and phosphorus levels resulted in a less than 2-fold increase in CaBP mRNA levels. Previous studies have demonstrated that receptor occupancy goes up 6-fold under these conditions; therefore there is apparently a very tight regulation of CaBP gene activity. 1,25(OH)2D3 administration to chicks raised on either low calcium, high calcium, or low phosphorus vitamin D-replete diets similarly showed only small changes in the intestinal CaBP mRNA levels; however there seemed to be qualitative differences in response attributable to the dietary alterations.

Animals↗
PubMed1992

Calbindin-D9k gene expression during pregnancy and lactation in the rat.

Calbindin-D9k (CaBP-9k) is a calcium binding protein expressed in mammalian intestine, uterus and placenta. It is believed to be involved in transepithelial calcium transport in intestine and placenta and regulation of cytosolic calcium concentration in uterus. CaBP-9k mRNA levels were measured by Northern blot analysis in maternal duodenum, uterus, placenta and fetal/neonatal duodenum during pregnancy and lactation. In maternal duodenum a maximal increase occurred at day 15 of lactation (2.3-fold) and 20 days post-lactation levels decrease to 30.3% of non-pregnant controls. In non-pregnant uterus a 10-fold variation of CaBP-9k mRNA levels was observed between individual animals despite a uniform expression of beta-actin. During pregnancy high CaBP-9k expression is found, averaging about 20% of duodenal levels, which abruptly drops below detection during early lactation. At late lactation CaBP-9k mRNA levels are again subject to great variation ranging from no expression to maximal levels found in the non-pregnant uterus. Placental CaBP-9k is maximally expressed at the end of pregnancy (day 20) reaching about 2.5% of duodenal levels. Fetal intestinal CaBP-9k mRNA was detectable in 20 micrograms total RNA at day 18 of pregnancy and rose sharply in early lactation reaching about 50% of adult duodenal levels at day 20 lactation. The profound changes of uterine CaBP-9k mRNA in non-pregnant (cycling), pregnant, and lactating rats indicate a rapid hormonal regulation of gene expression, most likely involving 17 beta-estradiol.

Animals↗
PubMed1992

Calbindin-D9k mRNA is tightly regulated during the estrous cycle in the rat uterus.

Calbindin-D9k (CaBP-9k) is a cytosolic calcium binding protein with a molecular weight of 9000. CaBP-9k is mainly expressed in intestine, uterus and placenta, with intestinal levels controlled by vitamin D and uterine levels controlled by estrogens. CaBP-9k mRNA levels were measured in rat uterus throughout the estrous cycle. On the morning of proestrus, estrus and diestrus animals were sacrificed. Serum 17 beta-estradiol concentrations were determined using a radioimmunoassay. Whole uterus was used for preparation of total RNA. Northern blot analysis was performed to quantify CaBP-9k and beta-actin mRNA. CaBP-9k levels were highest at proestrus, dropped 10-fold at estrus and were not detectable at diestrus. beta-Actin levels did not change significantly throughout the estrous cycle. Peak 17 beta-estradiol concentrations coincided with maximum CaBP-9k mRNA expression at proestrus. Despite minimal concentrations of 17 beta-estradiol at estrus, CaBP-9k mRNA was still present at 10% of the proestrus level. At diestrus, CaBP-9k mRNA was not detectable despite increasing 17 beta-estradiol. It is concluded that CaBP-9k is subject to 17 beta-estradiol regulation during the estrous cycle. Correlation between CaBP-9k mRNA and 17 beta-estradiol levels indicates a lag period for CaBP-9k induction in diestrus following a rise in steroid hormone levels.

Animals↗
PubMed1993

Calbindin-D9k gene expression during the perinatal period in the rat: correlation to estrogen receptor expression in uterus.

Calbindin-D9k (CaBP-9k) is a cytosolic calcium binding protein mainly expressed in duodenum, placenta and uterus. The gene encoding the rat CaBP-9k is subject to tissue specific induction by 1,25 dihydroxyvitamin D3 (intestine) and estradiol (E2) (uterus). Control of placental expression remains unknown. The expression of CaBP-9k mRNA during the perinatal period was studied (pregnancy day 21 (P21)-lactation day 4 (L4)). In uterus, maximal expression levels were found at P21 and maintained until L1. With the transition to L2, the CaBP-9k mRNA concentration dropped drastically below the detection limit as quantitated by Northern blot analysis. Measurements of E2 and progesterone (P) levels showed a gradual decrease at late pregnancy (P21; birth). Post partum E2 levels continued to decline and P concentrations increased slightly. Uterine estrogen receptor (ER) mRNA levels determined by cDNA/PCR analysis revealed close correlation between expression of ER and CaBP-9k mRNAs. ER mRNA levels were maximal at P22 and declined at parturition and with onset of lactation. At L2 and L3 ER mRNA levels were minimal and had decreased 5-fold compared to late pregnancy. CaBP-9k protein concentrations fluctuated only slightly dependent on the stage of the estrous cycle: estrus > proestrus > diestrus. During the perinatal period CaBP-9k concentration was overall lower than in non-pregnant uterus and revealed only a moderate increase at birth and decrease in early lactation. Similar to the uterine levels, placental CaBP-9k mRNA was highest at P21 and remained high until birth. Fetal duodenal CaBP-9k rose sharply just prior to birth and plateaued in the early postpartal period.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Expression of calbindin-D9k in the early pregnant rat uterus: effects of RU 486 and correlation to estrogen receptor mRNA.

Calbindin-D9k (CaBP-9k) is a calcium binding protein expressed at high levels in the rat uterus. The CaBP-9k gene carries an estrogen response element which is involved in the steroid hormone regulation of the gene during the estrous cycle and gestation. The present study was aimed at determining expression of the gene during the first half of pregnancy and to assess the role of progesterone (P4) and the estrogen receptor (ER). Expression of CaBP-9k mRNA was determined by Northern blot analysis during the first 10 days of pregnancy. On pregnancy day 1 (P1), CaBP-9k mRNA levels were relatively high. On P2, 3 and 5 CaBP-9k mRNA decreased to the detection limit using 10 micrograms total RNA probed with a random primed cDNA. On P10, CaBP-9k transcripts began to reappear at levels of about 30% of P1. Expression of beta-actin mRNA displayed a continuous increase during this period with a rapid rise of 240% between P2 and P3. The typical increase of P4 accompanied by moderate changes of estradiol (E2) was determined in serum of experimental groups. When RU 486 at 10 mg/kg was administered as a single s.c. injection on P3, the CaBP-9k down-regulation was rapidly interrupted and mRNA expression became extremely high. The effect was seen maximally at 24 h post injection and was maintained at 48 and 72 h. Expression of beta-actin mRNA was increased only moderately at 24 h and was unchanged at 48 and 72 h. Serum P4 remained unaffected by the treatment and E2 displayed a slight increase.(ABSTRACT TRUNCATED AT 250 WORDS)

Actins↗
PubMed1990

Short-term changes of parvalbumin and calbindin immunoreactivity in the rat hippocampus following cerebral ischemia.

The calcium-binding proteins, parvalbumin (PV) and calbindin (CaBP), were used as immunocytochemical markers for two different interneuron populations in the rat hippocampus shortly after transient cerebral ischemia. Besides in interneurons, CaBP immunoreactivity (-i) is located in hippocampal CA1 pyramidal cells and dentate granule cells. Shortly after ischemia, the PV-i and CaBP-i were unchanged but, around the 4th postischemic day, PV-i disappeared from somata and fibers located in CA1, CA3c, and the dentate hilus. Terminal PV-i was unchanged. Within days, the PV-i gradually reappeared, first in somata and then in fibers. The transient loss of PV-i was, on a time scale, closely accompanied by a permanent loss of CaBP-i in CA1 pyramidal cells. CaBP-i in interneurons was unchanged. In order to examine the effect of an increased intracellular calcium concentration on the PV-i and CaBP-i, the calcium ionophore A23187 was stereotaxically injected into CA1. In rats killed 30 min later and processed for PV-i and CaBP-i, both PV-i and CaBP-i had disappeared around the A23187 injection sites. Based on this observation and the changes observed after ischemia, it is suggested that the hippocampal PV-i interneurons suffer from a delayed and reversible calcium accumulation in the days after ischemia. Concomitantly, there could be a decreased synthesis or increased destruction of PV after ischemia.

Animals↗
PubMed1994

Calbindin D-28k in the lateral vestibular nucleus of mutant mice as a tool to reveal Purkinje cell plasticity.

Antibodies against the calcium-binding protein Calbindin D-28k (CaBP) are specific markers of cerebellar Purkinje cells (PC). To identify the origin of CaBP-immunopositive (CaBP+) terminals and fibres in the dorsal part of the lateral vestibular nucleus (dLVN), brains of Purkinje cell degeneration mutants (PCD) were immunoreacted for CaBP using the avidin-biotin method (ABC). In PCD an almost complete loss of CaBP+ fibres and terminals in the dLVN compared to the wildtype and the Weaver mutant was present. Morphometric analysis of CaBP+ synaptic terminals in the dLVN of adult Weaver mutants showed that the maximum and mean terminal size exceeded those in wildtypes by almost twice, which is a far larger difference than in GABA-immunoreacted material. The results show that CaBP-immunoreactivity and terminal size expansion in Weaver are both mainly attributable to PCs. Moreover, it can be concluded that the colocalization of CaBP and GABA in fibres and terminals of the dLVN in normal animals is almost entirely restricted to the PC-innervation of this nucleus. Therefore CaBP-immunocytochemistry is an excellent tool to selectively investigate the direct PC-projections in the dLVN, as it sets off the GABAergic PC-innervation from the total GABAergic innervation of this area.

Animals↗
PubMed1992

Distribution of calbindin D-28K and parvalbumin immunoreactivities in the nucleus olfactorius anterior of the rat.

The distributions of calbindin D-28K (CaBP) and parvalbumin (PV) in the rat nucleus olfactorius anterior (NOA) were described using monoclonal antibodies and the avidin-biotin-peroxidase method. The NOA showed a high immunoreactivity for CaBP, with a rostrocaudal increase in the positive neurons and fibres. Pars externa (NOAe) was the only subdivision which showed a low CaBP immunostaining. PV-positive elements were less abundant than those CaBP immunostained. The main difference in the distributions for both proteins was observed in the pars medialis which was practically PV negative. PV- and CaBP-stained neurons showed similar morphologies in the subdivisions where they were present. In NOAe, we observed a characteristic PV- and CaBP-positive neuronal type, with an oriented dendritic pattern. Transition areas were clearly observable in both CaBP- and PV-labelled sections.

Animals↗
PubMed1991

DNase I-hypersensitive sites are associated, in a tissue-specific manner, with expression of the calbindin-D9k-encoding gene.

We have examined the chromatin structure of a 28-kb chromosomal region containing the gene (CaBP9k) encoding calbindin-D9k in different rat tissues. DNase I-hypersensitive sites (HSs) were probed with DNase I using an indirect end-labeling technique. Duodenal chromatin, where the gene is strongly expressed, contained one major HS (HS4) and three minor HSs (HS2, HS3 and HS5) near the promoter region. The HS4 was mapped just upstream from the promoter region and had the characteristics of a tissue-specific HS. The HS5 was located at the transcription start point, it included the TATA box and its presence was correlated with a promoter function. The duodenal chromatin contained two additional HSs, a major HS (HS1) located approx. 3.5 kb upstream from the cap site and a minor HS (HS6) in the second intron at +0.5 kb. Despite the marked effect of 1,25-dihydroxyvitamin D3 (DHD3) on the CaBP9k mRNA level, the pattern of HSs in duodenal chromatin was unchanged after stimulation with DHD3. The liver chromatin contained one major HS (HS1) identical to the duodenum HS1 (although this tissue does not express CaBP9k). It also contained a liver-specific HS (HS0) 0.1 kb upstream from HS1. The interaction of HS0 with HS1 could explain the absence of CaBP9k expression in the liver. Thus, specific sets of HSs are associated with various functional states of CaBP9k in a tissue-specific manner.

Amino Acid Sequence↗
PubMed1989

The human calbindin 27-kDa gene: structural organization of the 5' and 3' regions, chromosomal assignment, and restriction fragment length polymorphism.

The 5' and 3' regions of the human gene coding for calbindin 27 kDa were cloned and sequenced. Structural features of the 5' region included the presence of an Alu repeat and two elements regularly associated with eukaryotic promoters: an alternating purine-pyrimidine element and a homopurine-homopyrimidine box. The 3' region contained a second Alu family member and a degenerate 1.4-kb L1 repeat. A comparison with the chicken promoter was made in order to define regions conserved in evolution and potentially important in gene expression regulation. The greater similarity is located around the TATA box, but strongly conserved elements were not found. The gene was assigned to chromosome 8 by using human-rodent hybrid cell lines. Two restriction fragment length polymorphisms (HindIII and SacI) were detected with a cDNA probe recognizing the 3' end of the gene.

Amino Acid Sequence↗
PubMedDate not supplied

The relationship of calbindin-containing neurons with substance P, Leu-enkephalin and cholecystokinin fibres: an immunohistochemical study in the rat thalamus.

In the rat thalamus, immunoreactivity for the calcium binding protein calbindin (Cb) is mostly confined to neuronal cell bodies, sometimes revealing proximal dendrites, of the midline, intralaminar and posterior regions. Substance P (SP)-, cholecystokinin (CCK)- and Leu-enkephalin (L-ENK)-immunoreactive (ir) elements in the thalamus are fibre-like structures, intermingled with punctate elements probably representing axonal arborizations and their synaptic boutons. These peptidergic fibres are unevenly distributed in several thalamic domains, including the areas that contain Cb-ir neurons. The relationship between Cb-ir cell bodies and these three different peptidergic systems of thalamic innervation was studied with immunohistochemistry. Single-labelling experiments on adjacent sections and double immunostaining on the same section were performed. A considerable overlap between Cb-ir perikarya and SP-ir fibres was found in most thalamic nuclei. In particular, in the intralaminar nuclei and posterior complex, SP-ir punctate elements were frequently observed in close proximity to Cb-ir cell bodies and dendrites. On the other hand, no consistent topographical correspondence between Cb-ir perikarya and CCK- or L-ENK-ir fibres was evident. Altogether, the present data suggest a selective anatomical and, possibly, functional relationship between SP and Cb in at least a subpopulation of rat thalamic neurons.

Animals↗