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PubMed1990

Peptidyl-prolyl cis-trans isomerase does not affect the Pro-43 cis-trans isomerization rate in folded calbindin D9k.

The calcium-binding protein calbindin D9k has previously been shown to exist in two folded forms only differing in the proline cis-trans isomerism of the Gly-42-Pro-43 amide bond. This bond is located in a flexible loop connecting the two EF-hand Ca2+ sites. Calbindin D9k therefore constitutes a unique test case for investigating if the recently discovered enzyme peptidyl-prolyl cis-trans isomerase (PPIase) can affect the cis-trans exchange rate in a folded protein. The 1H NMR saturation transfer technique has been used to measure the rate of interconversion between the cis and trans forms of calbindin in the presence of PPIase (PPIase:calbindin concentration ratio 1:10) at 35 degrees C. No rate enhancement could be detected.

Amino Acid Isomerases↗
PubMed1987

Calbindin in vertebrate classes: immunohistochemical localization and Western blot analysis.

Calbindin immunoreactivity was investigated in various vertebrates. Positive labeling was observed in the absorptive cells of the duodenum of all birds and reptiles but not in mammals, amphibia, or fish. Staining was present in the kidney distal convoluted tubule from amphibia and higher vertebrates. Fish kidney was negative. In the central nervous system of all species investigated, cellular bodies and fibers were Calbindin positive. Their distribution was quite broad and correlates well with the previously reported mapping for chick and rat. Western blot analysis revealed two Calbindins in brain from mammals, birds, reptiles, and amphibia (27,000 and 29,000 Da). Only one band was detected in fish. We conclude that Calbindin from the evolutionary point of view is primarily a neuronal protein, with a highly conservative character.

Amphibians↗
PubMed1989

Tissue-specific regulation of the concentration of calbindin D28K mRNA in the developing chicken.

A BamHI-HindIII restriction fragment containing the 5'-terminal portion of the gene encoding chicken Calbindin D28K was sequenced and used as a probe in Northern-blot hybridizations to RNA extracted from the brain and intestine of chickens at various stages of development. In both tissues Calbindin D28K mRNA consists of a family of three species, which differ by size. In the intestine Calbindin D28K mRNAs appear at hatching and reach a peak at day 7. In the brain the same RNA species are easily detected at least 7 days before hatching, show a moderate increase at hatching and remain essentially constant during the first 10 days of adult life. The concentration of Calbindin D28K mRNAs in the intestine is strictly dependent on Vitamin D, while it is not in the cerebellum.

Animals↗
PubMed1990

Monoclonal antibodies directed against the calcium binding protein Calbindin D-28k.

We have produced 25 clones secreting antibodies directed against chicken Calbindin D-28k. Two of them, 300 and 318, recognize determinants conserved in fish, chicken, mouse, rat, rabbit, monkey and human Calbindin D-28k. We demonstrate their use in the immunohistochemical localization of Calbindin D-28k, and in the detection of Calbindin D-28k on immunoblots.

Animals↗
PubMed1996

Barosensitive and chemosensitive neurons in the rat medulla: a double labeling study with c-Fos/glutamate, GAD, PNMT and calbindin.

The purpose of this study was to survey distribution and density of the barosensitive and chemosensitive neurons in the medulla of rats anesthetized with fentanyl/midazolam, using immunohistochemical methods. After stimulation of the arterial baroreceptor or the chemoreceptor, we identified c-Fos-labeled neurons with immunoreactions to antisera of glutamate. PNMT, GAD and calbindin in the nucleus tractus solitarii (NTS) and the ventrolateral medulla (VLM). The double labeled neurons were located in the medical part of the NTS, and in the lateral part of the paragigantocellular reticular nucleus and the ventral division of the ambiguus nucleus. Main findings were as follows: (1) No significant difference was found in distribution and density of glutamatergic, adrenergic and calbindin-containing neurons between the barosensitive and chemosensitivie types; (2) a few GABAergic neurons were distributed almost evenly in the NTS and VLM, and in these neurons the barosensitive type outnumbered the chemosensitive one; (3) glutamatergic and calbindin-containing neurons were dominant in the NTS; adrenergic neurons in the VLM. (4) as for the adrenergic neurons in the NTS, the chemosensitive type significantly outnumbered the barosensitive one. This study showed that distribution and density of the barosensitive neurons, either glutamatergic, adrenergic, or calbindin-containing neurons, overlapped with those of the chemosensitive corresponding neurons, suggesting presence of the neural matrix of the cardiopulmonary interaction. Exceptionally, the number of the barosensitive GABAergic neurons was significantly larger than that of the chemosensitive GABAergic ones.

Animals↗
PubMed1993

Reduction of calbindin-28k mRNA levels in Alzheimer as compared to Huntington hippocampus.

Disturbances in calcium homeostasis have been observed to be associated with Alzheimer's and other neurodegenerative diseases. Increased total calcium levels and decreased levels of calcium binding proteins have been found in Alzheimer brain tissue. However, the mechanism behind these disturbances remain unknown. In situ hybridization with tritiated antisense RNA probes for the calcium binding proteins, calbindin-28k and calmodulin, was used to examine the expression of genes coding for these proteins in Alzheimer and Huntington brain tissues matched for age, agonal process and autopsy interval. mRNA levels for calbindin-28k were reduced by 35% in CA1 and CA2 regions of Alzheimer hippocampus, as compared to Huntington control. In contrast, calmodulin expression was unchanged in CA1 but reduced by 30% in CA2. mRNA expression of calbindin-28k and calmodulin in Alzheimer temporal cortex did not differ from control. There were no significant differences in calcium binding protein message levels in cerebellar Purkinje cells between Alzheimer and Huntington control. There was no correlation between calcium binding protein message levels and brain weight, autopsy interval, patient age or the extent of neurofibrillary degeneration. Instead, decreased calbindin-28k expression in Alzheimer-affected hippocampus was due to an increase in the percentage of neurons expressing lower message levels for these proteins.

Aged↗
PubMed1991

Transfection of avian vitamin D-dependent calbindin-D28K 5' flanking promoter sequence in primary chick kidney cells.

Expression of the vitamin D induced calbindin-D28K protein is transcriptionally controlled by the steroid hormone 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) in a tissue-specific manner in the intestine and kidney. In order to examine the cis-acting elements of the calbindin-D28K promoter and its modulation by 1,25-dihydroxyvitamin D3, chimeric plasmids containing 2.1 kb of 5' flanking region linked to the reporter gene chloramphenicol acetyl transferase (CAT) were transfected by lipofection into primary cultures of chick kidney cells. Transfected chick kidney cells exhibited a high basal expression of the chloramphenicol acetyl transferase gene, reflecting the strong activity of the calbindin-D28K promoter. Expression of the pCaBP2.1 reporter gene was increased 2-fold in the presence of the hormone 1,25(OH)2D3 in the primary kidney cells. Deletion of a 1.42 kb fragment ending -679 base pairs upstream from the transcription start site led to a 2-fold repression in the reporter gene activity by the hormone 1,25(OH)2D3 in primary chick kidney cultures. These preliminary results suggest that both positive and negative elements normally act to regulate the expression of the calbindin-D28K gene in primary chick kidney cells.

Animals↗
PubMed1991

Sequences near the CCAAT region and putative 1,25-dihydroxyvitamin D3-response element and further upstream novel regulatory sequences of calbindin-D28k promoter show DNase I footprinting protection.

1,25-Dihydroxyvitamin D3, the hormonally active form of vitamin D (1,25(OH)2D3), plays a major role in the transcriptional regulation of the vitamin D-induced calcium binding protein calbindin-D28k in the chick intestine. Sequence-specific protein-DNA interactions within the promoter of the calbindin-D28k gene were studied by DNAse I footprinting analysis to obtain information on the mechanism by which the 1,25(OH)2D3 receptor and other transcription factors regulate its expression. Restriction fragments spanning nucleotides -679 to +44 of the calbindin-D28k gene were used as probes Intestinal nuclear extracts prepared from vitamin D-deficient chicks generated several protected regions. Two prominent areas of protection against DNase I digestion were located at nucleotides -595 to -572 (21 bp) and -372 to -337 (36 bp). The -372 to -337 protected segment includes a CACCC sequence motif. Additional protection regions (-333/-328, -319/-315 and -308/-304) were observed within and near the candidate chicken calbindin-D28k 1,25(OH)2D3-response element (-329/-313) and the CCAAT box (-326/-322). DNase I digestion patterns obtained with liver nuclear extracts, containing low levels of 1,25(OH)2D3 receptor, revealed weaker protein-DNA interactions in these regions.

Animals↗
PubMed1994

All calbindin-immunoreactive myenteric neurons project to the mucosa of the guinea-pig small intestine.

The projections of Dogiel type II myenteric neurons to the mucosa of the guinea-pig ileum were quantified by combining retrograde transport of DiI, in vitro, with immunohistochemistry. After DiI application to the mucosa over an area of 1.5 x 10 mm2, virtually all (> 97%) calbindin-immunoreactive Dogiel type II neurons in the myenteric plexus underneath the mucosal DiI application site were labelled, indicating that essentially all of these neurons project to the mucosa. From cell counts, on average 5 calbindin-immunoreactive neurons project to each villus, and each calbindin-immunoreactive neuron supplies on average 10 villi. Since Dogiel type II neurons that were not immunoreactive for calbindin (19% of all labelled nerve cells) also projected to the mucosa, it is likely that all Dogiel type II neurons, which are putative sensory neurons of the gut, project to the mucosa.

Animals↗
PubMed1994

The 9-kDa calbindin gene of Rousettus aegyptiacus: its identification and isolation from a genomic library.

A genomic library of the fruit bat (Rousettus aegyptiacus) was constructed in lambda phage gt11. The titre of the library was determined to be 2 x 10(5) pfu/ml. The genomic library was amplified and the titre of the amplified library increased 300-fold to 7 x 10(7) pfu/ml. The library was screened by in situ hybridization techniques using a fragment of the mouse 9-kDa calbindin cDNA as a probe. Screening of 10(5) plaques yielded a positive clone. Three additional rounds of screening were performed to purify the positive. Lambda phage DNA was isolated from the positive clone and restriction digest analysis, followed by hybridization studies, was performed on these digests in order to determine the location of the bat 9-kDa calbindin gene in the insert of the lambda phage vector. Restriction maps so derived were interpreted from the published sequence for the rat 9-kDa calbindin gene and indicate the successful isolation of the 9-kDa calbindin gene of Rousettus aegyptiacus.

Animals↗
PubMed1988

Calbindin D-28k-immunoreactive neurons in chick dorsal root ganglion: ontogenesis and cytological characteristics of the immunoreactive sensory neurons.

The expression of calbindin (28,000 mol. wt Vitamin D-dependent calcium binding protein) was studied in sensory neurons of the chick dorsal root ganglion by combining immunocytochemical and ultrastructural features. In the chick embryo at E10, about 20% of the neuroblasts were immunostained with antibodies raised to calbindin. After hatching, two subpopulations of primary sensory neurons were labeled with calbindin-antibodies and could be identified: the large Al cell bodies (6%) mainly characterized by huge blocks of rough endoplasmic reticulum and the small B1 cell bodies (14%) which contain parallel cisternae of rough endoplasmic reticulum. The other neuronal cell types A2 and B2 were devoid of any immunostaining. Thus, calbindin is an early and reliable marker of two subclasses of primary sensory neurons in the chick dorsal root ganglion.

Animals↗
PubMed1994

Chronic intrastriatal quinolinic acid produces reversible changes in perikaryal calbindin and parvalbumin immunoreactivity.

We recently reported the use of a chronic dialytic delivery system for intrastriatal administration of quinolinic acid in the rat. This system produces neurodegeneration with some characteristics similar to post mortem brain tissue from Huntington's disease patients, including reduced cytochrome oxidase staining, a decreased number of Nissl-stained neurons, and relative sparing of striatal NADPH-diaphorase containing neurons. The present findings show that chronic dialytic delivery of quinolinic acid also produces a Huntington's disease-like pattern of reduced calbindin and parvalbumin perikaryal immunoreactivity that is reversed in rats allowed four to eight weeks' recovery after cessation of quinolinic acid. Furthermore, cytochrome oxidase staining and the number of Nissl-stained cells were unchanged in the region of transient calbindin and parvalbumin immunoreactive perikaryal staining alterations. These results suggest that changes in calbindin and parvalbumin perikaryal immunoreactivity provide a relatively sensitive measure of quinolinic acid induced neurotoxicity. The reversible nature of reduced perikaryal immunoreactivity suggests a premorbid state of neurotoxicity, possibly marked by cellular redistribution of calbindin and parvalbumin.

Animals↗
PubMed1988

Calbindin (CaBP 28 kDa) localization in the peripheral vestibular system of various vertebrates.

Previous reports on calbindin, a 28 kDa vitamin D-induced calcium-binding protein, located in the mammalian peripheral vestibular system indicated that it is specifically distributed and postulated that it could play a role in the electrophysiological functioning of the sensory cells. This immunocytochemical investigation of the distribution of calbindin in the vestibular system of various vertebrates: fishes (goldfish and sea-perch), amphibia (frog), birds (chicken) and mammals (mouse, cat and baboon), was performed to verify these observations. In the vestibular ganglion, only a few neurons were faintly immunoreactive in the fishes and the frog, while the staining was more intense but still not present in all neurons of the chicken, the mouse and the cat. All the neurons were immunoreactive in the baboon. No immunoreactivity was observed in the sensory epithelia of the fishes. All hair cells were strongly immunoreactive in the frog. In the other species, most of the hair cells in the cristae were immunostained except those situated in the peripheral areas. In the maculae, the hair cells of the striola were either the only ones stained or were more intensely stained or were more intensely stained than the others. The localization of calbindin in specific cellular types and its increasing abundance from the fishes to the mammals suggest that calbindin is associated with the capacity of sensory and nerve cells to analyze precise mechanical or biochemical stimulations.

Animals↗
PubMedDate not supplied

Parvalbumin and calbindin in the rat claustrum: an immunocytochemical study combined with retrograde tracing frontoparietal cortex.

The distribution of the calcium binding proteins parvalbumin and calbindin D-28k was examined in the claustrum of the rat by means of immunohistochemistry. The two proteins displayed a different and largely complementary pattern of distribution. Parvalbumin-immunostaining was intense in the neuropil of the dorsal claustrum and virtually absent in the neuropil of the ventral claustrum; parvalbumin-immunoreactive neuronal cell bodies were relatively numerous in the dorsal claustrum and were detected only occasionally in the ventral region. On the other hand, calbindin-immunostaining was prevalent in the ventral claustrum; very few calbindin-positive neurons were seen in the dorsal sector of the nucleus, whereas they were relatively more numerous in the ventral claustrum. The cell bodies of the majority of the claustral parvalbumin- or calbindin-immunoreactive neurons were oval or round, but immunostained polymorphous neurons were also observed. The surface of the immunopositive dendritic branches was smooth, with no evidence of spines. Fluorescent retrograde tracing was combined with immunohistofluorescence to determine whether the parvalbumin-containing claustral cells project to the frontoparietal cortex. Neurons labelled after large fluorogold injections in frontoparietal cortical fields were highly intermingled in the dorsal claustrum with parvalbumin-immunoreactive cells but the two neuronal populations were separate. These data show that parvalbumin-immunoreactive claustral neurons do not project to the frontoparietal cortex. In addition, although these cells may project to other cortical or subcortical targets, the present findings suggest that they may represent, at least in part, local circuit claustral neurons, corresponding to the aspiny intrinsic neurons described in the rat claustrum in studies based on Golgi impregnation.

Animals↗
PubMed1996

Distribution of NADPHdiaphorase and calbindin-D28k neurons in the lateral septal area of the guinea pig, with special reference to the enkephalinergic hypothalamo-septal tract.

Nicotinamide adenine dinucleotide phosphate-diaphorase (NADPHd) histochemical techniques were used to identify neurons synthesizing nitric oxide in the lateral septum of the guinea pig. Double immunocytochemical procedures were used to detect neurons immunoreactive for calbindin-D28k and enkephalinergic fibers which project to the lateral septum. The present data demonstrate that (1) the neurons containing NADPH diaphorase and the neurons immunoreactive for calbindin-D28k are observed in discrete regions of the lateral septum; (2) these populations overlap in various areas of the lateral septum including its dorsal and mediolateral parts; (3) NADPH diaphorase and calbindin-D28k are colocalized in neurons located in the overlapping areas; (4) neurons identified by the presence of calbindin-D28k, NADPH diaphorase or both substances, are surrounded by enkephalinergic fibers. These observations indicate the chemical heterogeneity of the lateral septum and suggest that the enkephalinergic hypothalamo-septal tract does not preferentially contact a subpopulation of neurons.

Animals↗
PubMed2006

Developmental changes in the expression of calbindin and potassium-channel subunits Kv3.1b and Kv3.2 in mouse Renshaw cells.

One class of spinal interneurons, the Renshaw cells, is able to discharge at very high frequencies in adult mammals. Neuronal firing at such high frequencies requires voltage-gated potassium channels to rapidly repolarize the membrane potential after each action potential. We sought to establish the pattern of expression of calbindin and potassium channels with Kv3.1b and Kv3.2 subunits in Renshaw cells at different developmental stages of postnatal mice. The pattern of expression of calbindin changed dramatically during early postnatal development. An adult pattern of calbindin reactive neurons started to emerge from postnatal day 10 to postnatal day 14, with cells in laminae I and II of superficial dorsal horn and the ventral lamina VII. Renshaw cells were identified immunohistochemically by their expression of calbindin and their location in the ventral horn of the spinal cord. Western blot results of the lumbar spinal cord showed that Kv3.1b expression became faintly evident from postnatal day 10, reached a maximum at postnatal day 21 and was maintained through postnatal day 49. Double labeling results showed that all Renshaw cells expressed Kv3.1b weakly from postnatal day 14, and strongly at postnatal day 21. Western blot results showed that Kv3.2 expression became detectable in the lumbar cord from postnatal day 12, and increased steadily until reaching an adult level at postnatal day 28. In contrast to the Kv3.1b results, Kv3.2 was not expressed in Renshaw cells, although some neurons located at laminae VIII and VI expressed Kv3.2. We conclude that Renshaw cells express Kv3.1b but not Kv3.2 from postnatal day 14.

Age Factors↗
PubMed2003

Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.

Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts with Ran-binding protein M, a protein known to play a role in microtubule function. Using NMR methods, we show that a peptide, LASIKNR, derived from Ran-binding protein M, interacts with several regions of the calcium-loaded protein including the amino terminus and two other regions that exhibit conformational exchange on the NMR timescale. We suggest that the interaction between calbindin D(28K) and Ran-binding protein M may be important in calbindin D(28K) function.

Adaptor Proteins, Signal Transducing↗
PubMed2000

Nitric oxide synthase interneurons in the monkey cerebral cortex are subsets of the somatostatin, neuropeptide Y, and calbindin cells.

99%) immunoreactive for somatostatin and neuropeptide Y, but did not express calbindin. The LNOS cells comprised about 30% of the somatostatin cells and about 60% of the neuropeptide Y cells. The SNOS cells were nearly always (87-98%) calbindin-immunoreactive, and were rarely or never labeled with antibodies to somatostatin or neuropeptide Y. The SNOS cells accounted for about 20% of all of the calbindin cells. The findings demonstrate that the two types of nNOS cells can be distinguished by antibodies to calbindin, somatostatin and neuropeptide Y, but none of these markers is found exclusively in nNOS cells. Nevertheless, neuropeptide Y-immunoreactivity provides a useful marker for LNOS cells, because it is very dense in these cells and only light in the interneurons that lack nNOS.

Animals↗