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PubMed1996

Calbindins decreased after space flight.

Exposure of the body to microgravity during space flight causes a series of well-documented changes in Ca2+ metabolism, yet the cellular and molecular mechanisms leading to these changes are poorly understood. Calbindins, vitamin D-dependent Ca2+ binding proteins, are believed to have a significant role in maintaining cellular Ca2+ homeostasis. In this study, we used biochemical and immunocytochemical approaches to analyze the expression of calbindin-D28k and calbindin-D9k in kidneys, small intestine, and pancreas of rats flown for 9 d aboard the space shuttle. The effects of microgravity on calbindins in rats from space were compared with synchronous Animal Enclosure Module controls, modeled weightlessness animals (tail suspension), and their controls. Exposure to microgravity resulted in a significant and sustained decrease in calbindin-D28k content in the kidney and calbindin-D9k in the small intestine of flight animals, as measured by enzyme-linked immunosorbent assay (ELISA). Modeled weightlessness animals exhibited a similar decrease in calbindins by ELISA. Immunocytochemistry (ICC) in combination with quantitative computer image analysis was used to measure in situ the expression of calbindins in the kidney and the small intestine, and the expression of insulin in pancreas. There was a large decrease of immunoreactivity in renal distal tubular cell-associated calbindin-D28k and in intestinal absorptive cell-associated calbindin-D9k of space flight and modeled weightlessness animals compared with matched controls. No consistent difference in pancreatic insulin immunoreactivity between space flight, modeled weightlessness, and controls was observed. Regression analysis of results obtained by quantitative ICC and ELISA for space flight, modeled weightlessness animals, and their controls demonstrated a significant correlation. These findings after a short-term exposure to microgravity or modeled weightlessness suggest that a decreased expression of calbindins may contribute to the disorders of Ca2+ metabolism induced by space flight.

Animals↗
PubMed1991

In situ hybridization histochemistry of Spot 35 protein, a calcium-binding protein, in the rat brain.

Using in situ hybridization, we analyzed the localization of mRNA for Spot 35 protein (Spot 35), a calcium-binding protein of the EF-hand type, in the rat cerebellum at various developmental stages. A cDNA fragment corresponding to part of the 3'-noncoding region was 35S-labeled and used as a hybridization probe. Autoradiographic signals for Spot 35 mRNA were detected in all the Purkinje cells, but not in any other neurons or glial cells in the adult rat cerebellum. There was no significant difference in signal intensity among individual cells. The signals were observed exclusively in Purkinje cell bodies, but not in their processes, in striking contrast to previous immunohistochemical studies in which Spot 35 protein was demonstrated in both cell bodies and processes. In the time-course study, signals for Spot 35 mRNA were detected in Purkinje cell bodies weakly at embryonic day 19, thereafter more intensely at more developed stages and most intensely at postnatal days 30 and 60 (adulthood). The signal intensities of individual cells were similar at each of these developmental stages except for the very early stages at which signals were weak and slightly variable among cells. These findings, especially that of the characteristic coordinated expression of Spot 35 mRNA at given stages, should prove useful in studies of degenerative diseases in the cerebellum in experimental animals and man. A weak expression of Spot 35 mRNA in some of non-Purkinje cells was also noted.

Animals↗
PubMed2000

Cerebellar degeneration in hereditary dentatorubral-pallidoluysian atrophy and Machado-Joseph disease.

We examined the mechanism of cerebellar degeneration in brains obtained at autopsy from six cases of hereditary dentatorubral-pallidoluysian atrophy (DRPLA) and six cases of Machado-Joseph disease (MJD), using terminal deoxynucleotidyltransferase-mediated in situ nick end labeling (TUNEL) and immunohistochemistry for apoptosis-related proteins, neurotrophin receptors and glutamate transporters. In three subjects with DRPLA, who developed dementia and cerebellar ataxia at over 50 years of age, the number of Purkinje cells was mildly reduced, TUNEL-positive cells were observed in the molecular layer of the cerebellar cortex, and immunoreactivities for calbindin D28K and excitatory amino acid transporter-1 (EAAT1) were altered in the molecular layer. In addition, all cases of DRPLA showed a reduction of immunoreactivity for EAAT1 in the dentate nucleus. In MJD, augmentation of Bcl-x expression by the Purkinje cells, and increases in Trk B- and GFAP-immunopositive glial cells in the granular layer were observed in half of the cases, whereas immunoreactivity for EAAT-1 was preserved both in the cerebellar cortex and dentate nucleus. One case of MJD showed TUNEL-positive granular cells in the cerebellar cortex. Age-matched control subjects did not show TUNEL-positive cells or immunohistochemical changes in the cerebellum. There were neither TUNEL-positive cells nor alteration of the in situ expression of apoptosis-related proteins in the dentate nucleus in either variant of hereditary spinocerebellar degeneration, although both exhibited grumose degeneration in the dentate nucleus. These findings indicate that latent degeneration in the cerebellar cortex may occur in DRPLA and MJD, in addition to the dentate change, which is the cardinal feature in the neuropathology of these two diseases. The lesion of Purkinje cells and their processes in the molecular layer associated with altered glutamate transport may be important in DRPLA, while the significance of the abnormalities observed in some MJD cases, which might be related to apoptotic mechanism, remains unclear.

ATP-Binding Cassette Transporters↗
PubMed2005

Cerebellopontine calcification: a new entity of idiopathic intracranial calcification?

We report the autopsy case of a 40-year-old woman with severe intellectual and motor disabilities, who showed calcification in the cerebellum and pons but not in the basal ganglia on CT scan, and died of intracranial hemorrhage due to intractable hypertension. At autopsy, numerous calcium deposits were noted in the cerebellar cortex, the dentate nucleus, the cerebellar white matter and the ventral pons. These deposits were distributed both in the neuropil and the white matter, but rarely within the arterial walls or in contact with capillaries. This weak relationship between calcification and the blood vessels, in addition to the paucity of basal ganglia calcification, is in contrast to the findings with other disorders involving intracranial calcification, including Fahr's disease and calcium metabolism disorders. Immunohistochemistry revealed intense staining of calbindin-D28K and parvalbumin at sites of calcium deposits both in the present case and in a case of pseudohypoparathyroidism, whereas these proteins were not localized to calcium deposits in the cerebellum of a Fahr's disease brain. We propose that the present case may represent a distinct entity among diseases characterized by idiopathic intracranial calcification. In addition, calcium-binding proteins may be involved in the calcification process in some cases with intracranial calcification.

Adult↗
PubMed1998

Phenytoin alters Purkinje cell axon morphology and targeting in vitro.

In adult mice, administration of the anticonvulsive drug phenytoin caused focal swellings along the Purkinje cell axon correlated with ataxia and incoordination of movements. In our model, we used murine cerebellar slice cultures to study the influence of phenytoin on postnatal Purkinje cell axon differentiation. Almost all of our untreated cultures developed to mature-like cerebellar tissue. Immunohistochemistry with anti-calbindin-D28k or UCHTI (anti-CD3) antibodies revealed numerous Purkinje cell axons in the white matter. In the area of the deep cerebellar nuclei, immunolabelled axons formed a large axonal plexus. The few neurofilament-positive neurons in this area were densely covered with Purkinje cell axon terminals. The synaptophysin immunoreactivity revealed connections between the terminals and the neurons of the deep cerebellar nuclei. Treatment of cerebellar slice cultures with phenytoin (10-80 microM) for 10-16 days resulted in focal swellings of different size along the axon. The number of swellings increased with an increasing dosage. At concentrations of 40 microM phenytoin, Purkinje cell axons seemed to be unable to invade the deep cerebellar nuclei, but numerous aberrant, recurrent collaterals could be detected immunohistochemically with the two specific Purkinje cell antibodies. Possible cytotoxic effects after treatment, such as dendritic degeneration and a decrease in the number of immunolabelled Purkinje cells, were observed above 40 microM phenytoin. These data suggest that the response of juvenile Purkinje cells is dependent upon the dosage of the antiepileptic drug because of morphological alterations as well as a misrouting of previously established connections.

Adult↗
PubMed1999

Immunohistochemical evaluation of the marbled state in childhood hypoxic encephalopathy.

We have immunohistochemically analyzed the marbled state in 8 cases of perinatal hypoxic ischemic encephalopathy and 4 cases of infantile hypoxic encephalopathy, using antibodies against calbindin-D28k (CaBD), glial fibrillary acidic protein (GFAP), methionine-enkephalin (MEnk), myelin basic protein (MBP), neurofilament (NF), parvalbumin (PV), substance-P (SuP) and synaptophysin (SP). The marbled state was found in the thalamus in 11 cases, whose age at death was over 10 years. Four cases demonstrated the marbled state in the cerebral cortex, in addition to the striatum and/or the thalamus. The abnormally myelinated fibers in the marbled state were stained with both Kluver-Barrera and Holzer stainings; however, they were partly immunopositive for MBP and completely immunonegative for GFAP, CaBD, MEnk, PV, SuP and SP, although some of the neurons and/or fibers showed immunoreactivities for those calcium-binding proteins and/or neurotransmitters. The axons were visualized in the abnormally myelinated fibers by Bodian staining and/or anti-NF immunostainings in the cerebral cortex and striatum but not in the thalamus. GFAP-positive astrocytes did not show any continuity with the abnormally myelinated fibers. These histological features were seen in the cerebral cortex, striatum and thalamus. Difference of the etiology did not affect the histological features with the exception of anti-PV staining, in which PV-immunopositive neurons were observed only in aged subjects with infantile hypoxic encephalopathy, and seemed to be more severely affected by hypoxic stress during the perinatal period than the early infantile period. These data suggest that the site of lesion or the length of survival period after brain injury might influence the formation of the marbled state rather than the etiology. And the direct relationship between the abnormally myelinated fiber and astrocytic process was not verified.

Adolescent↗
PubMed1997

Localization of calbindin-D28k in normal and incised mouse skin: immunohistochemical and immunoblot analysis.

The subcellular localization of the protein calbindin-D28k in normal and incised mouse skin was investigated by immunohistochemical staining and immunoblot analysis. In normal skin, the presence of calbindin-D28k was demonstrated in both the nucleus and the cytoplasm of epidermal keratinocytes. Higher levels of calbindin-D28k were detected in the nucleus than in the cytoplasm. Following incision, the levels of calbindin-D28k were significantly decreased in epidermal keratinocytes, particularly in the nucleus, compared with those in normal skin. The immunohistochemical staining and immunoblot analysis showed nuclear calbindin-D28k to be decreased or absent during a 10-day observation period following skin incision. Based on these findings, it is suggested that calbindin-D28k may be distributed in both the nucleus and cytoplasm of epidermal keratinocytes in mice, and this protein may be involved in active cell proliferation of the epidermis induced by skin incision.

Animals↗
PubMedDate not supplied

Subcellular localization of specific mRNAs and their protein products in Purkinje cells by combined fluorescence in situ hybridization and immunocytochemistry.

In this study we have investigated the subcellular distribution of two mRNAs coding for the Purkinje cell-specific proteins, calbindin D28K and L7 (L7/pcp-2). Whereas calbindin mRNA was found to be in the cell body only, L7 transcripts could be detected within the molecular layer, corresponding to Purkinje cell dendrites. We have now combined a highly sensitive fluorescence-based in situ hybridization protocol with immunofluorescence in conjunction with confocal optical sectioning to analyze the precise localization of these mRNAs in individual Purkinje neurons. We show that L7 mRNA is localized in clusters within the proximal and distal branches of dendrites, but also in the proximal part of Purkinje cell axons. In contrast, calbindin transcripts are restricted to the axonal pole of the perikaryon. Purkinje cells grown in primary cultures reveal similar mRNA distribution patterns for the two transcripts. Thus, the mechanism underlying localization of mRNA within Purkinje cells seems to function in a cell-intrinsic manner, guiding specific transcripts, such as L7 mRNA, to neuronal processes while restricting others, such as calbindin mRNA, to the perikaryon.

Alkaline Phosphatase↗
PubMed1998

Calcium-binding proteins in the retina of a calbindin-null mutant mouse.

Calcium-binding proteins are abundantly expressed in many neurons of mammalian retinae. Their physiological roles are, however, largely unknown. This is particularly true for calcium-modulating proteins ("calcium buffers") such as calbindin D28k. Here, we have studied retinae of wildtype (+/+) and calbindin-null mutant (-/-) mice by using immunocytochemical methods. Although calbindin immunoreactivity was completely absent in the calbindin (-/-) retinae, those cells that express the protein in wildtype retinae, such as horizontal cells, were still present and appeared normal. This was verified by immunostaining horizontal cells for various neurofilament proteins. In order to assess whether other calcium-binding proteins are upregulated in the mutant mouse and may thus compensate for the loss of calbindin, mouse retinae were also immunolabeled for parvalbumin, calretinin, and a calmodulin-like protein (CALP). In no instance could a change in the expression pattern of these proteins be detected by immunocytochemical methods. Thus, our results show that calbindin is not required for the maintenance of the light-microscopic structure of the differentiated retina and suggest roles for this protein in retinal function.

Animals↗
PubMed1999

Immunohistochemical localization of calbindin D28k during root formation of rat molar teeth.

The present study was undertaken to examine the localization of calbindin D28k (CB)-like immunoreactivity (-LI) during the root formation of the rat molar. In the adult rat, CB-LI was detected in some of the cells of the epithelial rest of Malassez at the bifurcational region and in certain cells between the root dentin and cementum at the apical region. These cells had indented nuclei and many tonofilaments, and cementocytes lacked CB-LI. Moreover, CB-LI was observed in the periodontal fibroblasts in the alveolar half of the apical region. During root formation, the cells in the Hertwig's epithelial root sheath (HERS) lacked CB-LI, but most fragmented cells along the root surface began to express CB-LI when HERS was disrupted. Preodontoblasts and odontoblasts at the apical portion of the root also showed CB-LI. After the formation of cellular cementum, the CB-immunoreactive (-IR) cells were entrapped between the root dentin and cementum in the apical portion of the root. The number of CB-IR cells at the root surface decreased gradually, while that between the root dentin and cementum increased. The fibroblasts in the periodontal ligament began to express CB-LI after commencement of the occlusion, and the number and the staining intensity of CB-IR fibroblasts increased gradually with the passage of time. The present results suggest that CB may play an important role in the survival of the epithelial cells, in the cellular responses of periodontal fibroblasts against mechanical forces caused by the occlusion, and in the initial mineralization by the odontoblasts through the regulation of intracellular Ca(2+) concentration.

Animals↗
PubMed1991

Subcellular co-localization and co-variations of two vitamin D-dependent proteins in rat ameloblasts.

The immunocytochemical patterns of calbindin-D9k (CaBP 9k) and calbindin-D28k (CaBP 28k) were compared by light and electron microscopy throughout amelogenesis. Labelling on serial sections and co-localization of CaBPs confirmed that the two proteins were restricted to a single cell type, the ameloblasts. Their quantity increased during presecretion, was stable during secretion and alternately high and low during the cyclic modulation of ameloblasts which occurs during maturation. Ruffle-ended ameloblasts contained the highest apparent concentration. Investigations with several fixatives indicated that the CaBPs were present in the cytosol and the nucleus, although there were slight differences with various fixatives by light microscopy. Their concentrations in these compartments varied in parallel throughout amelogenesis. However, mitochondria contained only immunoreactive CaBP 9k. While the distribution of CaBP 9k in zones containing Golgi apparatus and rough endoplasmic reticulum was similar, CaBP 28k concentration has, in another paper, been shown to be higher near the rough endoplasmic reticulum.

Amelogenesis↗
PubMed1988

Loss of calbindin-28K immunoreactive neurones from the cortex in Alzheimer-type dementia.

An antibody raised against chick intestinal calbindin D28K was used to study the number and size of calbindin immunoreactive neurones in postmortem human brains from neurologically normal controls and from patients with neuropathologically diagnosed Alzheimer-type dementia (ATD). In the controls, calbindin immunoreactive neurones were observed in all cerebral cortex areas examined including the frontal, temporal and parietal cortices. When compared with the controls, the number and size of calbindin immunoreactive neurones were significantly reduced in the cortices of patients with ATD. These findings suggest that calbindin containing neurones are affected in ATD.

Aged↗
PubMed1989

Effects of altered thyroid states and undernutrition on the calbindin-D28K (calcium-binding protein) content of the hippocampal formation in the developing rat.

A quantitative study of calbindin-D28K (calcium-binding protein) was carried out on the developing hippocampal formation in normal, hypothyroid, hyperthyroid, and underfed rats. In normal animals, the calbindin-D28K content increased after birth in agreement with the distribution of the protein previously reported by immunocytochemistry. Calbindin-D28K was strikingly spared, compared to the other proteins, from the effects of hypothyroidism. On the contrary, the calbindin-D28K:protein ratio was transiently reduced by hyperthyroidism. Corrective doses of thyroxine to hypothyroid rats increased the calbindin-D28K content whatever the period of the hormonal treatment, but they also had a marked effect on the hippocampal weight and the protein content, especially when the hormone was given on days 2-3. With this latter replacement therapy schedule, the calbindin-D28K:protein ratio dropped from the high value of the hypothyroid animal to normal. Taken together, the results obtained in hypothyroidism, hyperthyroidism and replacement therapy are consistent with a pronounced action of thyroid hormone on hippocampal structures other than those containing calbindin-D28K. Undernutrition, which, like hypo- or hyperthyroidism, also markedly impairs hippocampal growth, affected the calbindin-D28K content per hippocampus but not the calbindin-D28K:protein ratio. This emphasizes the unique influence of thyroid hormone on brain development. The relative preservation of calbindin-D28K in the hippocampal formation of animals lacking thyroid hormone suggests that calbindin-D28K function may be crucial in this brain region.

Animals↗
PubMed1989

Calbindin-immunoreactive cholinergic neurones in the nucleus basalis of Meynert in Alzheimer-type dementia.

An antibody to the calcium binding protein, calbindin D28K (CaBP), was used to study the number and size of CaBP-immunoreactive neurones in the nucleus basalis of Meynert (nbM) of postmortem human brains from neurologically normal controls and from patients with neuropathologically diagnosed Alzheimer-type dementia (ATD). In controls, almost all the large neurones and their processes in the nbM were CaBP immunoreactive. Compared to neurologically normal controls the number of CaBP-immunoreactive neurones in the nbM in patients dying with ATD was significantly reduced and there was a clear loss of the majority of CaBP immunoreactive neurones. The few remaining nbM CaBP immunoreactive neurones in the ATD cases were smaller than those in the neurologically normal controls. Double-staining experiments revealed that many of the nbM CaBP-immunoreactive neurones contained choline acetyltransferase immunoreactivity, so that CaBP is an alternative marker for the nbM cholinergic neurones in the human fore-brain. These findings suggest that a disturbance in calcium homeostasis may be a possible factor contributing to the loss of these cholinergic/CaBP-containing neurones.

Adult↗
PubMed1989

Long-term structural changes in the rat hippocampal formation following cerebral ischemia.

Histological and immunohistochemical techniques were used to investigate the long-term structural changes that occur in the rat hippocampal formation following the induction of transient forebrain ischemia. Histological analysis showed that after 6-12 months cell loss was still largely restricted to the CA1 region but within this region degeneration was progressive and culminated in a severe shrinkage of the stratum oriens and stratum radiatum. Using the immunohistochemical markers calbindin-D28K and parvalbumin, we were able to demonstrate some of the structural changes that reflect this shrinkage. Calbindin immunohistochemistry clearly illustrated that the shrinkage was primarily due to the loss of the pyramidal neurons and the framework normally provided by their long apical dendrites. Parvalbumin immunostaining demonstrated that although a few GABAergic interneurons survived the insult, their terminal network was reduced greatly and the dendrites which normally extended the length of the stratum radiatum were retracted. Additionally, the normally dense band of parvalbumin immunoreactivity in the stratum lacunosum-moleculare, thought to be indicative of a fiber bundle travelling through the CA1 region, was almost completely depleted. These data illustrate that the primary damage observed in the CA1 region following cerebral ischemia is not static but progressive and may thus have important functional implications.

Animals↗
PubMed1989

Immunocytochemical characterization of neuron-rich rat brain primary cultures: calbindin D28K as marker of a neuronal subpopulation.

The function in neurons of the vitamin D-dependent calcium ion-binding-protein of 28 kDa mol. wt., calbindin D28K, is unknown. In order to find a simple system for studying the function of this protein, neuron-rich primary cultures derived from brains of 16-day-old rat embryos were analyzed for the presence of calbindin D28K by immunocytochemical mono- and double-labelling techniques. The studies were carried out between the 5th and 23rd day after seeding. In contrast to the neuronal marker neuron-specific enolase which was found in nearly all cells in the culture, calbindin D28K was expressed only in a subpopulation of neurons. Calbindin D28K-positive cells were intensely stained in their cell bodies and were also stained in their processes. Astroglial cells identified by the presence of the processes. Astroglial cells identified by the presence of the specific marker glial fibrillary acidic protein did not express calbindin D28K. Therefore, calbindin D28K is a useful marker for defining a neuronal subpopulation in neuron-rich primary cultures. Such cultures may be employed as a tool in searching for function(s) of calbindin D28K.

Animals↗
PubMed1990

Calbindin D28K as a marker for the degeneration of the striatonigral pathway in Huntington's disease.

An antibody raised against the chick calcium-binding protein calbindin D28K was used in immunohistochemical studies of normal post mortem human brain and the brains of individuals with Huntington's disease. Calbindin D28K immunoreactivity in the caudate nucleus and putamen coincided with the distribution of areas of acetylcholinesterase staining termed the matrix. In the matrix, calbindin D28K immunoreactivity was present in medium-sized neurons, the major neuronal population, however a further minor population of more strongly stained large neurons was detected. In Huntington's disease there was a dramatic loss of the majority of matrix calbindin D28K immunoreactive neurons and a parallel loss of calbindin D28K immunoreactivity from the substantia nigra. In contrast to the medium-sized calbindin D28K immunoreactive neurons which degenerate in Huntington's disease, the larger immunoreactive neurons were relatively preserved.

Acetylcholinesterase↗