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PubMed1991

Immunoreactive calbindin-D9K in bone matrix vesicle.

This electron microscope study describes the subcellular occurrence and distribution of immunoreactive calbindin-D9K in the trabecular metaphyseal and compact cortical bone of normal rats, rachitic vitamin-D-deficient rats, and rachitic rats given 1,25-(OH)2D3. Undecalcified bones were embedded in Lowicryl K4M and calbindin-D9K antigenicity was detected by the protein A-gold method. Immunoreactive calbindin-D9K was localized in the cytoplasm and cell processes of osteoblasts and osteocytes. Immunoreactive calbindin-D9K was also found within matrix vesicles and calcifying matrix vesicles, where it lay over the needle-shaped crystallites, at the apparent site of initial crystal formation, but not along the whole crystallites. In fully mineralized bone it occurred at the same site, over the crystallites. Calibindin-D9K was vitamin-D-dependent in the osteoblasts and matrix vesicles, where its presence was correlated with the reappearance of crystallites in 1,25-(OH)2D3-treated vitamin-D-deficient rats. This suggests that immunoreactive calbindin-D9K is involved in mineral deposition in bone matrix vesicles. Abnormal intracellular calcification associated with calbindin-D9K antigenicity in the osteoblasts of 1,25-(OH)2D3-treated vitamin-D-deficient rats indicates that immunoreactive calbindin-D9K may also play a part in abnormal intracellular mineral deposition.

Animals↗
PubMed2004

Calbindin-immunopositive cells are cholinergic interneurons in the myenteric plexus of rabbit ileum.

The 28-kDa calcium-binding protein (calbindin) is a widely studied neuronal marker in the enteric nervous system of numerous species. Calbindin has previously been detected in myenteric neurons of rabbit ileum in which 3% of all myenteric neurons are calbindin-immunopositive. We have studied the detailed morphology and chemical coding of calbindin-immunopositive neurons in this segment of the gut. We have found calbindin immunoreactivity in both strongly and weakly stained neurons. Of these, the strongly immunoreactive neurons belong to the Dogiel type I category. These neurons project only to other ganglia and primary strands of the plexus and their processes never run to the muscle or mucosal layers. The neurons within this group are 29.5+/-6.6 microm in length and 14.7+/-3.8 microm in width. The second smaller group of immunoreactive cells (27%) label faintly and have different morphological properties. They are characterized by their round medium-sized cell bodies (long axis: 24.4+/-5.2 microm; short axis: 15.5+/-2.9 microm) and do not exhibit immunoreactivity either in their dendrites or in their axonal processes. Double-label studies show that all calbindin-immunopositive neurons lack immunoreactivity for nitric oxide synthase, vasoactive intestinal peptide and substance P but all are immunoreactive for the synthesizing enzyme of acetylcholine, choline acetyltransferase. Thus, populations of neurons containing calbindin are cholinergic interneurons in the myenteric plexus of rabbit ileum.

Animals↗
PubMed1995

Parvalbumin and calbindin D-28k in vagal and glossopharyngeal sensory neurons of the rat.

Parvalbumin- and calbindin D-28k-immunoreactivities (ir) were examined in the glossopharyngeal and vagal sensory ganglia (petrosal, nodose and jugular ganglia), the carotid sinus nerve and the carotid body. Parvalbumin-ir nerve cells were mostly localized in the petrosal and nodose ganglia and were rare in the jugular ganglion. Calbindin D-28k-ir nerve cells were found in moderate and large numbers in the petrosal and nodose ganglia, respectively. Only a few calbindin D-28k-ir nerve cells were observed in the jugular ganglion. The carotid sinus nerve and carotid body contained numerous calbindin D-28k-ir nerve fibers but few parvalbumin-ir nerve fibers. Studies of the coexistence of these calcium-binding proteins with calcitonin gene-related peptide (CGRP)- and tyrosine hydroxylase (TH)-ir showed that CGRP-ir was rarely colocalized in parvalbumin- or calbindin D-28k-ir nerve cells in the petrosal or nodose ganglion. Moreover, TH-ir was not generally contained in parvalbumin-ir nerve cells in the petrosal, nodose and jugular ganglia while a portion (15-19%) of calbindin D-28k-ir neurons in the petrosal and nodose ganglia colocalized TH-ir. These findings are consistent with the involvement of calcium-binding proteins, particularly calbindin D-28k, in the function of visceral sensory neural systems of the glossopharyngeal and vagus nerves and, perhaps, in baro- and chemoreceptor neurotransmission.

Animals↗
PubMed1995

Effect of treatment with the dihydropyridine-type calcium antagonist darodipine (PY 108-068) on the expression of calbindin D-28K immunoreactivity in the cerebellar cortex of aged rats.

The influence of long term treatment with the dihydropyridine-type Ca2+ antagonist darodipine (PY 108-068) on age-dependent changes in calbindin D-28K immunoreactivity in the cerebellar cortex of male Wistar rats was assessed. In 12-month-old rats used as an adult reference group, specific calbindin D-28K immunoreactivity was found within the cytoplasm of Purkinje neurons and their dendritic processes. The number of Purkinje neurons displaying calbindin D-28K immunoreactivity was decreased in the cerebellar cortex of aged in comparison with adult rats. The pattern of calbindin D-28K immunoreactivity was similar in the cerebellar cortex of 24-month-old rats (aged), although a significant decrease in the intensity of immunoreactivity was noticeable. Treatment of aged rats with darodipine for 6 months increased the percentage of immunoreactive Purkinje neurons and the intensity of calbindin D-28K immunoreactivity in the cytoplasm of Purkinje neurons. Calbindin D-28K is a Ca2+ binding protein probably involved in the modulation of Ca2+ homeostasis. The observation of a positive effect of darodipine treatment on calbindin D-28K immunoreactivity in the cerebellar cortex suggests that manipulation of dihydropyridine-type Ca2+ channels may contribute to counter age-dependent changes of Ca2+ homeostasis.

Aging↗
PubMed1995

Location of sensory nerve cells that provide calbindin-containing laminar nerve endings in myenteric ganglia of the rat esophagus.

To determine the origin of the calbindin-containing laminar nerve endings in the myenteric ganglia of the rat esophagus, retrograde tracing experiments combined with immunohistochemistry using an antibody for calbindin were carried out. After Fast blue was injected into the cervical portion of the esophagus, labeled neurons were found bilaterally in the nodose ganglion and dorsal root ganglia of C1 to T3. 80% of the total neurons in the nodose ganglion and 20% of those in the dorsal root ganglia showed calbindin immunoreactivity. Moreover, 79% of Fast-blue-labeled neurons found in the nodose ganglion and 18% of those in the dorsal root ganglia were immunoreactive for calbindin. These results suggest that the calbindin antibody we used is useful as a marker for identifying esophageal vagal afferents derived from the nodose ganglion. The calbindin-immunoreactive nerve fibers forming the laminar endings in the myenteric ganglia of the rat cervical esophagus are mainly derived from sensory neurons in the nodose ganglion and partly derived from those in the cervical and upper thoracic dorsal root ganglia. Calbindin-containing laminar nerve endings may be related to mechanoreceptors in the esophagus.

Amidines↗
PubMed1988

Calbindin (CaBP 28 kDa) appearance and distribution during development of the mouse inner ear.

Previous reports of the distribution of calbindin, a 28 kDa vitamin D-induced calcium-binding protein, in the mammalian peripheral vestibular system postulated that this protein was involved in the calcium-dependent mechanisms occurring in the hair cells and ganglion cells. In this study, we examined the possibility of a relationship between the presence of calbindin and neurotransmission by comparing calbindin appearance in the inner ear to the sequence of synaptogenesis. Calbindin distribution was studied by immunocytochemistry, in the developing mouse inner ear from gestational day 12 to postnatal day 40. During the early development, calbindin was localized in non-neuronal structures: Kolliker's organ, spiral limbus and crista supporting cells; and in cochlear and vestibular ganglion neurons and sensory cells. At later stages and in the adult, no reactivity was observed in the non-neuronal cell populations and only certain sensory and nerve cells remained stained: inner hair cells, outer hair cells, vestibular hair cells of the apex of the cristae and of the striola in the maculae, all Corti's ganglion neurons and some vestibular ganglion neurons. The sequence of appearance of calbindin immunoreactivity in the sensory and nerve cells was not completely parallel to the maturation sequence of the inner ear, especially synaptogenesis. The dual distribution of calbindin during development and its expression in specific sensory and nerve cells opens new perspectives on its role in the inner ear.

Aging↗
PubMed1996

Calbindin localization in African giant rat kidney (Cricetomys gambianus).

Cricetomys gambianus are rodents living in savanna and follow area. They can live with restricted drinking water eating fresh food. Therefore their kidney may have some adaptive mechanisms for ion/water homeostasis compared to usual laboratory rats. In this study we have looked for calbindin, an intracellular calcium binding protein previously found in distal convoluted tubules from all mammalian species that have been studied and able to increase, in vitro, Ca2+ reabsorption. We have shown by using in situ hybridization, immunoblotting and immunohistochemistry that calbindin was expressed in three different portions of the distal nephron of the African giant rat. Calbindin was found in distal convoluted tubules, in cortical collecting tubules and in outer medullary collecting ducts. By contrast, in laboratory rat, calbindin was only found in distal convoluted tubules and undetectable in medullary collecting ducts. Thick ascending limb of Henle's loop were calbindin negative as shown by double immunolabelling using anti-uromucoid (Tamm-Horsfall protein). As previously shown in laboratory rat and rabbit, transcellular Ca2+ movement seems to be facilitated by calbindin in renal tubules segments predominantly actively transporting Ca2+, it may be suggested that in African giant rat, outer medullary collecting ducts may also actively transport Ca2+. As calretinin, another intracellular calcium binding protein highly homologous to calbindin but whose function is still conjectural has been suspected to be expressed in kidney, we have looked and not found any calretinin in both adult rat species.

Animals↗
PubMed1991

Vitamin D-independent expression of chick brain calbindin-D28K.

A combination of calbindin-D28K-specific cDNA probes and polyclonal antisera were used to investigate expression of the calbindin-D28K in the vitamin D-deficient avian brain in vivo in response to pharmacological doses of the vitamin D3 metabolite, 1,25-dihydroxyvitamin D3 (1,25(OH)2D3). Serum calcium levels were stimulated (2-fold) and intestinal calbindin-D28K expression (between 10- and 30-fold) by 1,25(OH)2D3 (6.5 nmol/animal) after 12 h. In marked contrast, steady-state whole brain levels of calbindin-D28K as judged by enzyme-linked immunoassay (ELISA) remained constant. Northern gel analysis revealed that three species of calbindin-D28K mRNA (2.0, 2.6 and 3.1 kb) were present a priori in the vitamin D-deficient chick brain and that administration of pharmacological doses (6.5 nmol/animal) of 1,25(OH)2D3 failed to influence their relative abundance. Separate but parallel dot blot hybridization analyses also confirmed that brain calbindin-D28K-mRNA levels were not influenced by 1,25(OH)2D3. These experiments demonstrate at the molecular level that, in contrast to the intestine, the gene encoding calbindin-D28K in the brain is regulated by mechanism(s) or factors which are independent of vitamin D status.

Animals↗
PubMed1989

Inducing effect of skeletal muscle extracts on the appearance of calbindin-immunoreactive dorsal root ganglion cells in culture.

Calbindin D-28k is a calcium-binding protein which is not expressed by dorsal root ganglion cells cultured from 6-day-old (E6) chick embryos. When soluble muscle extracts from embryos at E11, E18 or chickens 2 weeks after hatching were added immediately after seeding, dorsal root ganglia cells grown at E6 displayed neuronal subpopulations expressing calbindin immunoreactivity with time; the effect of muscle extract on the percentage of calbindin-immunoreactive dorsal root ganglia cells followed a dose-response curve. When muscle extract was added to cultures after a 3 day delay, the percentage of calbindin-expressing neurons was unchanged. The effect produced by muscle extract and, to a lesser degree, skin extract on the appearance of calbindin-positive neurons was not reproduced by brain or liver extracts while all four exerted a trophic action on cultured neurons. Hence it is assumed that muscle extract contains a factor which produces an inductive effect on the initiation of calbindin-expression by uncommitted subpopulations of sensory neurons rather than a trophic influence on the selective survival of covertly committed neuronal subpopulations. The fact that muscle extract promoted calbindin expression by dorsal root ganglia cells in neuron-enriched as well as in mixed dorsal root ganglion cell cultures indicates that the factor would act directly on sensory neurons rather than indirectly through mediation of non-neuronal cells. Since the active muscular factor was non-dialysable, heat-inactivated, trypsin-sensitive and retained by molecular filters with a cut-off of 30 K, this factor is probably a protein.

Animals↗
PubMed1992

Prenatal development of calbindin immunoreactivity in the dorsal thalamus of the rat.

The distribution of calbindin immunoreactivity was studied in the developing rat dorsal thalamus at embryonic days 14, 16, 18 and 20. At early stages (days 14-16), calbindin is expressed throughout the dorsal thalamic cell mass. Most intense labeling occurs in cells adjacent to the ventricular surface, in a spatial gradient reflecting the well-known outside-in generation pattern. Between days 16 and 20, calbindin-positive periventricular cells are redistributed in the dorsal thalamus according to two different patterns. They first become oriented tangentially within the periventricular layer, and diminish in number at the central locus where midline thalamic fusion occurs at 18 days. Periventricular calbindin immunoreactivity becomes restricted to a ring of late-born cells surrounding the gray commissure. Recognizable portions of this ring-shaped primordium will mature forming n.paratenialis, n.reuniens, n.paraventricularis, and n.subparafascicularis magnocellularis. Simultaneously, a massive contingent of radially-oriented, fusiform, calbindin-positive young neurons extends from the periventricular ring-shaped aggregate to the lateral brain surface at the caudoventral pole of the dorsal thalamus at embryonic days 17/18. These cells surround the primordium of the medial geniculate body, participating in the constitution of its marginal zone, and invade the lateral posterior nucleus, accumulating within its caudomedial part. Other portions of this stream form the parvocellular subparafascicular nucleus and the peripeduncular nucleus. The observed patterns of calbindin expression suggest that dorsal thalamic postmitotic neurons transiently express the marker during initial phases of axogenesis, whereas a specific, late-born population expresses calbindin continuously into adulthood. This late subpopulation displays migratory behavior, and finally subdivides into several nuclei of the mature midline, superficial and posterior thalamus.

Animals↗
PubMed1992

Presence of calbindin and lack of parvalbumin in progesterone receptor-containing neurons of the monkey mediobasal hypothalamus.

All of the progesterone receptor-containing cells of the monkey hypothalamus are GABAergic. The aim of this study was to further characterize these GABAergic progesterone receptor-containing neurons based on their calbindin or parvalbumin content. These calcium-binding proteins are characteristic markers of different populations of GABAergic neurons in the central nervous system. Double-immunolabeling for progesterone receptor and either calbindin or parvalbumin was performed on hypothalamic Vibratome sections of estrogen primed African green monkeys (Cercopithecus aethiops). Progesterone receptor-containing calbindin-immunoreactive neurons were observed in the ventromedial and periventricular areas of the hypothalamus. Forty-one per cent of the progesterone receptor-containing cells in this area were calbindin immunopositive. No double-immunolabeled neurons could be detected in the infundibular (arcuate) nucleus. In tissue double-immunolabeled for progesterone receptor and parvalbumin, none of the progesterone receptor-containing neurons exhibited immunoreactivity for parvalbumin. Electron microscopic double-immunostaining for progesterone receptor and calbindin confirmed the light microscopic results. Furthermore, a large number of asymmetric synaptic contacts were observed on the calbindin-immunoreactive neurons. These observations demonstrate that progesterone receptor-containing cells in the monkey mediobasal hypothalamus consist of at least two different types of GABA neurons, and indicate that progesterone receptor-containing calbindin cells may be postsynaptic targets of excitatory fibers.

Animals↗
PubMed2006

Parvalbumin and calbindin D-28k immunoreactivity in transgenic mice with a G93A mutant SOD1 gene.

Immunohistochemical study was performed to examine if calcium-binding proteins are involved in the degeneration of motor neurons in the brain stems and the spinal cords of transgenic mice carrying a G93A mutant human SOD1 gene. Specimens from age-matched non-transgenic wild-type mice served as controls. In the spinal cord of the controls, the density of parvalbumin-immunoreactive neurons was highest in the large anterior horn neurons and lower in the posterior horn neurons in the spinal cord. On the other hand, calbindin D-28k immunoreactivity was much less apparent than that observed with parvalbumin antisera. Rexed's lamina II was densely immunostained for calbindin D-28k, whereas, in the anterior horn, calbindin-D-28k-positive small neurons were barely dispersed in a scattered pattern. In transgenic mice, parvalbumin-positive anterior horn neurons were severely reduced, even at the presymptomatic stage, whereas calbindin-positive neurons were largely preserved. At the symptomatic stage, both parvalbumin and calbindin D-28k immunoreactivity markedly diminished or disappeared in the anterior horn. Immunoblotting analysis revealed a significant reduction of immunoreactivity to parvalbumin antibody in transgenic mice compared with the controls. In the brain stem, parvalbumin-positive oculomotor and abducens neurons and the calbindin D-28k-positive sixth nucleus were well-preserved in transgenic mice as well as in the controls. Thus, the diffuse and severe loss of parvalbumin immunoreactivity of large motor neurons even at early stages in SOD1-transgenic mice and the absence of calbindin D-28k immunoreactivity of normal large motor neurons suggest that these calcium-binding proteins may contribute to selective vulnerability and an early loss of function of large motor neurons in this SOD1-transgenic mouse model.

Abducens Nerve↗
PubMed2002

Cytoprotective effects of calbindin-D(28k) against antimycin-A induced hypoxic injury in proximal tubular cells.

Intracellular calcium plays an important role on the pathogenesis of hypoxia-induced cellular injury. Calbindin-D(28k), a cytosolic vitamin D-dependent calcium binding protein, can serve as a buffer to limit a surge in intracellular Ca2+ concentration ([Ca2+]i) induced by various stimulations. To evaluate the possible cytoprotective effect of calbindin-D(28k) against hypoxic injury in proximal tubular cells, a plasmid containing calbindin-D(28k) cDNA under the control of CMV immediate-early gene promoter was transfected into the murine proximal tubular epithelial (MCT) cells. The expression of calbindin-D(28k) in the transfected cells was verified with Northern blot analysis, Western blot analysis, and immunofluorescent staining. The non-transfected and transfected MCT cells were subjected to chemical hypoxia induced by antimycin A (10 microM) and glucose deprivation for 30-120 min. The transfection of calbindin-D(28k) reduced lactate dehydrogenase (LDH) release by 41%, 41%, 24%, and 24%, respectively, at 30, 60, 90 and 120 min after hypoxia when compared to the non-transfected cells (all p < 0.05). Cell viability after hypoxic injury was also significantly higher in transfected cells than non-transfected cells. Transfection with the plasmid without calbindin-D(28k) cDNA did not affect LDH release or cell viability after chemical hypoxic injury. [Ca+2]i was measured ratiometrically with fura-2 after exposure to chemical hypoxia. The rate of initial rise in [Ca2+]i and final [Ca+2]i at 30-120 min were significantly lowered in transfected cells. In conclusion, this study demonstrated that transfection of calbindin-D(28k) gene into MCT cells provide protective effects against chemical hypoxic injury probably through its buffering effects on [Ca+2]i.

Animals↗
PubMed2002

Calbindin-D(28K) cells selectively contact intra-SCN neurons.

Calbindin-D(28K)-immunoreactive cells are tightly packed within a discrete region of the caudal aspect of the suprachiasmatic nuclei of hamsters. These cells receive direct retinal input and are Fos-positive in response to a light pulse. Knowledge of their afferent and efferent connections is necessary to understand suprachiasmatic nucleus organization. The first aim of the present study is to identify interconnections between calbindin and other peptidergic cells of the suprachiasmatic nuclei, using epi- and confocal microscopy and intra-suprachiasmatic nucleus tract tracing. The results indicate that essentially all calbindin cells receive numerous appositions from vasoactive intestinal polypeptide (VIP), neuropeptide Y and serotonin fibers and that most receive appositions from gastrin releasing peptide (GRP) and cholecystokinin (CCK) fibers. Reciprocal connections are seen from VIP, GRP and CCK cells but surprisingly, not from dorsomedial vasopressin cells. Injection of biotinylated dextran amine into the suprachiasmatic nucleus indicates that the ventrolateral suprachiasmatic nucleus projects to the entire nucleus, while the dorsal and medial regions of the suprachiasmatic nucleus project densely to most of the nucleus, except to the calbindin region. Analysis of colocalization of the peptides in the calbindin cell region shows that 91% of the substance P cells, 42% of the GRP cells and 60% of the VIP cells in the calbindin subnucleus coexpress calbindin-D(28K). Our results reveal a highly specialized topographical organization of connections among suprachiasmatic nucleus cells.

Animals↗
PubMed2002

Activity-dependent expression of calbindin in rabbit floccular Purkinje cells modulated by optokinetic stimulation.

Optokinetic stimulation activates visual climbing fiber pathways that synapse upon contralateral floccular Purkinje cells. Long-term horizontal optokinetic stimulation causes a progressive decrease in gain of the optokinetic reflex and leads to the subsequent genesis of a prolonged negative optokinetic afternystagmus. Since the flocculus is involved in adaptation to optokinetic stimulation, we used the technique of differential display reverse transcription-polymerase chain reaction to explore transcriptional changes in the flocculus evoked by long-term optokinetically evoked climbing fiber discharge. Several differentially transcribed gene products were isolated and sequenced. One of these, calbindin mRNA, was expressed in relatively decreased abundance in the flocculus that received increased climbing fiber input. Decreased transcription of calbindin mRNA was confirmed by northern blots. Hybridization histochemistry was used to localize calbindin mRNA to Purkinje cells and confirmed decreased transcription of calbindin mRNA in Purkinje cells located in folium 1 of the flocculus. Western blots and immunohistochemistry localized the climbing fiber-evoked decreased expression of calbindin to Purkinje cells in folia 1 of the flocculus. The expression of four other calcium-binding proteins in the flocculus was not influenced by optokinetic stimulation. Changes in expression of calbindin could be evoked by decreases in intracellular calcium associated with climbing fiber-evoked decreases in Purkinje cell simple spike activity.The application of differential display reverse transcription-polymerase chain reaction has provided a positive screen for several molecules in addition to calbindin whose expression is affected by naturally evoked activity in a major synaptic pathway to the cerebellum. Further experiments will be required to specify the functional role of each of these molecules.

Animals↗
PubMedDate not supplied

Neurochemical compartmentation of monkey and human visual cortex: similarities and variations in calbindin immunoreactivity across species.

The compartmental organization of visual cortical neurons was examined across species of primates by directly comparing the pattern of immunoreactivity for the 28-kD vitamin D-dependent calcium-binding protein (calbindin) in area 17 of squirrel monkeys, macaques, and neurologically normal adult humans. Area 17 of macaques and squirrel monkeys was similar in that somata and processes intensely immunoreactive for calbindin were present in the same layers (II-III, IVB, and V) and in both species formed a well-stained matrix that surrounded the CO-rich puffs in layer III. These intensely calbindin-immunoreactive neurons were identified as subpopulations of GABA-immunoreactive neurons. Among the most obvious differences in the two monkey species was the distribution of calbindin-positive elements outside of layer III: a dense immunostained matrix surrounded the puffs in layers II, IVB, V, and VI of squirrel monkeys but the immunostained neurons adopted no regular pattern outside layer III in macaques. In addition, although somata lightly immunoreactive for calbindin were present in both species, they were much more abundant in squirrel monkeys than macaques. The pattern of calbindin immunostaining in human area 17 resembled that of macaques in forming an intense matrix that surrounded puffs only in layer III, yet also resembled that of squirrel monkeys by including large numbers of light immunoreactive somata. These lightly immunostained somata included a very dense population forming a prominent band in layer IVA of human visual cortex. We conclude that for layer III of primary visual cortex, a similar pattern of neuronal chemistry exists across species of primates which is related to this layer's compartmental organization. Yet for other layers, the expression of calbindin immunoreactivity varies from one species to the next, perhaps reflecting variations in other neuronal properties.

Aged↗
PubMed2000

Ca(2+)- and H(+)-dependent conformational changes of calbindin D(28k).

Calbindin D(28k) is a member of a large family of intracellular Ca(2+) binding proteins characterized by EF-hand structural motifs. Some of these proteins are classified as Ca(2+)-sensor proteins, since they are involved in transducing intracellular Ca(2+) signals by exposing a hydrophobic patch on the protein surface in response to Ca(2+) binding. The hydrophobic patch serves as an interaction site for target enzymes. Other members of this group are classified as Ca(2+)-buffering proteins, because they remain closed after Ca(2+) binding and participate in Ca(2+) buffering and transport functions. ANS (8-anilinonaphthalene-1-sulfonic acid) binding and affinity chromatography on a hydrophobic column suggested that both the Ca(2+)-free and Ca(2+)-loaded form of calbindin D(28k) have exposed hydrophobic surfaces. Since exposure of hydrophobic surface is unfavorable in the aqueous intracellular milieu, calbindin D(28k) most likely interacts with other cellular components in vivo. A Ca(2+)-induced conformational change was readily detected by several optical spectroscopic methods. Thus, calbindin D(28k) shares some of the properties of Ca(2+)-sensor proteins. However, the Ca(2+)-induced change in exposed hydrophobic surface was considerably less pronounced than that in calmodulin. The data also shows that calbindin D(28k) undergoes a rapid and reversible conformational change in response to a H(+) concentration increase within the physiological pH range. The pH-dependent conformational change was shown to reside mainly in EF-hands 1-3. Urea-induced unfolding of the protein at pH 6, 7, and 8 showed that the stability of calbindin D(28k) was increased in response to H(+) in the range examined. The results suggest that calbindin D(28k) may interact with targets in a Ca(2+)- and H(+)-dependent manner.

Anilino Naphthalenesulfonates↗
PubMed2001

Locally reduced levels of acidic FGF lead to decreased expression of 28-kda calbindin and contribute to the selective vulnerability of the neurons in the entorhinal cortex in Alzheimer's disease.

Recent studies demonstrate that a disturbed calcium-homeostasis leading to increased susceptibility to excitotoxic triggers plays a major role in the neurodegenerative process initiating in layer 2 of the entorhinal cortex (EC2) during Alzheimer's disease (AD). Thus, proteins binding free Ca++ (i.e. calbindin) and factors regulating these proteins are of great importance for the neuroprotective-neurotoxic balance in the affected brain regions. In the present combined human and in vitro study evidence is provided that altered levels of the acidic fibroblast growth factor (aFGF) and calbindin expression are concomitantly present in EC2 neurons and have interactive effects. A dramatic loss of aFGF- and calbindin-labeled EC2 neurons was found. Further analysis of the surviving EC2 neurons revealed a strong immunoreactivity to calbindin and aFGF. In vitro experiments show that aFGF regulates calbindin expression, because treatment of differentiating neurons with recombinant aFGF increases calbindin expression in a time-dependent fashion. The data imply that a reduced expression of aFGF in EC2 neurons of AD brains leads to lower levels of calbindin resulting in decreased neuroprotective capacity.

Aged↗