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PubMed1994

Subterranean mole-rats naturally have an impoverished calciol status, yet synthesize calciol metabolites and calbindins.

Mole-rats (Family Bathyergidae) have no obvious source of calciol. They live in an environment devoid of sunlight and consume a herbivorous diet. Calciol status, metabolism and expression were examined in six species of Bathyergids. Serum levels of calcidiol in all species were < 5 micrograms/l and those of calcitriol were low (18.0 +/- 11.0 (SD) ng/l, N = 57) when compared to other rodents. Within 72 h of injecting animals with tritium-labelled calciol, most of the labelled prohormone had been metabolized to more polar metabolites. Three times more tritium-labelled calcitriol (19.3 +/- 2.9%) was present than (24R)-hydroxycalcidiol (6.2 +/- 10%). The natural absence of detectable circulating concentrations of calcidiol and the threefold greater amount of calcitriol to (24R)-hydroxycalcidiol produced indicate that calciol naturally is in short supply. Calciol-dependent calbindins were absent in the duodenum. Calbindin-D28k was present in the Purkinje cells of the cerebellum and in some collecting ducts and proximal and distal convoluted tubules of the kidney. Calbindin-D9k also was present but was localized uniquely in the juxtaglomerular cells of the five southern African species. These data confirm that Bathyergid mole-rats naturally have an impoverished calciol status. Despite the presence of calbindins in renal tissues, the functional importance of this hormone in calbindin synthesis and other normal mole-rat physiology is not known.

Animals↗
PubMed1999

Alteration in the expression level of calbindin D28k in the periodontal ligament of the rat molar during experimental tooth movement.

The present immunohistochemical study was designed to investigate changes in the distribution and expression level of calbindin D28k in the periodontal ligament during experimental tooth movement in the rat molar to clarify the physiological role of this protein in the ligament. In normal animals, calbindin D28k-like immunoreactivity appeared sparsely in spindle-shaped cells in the alveolar half of the periodontal ligament. Electron microscopic observations showed that these immunoreactive cells were characterized by well-developed rough-surfaced endoplasmic reticulum and phagosomes--which often contained collagen fibers--suggesting that these cells could be categorized as periodontal fibroblasts. Twelve hours following the onset of the experimental tooth movement, cells positive for calbindin D28k increased in number in the periodontal ligament, especially in the alveolar half of the pressured side. Immunoelectron microscopy showed that the calbindin D28k-immunopositive cells had morphological features similar to those of fibroblasts in the normal ligament, and that these cells occasionally made contact with immunonegative macrophage-like cells. Immunopositive cells gradually decreased in number, and the distribution of the cells and intensity of the immunoreactivity returned to normal levels by 14 days following the induction of the experimental tooth movement. The present results suggest that calbindin D28k plays an important role in the homeostasis and cyto-protection of fibroblasts in the periodontal ligament at the initial phase of experimental tooth movement.

Animals↗
PubMed2003

Developmental pattern of calbindin D28k protein expression in the rat striatum and cerebral cortex.

We examined the protein expression of the calcium-binding protein calbindin D28k in two developing rat brain structures, the striatum and the cerebral cortex. The relative protein concentration level was quantified by means of the Western blotting method and densitometric scanning. 32 Wistar rats were used, divided according to survival period (P0-P120-postnatal days). Observations of the calbindin D28k protein expression in the rat striatum and the cerebral cortex revealed an increase in band color intensity between P0 and P10. The intensity of protein staining in older groups of animals stabilised at a similar level and in the P28 and P120 groups we observed a decrement of calbindin expression in the striatum. Calbindin D28k stabilises the intracellular calcium level, preventing calcium-induced apoptotic cell death in neurons. Thus, changes in calbindin D28k expression might be related to its neuroprotective role in differentiation and synaptogenesis during the postnatal development of the brain.

Animals↗
PubMed2005

Alterations in the localization of calbindin D28K-, calretinin-, and parvalbumin-immunoreactive neurons of rabbit retinal ganglion cell layer from ischemia and reperfusion.

Calcium-binding proteins are thought to play important roles in calcium buffering. The present study investigated the effects of ischemia and reperfusion on calbindin D28K, calretinin, and parvalbumin immunoreactivity in the ganglion cell layer of the rabbit. Rabbits were administered ischemic damage by increasing the intraocular pressure. After 60 and 90 min of ischemia, reperfusion (7 d) was allowed to occur. The b-wave of the electroretinogram (ERG) was reduced by more than 50% and almost 80% in retina given ischemia for 60 and 90 min, respectively. The oscillatory potential (OPs) wave was reduced approximately 50% at 60 min ischemia and 70% at 90 min ischemia. In both normal and ischemic-treated retina, calcium-binding protein immunoreactivity was seen in many cells in the ganglion cell layer. In eyes subjected to 60 min ischemia, there was a decrease of the density of calbindin D28K- (8.29%), calretinin- (14.44%), and parvalbumin- (26.83%) immunoreactive (IR) cells compared to the control retina. In eyes subjected to 90 min ischemia, there was a higher decrease of the density of calbindin D28K- (18.48%), calretinin- (33.59%), and parvalbumin- (54.26%) IR cells than at 60 min. Some calcium-binding protein-IR neurons, especially calretinin-IR neurons, showed aggregations that were abnormally packed together in retina subjected to ischemia for 90 min. The results show that calbindin D28K-, calretinin-, and parvalbumin-IR cells in the ganglion cell layer are susceptible to ischemic damage and reperfusion. The degree of reduction varied among different calcium-binding proteins and ischemic damage times. These results suggest that calbindin D28K-containing neurons are less susceptible to ischemic damage than calretinin- and parvalbumin-containing neurons in the ganglion cell layer of rabbit retina.

Animals↗
PubMed1988

Calbindin-D28K and the peptidergic neuroendocrine system in rat gut: an immunohistochemical study.

Calbindin-D28K was immunohistochemically localized in myenteric and submucosal plexuses throughout the rat intestine. Calbindin-D28K immunoreactivity was found in about half of myenteric neurons and in more than 90% of submucosal neurons. Calbindin-D28K was also observed in nerve processes running inside ganglia, muscle layers and lamina propria. No correlation could be established between the presence of calbindin-D28K and the distribution of neuropeptides localized in this study (VIP, enkephalin, somatostatin and substance P). In addition, some endocrine-like cells of the ileum were calbindin-D28K-positive. Half of these endocrine cells also contained neurotensin but none of the other neuropeptides investigated.

Animals↗
PubMed1994

Effects of magnesium on renal and intestinal calbindin-D.

The possible effects of magnesium on the vitamin D-dependent renal and intestinal calbindin-D were investigated. In a low magnesium model 70 Wistar rats were allocated to either a normomagnesemic diet (Mg 3.2 g/kg) or a Mg-deficient diet (Mg 0.18 g/kg) for 10 or 24 days. The rats had intraperitoneal injections of 1,25-(OH)2 vitamin D3 0.2 microgram, MgSO4 100 mumol or placebo daily for the last 4 days. In a high magnesium model 60 Wistar rats were allocated to three groups on a normomagnesemic diet supplied with intraperitoneal MgSO4 20 mumol, 100 mumol or placebo daily. Half of the animals in each group were further supplied with intraperitoneal 1,25-(OH)2 vitamin D3 0.2 micrograms daily. The concentrations of intestinal calbindin-D9k increased on the low Mg diet from 1.6 (1.1-2.0) to 2.7 (2.0-2.9) micrograms/mg protein (p < 0.02), but were unchanged in the high Mg groups. Vitamin D treatment raised the levels of calbindin-D9k in the normomagnesemic group (p < 0.01), but not significantly in the low Mg group. Administration of MgSO4 to the low Mg rats normalized the elevated levels of intestinal calbindin-D9k (p < 0.05). The concentrations of renal calbindin-D28k were not changed by the low Mg diet, but were lower in the high Mg group [0.8 (0.6-1.1) micrograms/mg protein] than in the control group [1.5 (1.1-1.8) micrograms/mg protein; p < 0.05]. Animals in the low, high and normal magnesium group showed no differences in plasma concentrations of 1,25-(OH)2 vitamin D.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1998

Cytological compartmentalization in the staggerer cerebellum, as revealed by calbindin immunohistochemistry for Purkinje cells.

The staggerer mouse carries a deletion in a gene encoding the nuclear hormone receptor RORalpha, which leads to severe impairments in phenotypic differentiation of cerebellar Purkinje cells. We previously found parasagittal compartments in the mature staggerer cerebellum, as defined by different transcription levels of Purkinje cell-specific molecules including calbindin. In the present study, we developed a hightiter anti-calbindin antibody to examine morphological features of the staggerer Purkinje cells. Immunohistochemistry for calbindin revealed compartmentalized Purkinje cell populations with different cell sizes, alignments, cell densities, and dendritic arborization, as well as different immunoreactivities, corresponding to the "transcriptional" compartments. Based on these immunohistochemical and cytological characteristics, the rostral cerebellum was clearly subdivided into three to seven parasagittal zones (Zones I-VII). Purkinje cells in Zones I and III were associated with the strongest calbindin immunoreactivities and exhibited morphological features reminiscent of the wild-type cells, i.e., large flask-shaped cell bodies, monolayer alignment, and arborized dendrites. Purkinje cells in Zone V were also labeled strongly, but they were small in cell size, ectopic and possessed long unbranched dendrites. On the other hand, Purkinje cells in Zones II, IV, and VI were very low in calbindin immunoreactivity and marked by small cell size, ectopia, poorly-developed dendrites and low cell density. Considering that this unique cytological compartmentalization emerges as the result of RORalpha gene mutation, it is suggested that normal cytodifferentiation of Purkinje cells is governed by both RORalpha-dependent and -independent mechanisms, and further that the latter mechanism might exert unevenly along the mediolateral cerebellar axis.

Animals↗
PubMed1992

Differential calbindin-like immunoreactivity in the brain stem auditory system of the chinchilla.

Calbindin is a 28 kD calcium-binding protein found in neural tissue. Although its functional role in neurons is unknown, it has been proposed that calbindin is involved in intracellular buffering and could therefore influence temporal precision of neuronal firing. In the barn owl, calbindin-like immunoreactivity was found to be selectively present in brain stem auditory pathways used to process interaural time differences, but was absent from the interaural intensity pathway. The present study demonstrates calbindin immunoreactivity in the auditory brain stem of the chinchilla, a rodent with exceptionally good low-frequency hearing. In the superior olivary complex and periolivary areas, immunoreactivity was divided between neuropil labeling in the lateral and medial superior olives and dorsomedial periolivary nucleus, and labeling of the somata of the medial and ventral nuclei of the trapezoid body and anterolateral periolivary nucleus. Strong immunoreactivity was observed in the ventral and dorsal divisions of the ventral nucleus of lateral lemniscus somata and the ventral division's columnarly organized fiber plexus. The dorsal nucleus of the lateral lemniscus was void of immunoreactivity. Virtually all principal neurons of the sagulum showed darkly labeled somata surrounded by a densely labeled fiber plexus. Immunoreactivity in the inferior colliculus was primarily limited to the paracentral nuclei, with only an occasional labeled cell in the central nucleus. In conclusion, although selective labeling of calbindin in the mammalian auditory brain stem is impressive, no distinctive labeling of a functionally defined timing pathway was apparent as reported previously in the barn owl or electric fish.

Animals↗
PubMed1999

Large-scale HPLC purification of calbindin D9k from porcine intestine.

Two efficient procedures for large-scale purification of calbindin D9k from porcine intestine by HPLC were developed. Both protocols start with heat treatment of the intestinal tissue followed by acetic acid extraction, a capture with alginic acid, NaCl precipitation of other proteins, and a concentration step on Amberlite XAD-2. In the first method, a single reverse-phase HPLC step completes the purification and results in milligram quantities of pure calbindin. In the second method, an additional ion exchange HPLC step was introduced, followed by a reverse-phase HPLC resulting in 100 milligram-scale preparations of homogeneous calbindin in a 56% yield from the Amberlite step. Both methods yielded a homogeneous metal-free apoprotein with a molecular weight of 8838.0 +/- 8.8 as analyzed by MALDI TOF mass spectrometry corresponding to N-acetylated porcine calbindin. The isolated apocalbindin was fully reconstituted with 2 molar equivalents of Ca(2+) and the protein displayed UV and fluorescence spectra characteristic of those of native calbindin D9k.

Animals↗
PubMed1994

Poor correlation between delayed neuronal death induced by transient forebrain ischemia, and immunoreactivity for parvalbumin and calbindin D-28k in developing gerbil hippocampus.

In the normal developing hippocampus of the gerbil, parvalbumin-immunoreactive neurons first appear in the stratum pyramidale of CA3 at postnatal day 15 (P15), and in CA2 and hilus of the dentate gyrus from P21 onwards. Immunoreactive terminals also follow the same sequence from CA3 to CA1 to reach adult patterns by the end of the 1st month. Calbindin D-28k immunoreactivity is seen in the external part of the upper blade of the dentate gyrus at P5, and progresses to the granule cell and molecular layers of the whole gyrus by P15, except for a thin band of immature cells located at the base of the granule cell layer which are calbindin negative. Calbindin immunoreactivity in mossy fibers progresses from the external to the hilar region of CA3 during the same period. A few immunoreactive cells are also found in the stratum radiatum/lacunare of the CA3, but no calbindin-immunoreactive cells are observed in the CA1 and CA2 subfields. The adult pattern of calbindin immunoreactivity is reached at P21. Vulnerability following transient forebrain ischemia for 20 min was examined in the hippocampal formation of gerbils during postnatal development. No cellular damage was seen in animals aged 7 days. Dying cells were observed at the base of the granule cell layer of the dentate gyrus in animals aged 15, 21 and 30 days. Pyramidal cells in the CA3 subfield were also sensitive to ischemia in gerbils aged 15 days, and less frequently in animals aged 21 days. The adult pattern of cellular damage, characterized by selective vulnerability of the CA1 subfield, was seen from day 30 onwards.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Immunohistochemical demonstration of calbindin-containing nerve endings in the rat esophagus.

Immunoreactivity for calbindin was found in nerve endings with irregular laminar shapes in the rat esophagus. In the myenteric ganglia, laminar endings of a range of sizes formed a complex network and appeared to lie at the surface of the ganglion. The myenteric ganglia that contained nerve endings were most abundant in the upper portion of the esophagus, their number decreasing orally to anally. Calbindin-immunoreactive nerve cell bodies were scattered throughout the esophagus. Laminar terminals were found in the connective tissue of the lamina propria immediately beneath the epithelium and in the muscularis mucosae. Occasional nerve branches formed a network of aborizing endings that surrounded part of the submucosal arterioles. Immunoreactive nerve endings in the mucosa and submucosa were present only in the upper part of the cervical esophagus. Unilateral vagotomy caused a remarkable decrease in the number of the myenteric ganglia containing the calbindin-immunoreactive laminar endings after 15 days or survival; in some of ganglia, the laminar structures disappeared and nerve endings showing weak immunoreactivity had an indistinct appearance, so that the outline of the ganglia became obscure. In operated rats at 24 days, the number of innervated ganglia was about half that in normal rats. However, there was no change in the morphology and the occurrence of the immunoreactive laminar structures in the mucosa and submucosa after denervation. The results show that many of the laminar endings that are immunoreactive for calbindin in the myenteric ganglia are derived from the vagus nerve. Thus, the calbindin-immunoreactive nerve endings with laminar expansions that are found in the rat esophageal wall could be sensory receptors.

Animals↗
PubMed1992

Distribution of calbindin and parvalbumin in the developing somatosensory cortex and its primordium in the rat: an immunocytochemical study.

Immunocytochemical techniques were used to analyze the distribution of the calcium-binding proteins calbindin and parvalbumin during the pre- and postnatal development of the rat somatosensory cortex. Calbindin occurs in most early differentiated neurons that form the primordial plexiform layer at embryonic day 14. This expression in transient; during the perinatal period, calbindin becomes immunologically undetectable within the structures derived from the primordial plexiform layer, i.e., the prospective layers I and VIb. Immunoreactive neurons are also absent from adult layers I and VIb. Calbindin is also detected in a second population of neurons which, from embryonic day 18 onwards, distributes diffusely within the cortical plate. Some neurons of this population show morphological traits of immaturity, while others show complete dendritic arborization. The definitive pattern of distribution of calbindin-immunoreactive neurons is achieved by postnatal day 22. Infragranular layers contain intensely-immunoreactive cells whose numerical density decreases during postnatal development, whereas in supragranular layers similar neurons are interspersed among numerous faintly-stained neurons. Parvalbumin is detected for the first time at postnatal day 6, within a small group of neurons located in cortical layer V, and extends afterwards through the whole thickness of the cerebral cortex. At this same postnatal stage, groups of immunoreactive puncta are also found in layer IV of the somatosensory cortex; these puncta increase in density progressively and, at embryonic day 13, immunoreactive cells appear also grouped at this level. At this postnatal age, parvalbumin immunostaining delineates the somatosensory map in cortical layer IV. From this stage to adulthood, the number of immunoreactive neurons increases in the whole thickness of the somatosensory cortex. Barrels in layer IV become less distinct as immunoreactive cells and processes invade the septa. Layer IV in the adult somatosensory cortex appears more densely populated by parvalbumin immunoreactive neurons and puncta than in the surrounding areas.

Aging↗
PubMed1997

Parvalbumin-containing cells of the angular portion of the vertical limb terminate on calbindin-immunoreactive neurons located at the border between the lateral and medial septum of the rat.

In the septal complex, both parvalbumin and calbindin neurons cocontain GABA. In the same area, a large number of GABA-GABA synaptic connections can be observed. In order to further characterize their neurochemical nature, as well as the extrinsic and/or intrinsic origin of these GABA terminals, the following experiments were performed: (1) correlated light- and electron-microscopic double immunostaining for calbindin and parvalbumin on septal sections of control rats: (2) light microscopic parvalbumin immunostaining of septal sections after surgical isolation (5 days) of the septum from its telencephalic or (3) hypothalamic afferents; and (4) parvalbumin immunostaining of sections prepared from the entire brain 2 days following horseradish peroxidase injection into the border between the lateral and medial septum. The results demonstrated that: (1) in a well-circumscribed, vertically longitudinal area located between the lateral and medial septum, 0.1-0.6 mm anterior to the bregma, a group of calbindin-containing, nonsomatospiny neurons are surrounded by parvalbumin-immunoreactive baskets; (2) these basket-forming axon terminals establish symmetric synaptic contacts with their targets; and (3) their cells of origin are not in the medial septum, but in the angular portion of the vertical limb. These observations indicate that a portion of the septal complex GABA-GABA synaptic connections represent functional interaction between two different types of GABAergic neurons. The presynaptic GABAergic neurons contain parvalbumin, and the postsynaptic GABAergic cells are immunoreactive for calbindin. Furthermore, a population of the medial septum/diagonal band parvalbumin neurons project only to the hippocampus, while others, which may also send axons to the hippocampus, terminate on lateral septum calbindin cells as well.

Animals↗
PubMed1998

Significant elevation of urinary 28-kD calbindin-D and N-acetyl-beta-D-glucosaminidase levels in patients undergoing extracorporeal shock wave lithotripsy.

Calbindin-D, a vitamin D-dependent calcium binding protein with a molecular mass of 28 kD, is found predominantly in distal renal tubules and central nervous system tissues in man. We have developed a highly sensitive enzyme immunoassay for human 28-kD calbindin-D and demonstrated its advantages as a new marker for damage to distal renal tubules. Urinary N-acetyl-beta-D-glucosaminidase (NAG), a lysosomal enzyme of the proximal renal tubules, is another segment-specific indicator of renal damage. To clarify whether both proximal and distal renal tubules are similarly affected by extracorporeal shock wave lithotripsy (SWL) treatment, urinary 28-kD calbindin-D and NAG were measured before, then immediately, 2 and 24 hours after SWL in 17 renal lithiasis patients. Levels of urinary calbindin-D were markedly elevated immediately and 2 hours after SWL and then decreased. In sera, levels of calbindin-D also increased, closely correlated with the changes in urinary values. Levels of urinary NAG were also significantly elevated immediately after SWL and then decreased. The results indicate that damage to both proximal and distal renal tubules occurs simultaneously with SWL and that the two markers can be applied as sensitive indicators of such side effects and their alleviation with protective agents.

Acetylglucosaminidase↗
PubMed2001

Distribution of the calcium-binding proteins calbindin D-28K and parvalbumin in the superior colliculus of adult and neonatal cat and rhesus monkey.

The distribution of the calcium-binding proteins calbindin D-28K and parvalbumin was examined in newborn and adult superior colliculus of cat and rhesus monkey using immunohistochemical techniques. In adult animals of both species, calbindin-immunoreactive neurons had a three-tiered arrangement: one band was present in the upper aspects of the superficial laminae, a second in the intermediate laminae, and a third in the deep laminae. The intermediate tier was less obvious in the monkey, whereas the deep tier was less pronounced in the cat. Parvalbumin-immunoreactive neurons had a complementary distribution to calbindin-immunoreactive neurons within these laminae in both species, although the segregation of calbindin immunoreactivity and parvalbumin immunoreactivity in the superficial laminae was not as precise in the monkey as it was in the cat. At birth, calbindin immunoreactivity in the newborns of both species was remarkably mature, with its three-tiered distribution clearly evident. By contrast, parvalbumin immunoreactivity was distinctly different in the newborn cat than in the newborn monkey: whereas parvalbumin immunoreactivity in the newborn monkey was already very similar to its adult-like pattern, the pattern in the newborn cat was quite immature. The superficial laminae of the newborn cat were virtually devoid of parvalbumin immunoreactivity, and, although the intermediate laminae displayed robust parvalbumin-immunoreactive neuropil, comparatively fewer parvalbumin-immunoreactive neurons were observed. Conspicuously few in number were the large multipolar neurons in the intermediate laminae, which give rise to the descending efferents to the brainstem. However, parvalbumin-immunoreactive neurons were present within the deep laminae, suggesting a ventral-to-dorsal maturational gradient in parvalbumin expression that parallels the ventral-to-dorsal gradient of neurogenesis. The differences in parvalbumin immunoreactivity observed between these two species at parturition are consistent with the advanced visual and visuomotor capabilities of the newborn monkey and the absence of visually related behaviors in the newborn cat.

Animals↗
PubMed1996

Calcium transport and the localisation of calbindin-D9k in the ruminant placenta during the second half of pregnancy.

In late pregnancy the sheep fetus requires 3 g of calcium per day, all of which must be transported across the trophoblast epithelium of the placenta. Such high levels of calcium transport across other epithelia are normally associated with the presence of calbindin-D9 or -28k. Our immunocytochemical results show that ovine, bovine and caprine interplacentomal trophoblast have high levels of calbindin-D9k, about eight to ten times more than in the placentomal region. The protein is detectable only in the uninucleate trophoblast cells in sheep and goat, the frequent binucleate cells show none. The calbindin-D9k is also present in the maternal glandular epithelium but not the surface epithelium of the uterus. The cellular distribution of the calbindin-D9k immunoreactivity suggests a soluble protein homogenously distributed through cytosol and nucleoplasm but absent from all organelles and intercellular spaces. In contrast, the uterine milk protein(s) are localised in Golgi cisternae and secretory vesicles in gland cells and in apical small endocytic vesicles and lysosomes in the uninucleate trophectodermal cells. The distribution of calbindin-D9k supports the concept that it mediates the high calcium flux by facilitated diffusion and not via any vesicular, membrane-bounded system.

Animals↗
PubMed1991

Acute actions of 1,25-dihydroxyvitamin D3 upon chick pancreatic calbindin-D28K.

We have compared the relative responsiveness of pancreatic, intestinal and renal tissue calbindin-D28K protein content to the stimulatory actions of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] in vitamin D-deficient (-D) chicks. Tissue concentrations of calbindin-D28K were undetectable in the -D chick intestine but present, albeit at low concentrations (less than 1 microgram CaBP/mg protein) in the -D kidney and pancreas. Intestinal, pancreatic and renal calbindin-D28K content was stimulated 318, 9.8 and 2.9 fold respectively, 48 hours after -D chicks received a single dose of 1,25(OH)2D3 [6.5 nmol/animal]. The pancreatic calbindin-D28K content could be significantly stimulated as early as 5 hours after 1,25(OH)2D3 administrations in vivo. These findings support the contention that the pancreas is a target for vitamin D, and is consistent with the view that calbindin-D28K plays a role in normal pancreatic functions.

Animals↗
PubMed1996

Cyclosporine A decreases the protein level of the calcium-binding protein calbindin-D 28kDa in rat kidney.

Despite the widespread use of cyclosporine A (CsA), its mechanism of action and side effects are not yet completely understood. There exists a large body of evidence suggesting that disturbance of calcium homeostasis is a critical step in the cascade of cellular and molecular events induced by the drug. As recently shown in our laboratory by two-dimensional protein gel electrophoresis (2-DE) analysis of kidney homogenates, CsA induced numerous changes in several kidney proteins. One kidney protein in particular was shown to be strongly down-regulated by the drug. In this work we report the identification of the strongly decreased kidney protein as calbindin-D 28kDa, a vitamin D-dependent calcium-binding protein associated with calcium handling by cells. The assignment of the down-regulated protein spot is based on its internal amino acid sequence analysis and its specific reaction with a monoclonal antibody raised against calbindin-D 28kDa. In kidney homogenates of male Wistar rats treated with 50 mg/kg/d CsA for up to 28 days, calbindin levels were measured by ELISA and were shown to be continuously decreased with prolonged CsA treatment. To our knowledge, this is the first report describing the effect of CsA on kidney calbindin-D 28kDa protein levels. Further studies are needed to elucidate whether the CsA-mediated down-regulation of the calcium-binding protein calbindin-D 28kDa may be a critical factor for the renal adverse effects induced by this drug.

Amino Acid Sequence↗