Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Calbindin-D 28 kDa (CaBP 28 kDa), a vitamin D-dependent calcium-binding protein, has been associated with calcium handling by cells. We have investigated the expression of this protein in the rat incisor enamel organ, an epithelium interposed between a mineralizing matrix and connective tissue rich in blood vessels, by radioimmunoassay (RIA), Western blotting, and quantitative protein A-gold immunocytochemistry with antibodies to rat kidney CaBP 28 kDa. RIA of cytosolic extracts showed that enamel organs contained relatively high concentrations of CaBP 28 kDa (compared to kidney; see review by Christakos S., C. Gabrielides, and W.B. Rhoten 1989 Endocr. Rev., 10:3-25). Immunoblotting of proteins extracted from enamel organ strips revealed an intensely-stained band near 28 kDa throughout amelogenesis following ameloblast differentiation. Immunocytochemically, CaBP 28 kDa was localized exclusively within ameloblasts. The density of labelling increased from the presecretory stage to the secretory stage and fluctuated across the maturation stage in relation to ameloblast modulation. Ruffle-ended ameloblasts consistently showed the most intense immunoreaction. Gold particles were present throughout the cytoplasm and nuclei of ameloblasts but regions rich in rough endoplasmic reticulum or cell webs showed a higher immunolabelling. Some gold particles were also associated with the external face of the rough endoplasmic reticulum. Multivesicular bodies in maturation stage ameloblasts were occasionally immunoreactive. These data suggest that the intracellular concentration of CaBP 28 kDa is regulated throughout amelogenesis reflecting a stage-specific control of calcium homeostasis in ameloblasts.
Anat Rec 1991 Jun
PMID:Differential expression of calbindin-D 28 kDa in rat incisor ameloblasts throughout enamel development. 186 92

An indirect immunoperoxidase procedure was used to detect the presence of calbindin-D28K and calbindin-D9K in the cerebellum, kidney, and duodenum of the baboon Papio ursinus. Antibodies to chick calbinding-D28K and to both rat and mouse calbindin-D9K were used. The cerebellum and kidney were shown to contain calbindin-D28K; the doudenum contained calbindin-D9K. In the cerebellum, positive staining was found in the Purkinje cells only; in the kidney, positive staining was found in the distal convoluted tubules, connecting tubules, and collecting tubules, extending deep into the medullary regions of the kidney. Staining in the duodenum was confined to the enterocytes of the villi, with no stain present in the crypt regions or goblet cells. Thus the baboon, a primate, contains the larger of the calbindins in both the cerebellum and kidney as does the human and monkey, but its distribution in the kidney is more generalized than that found in humans. The molecular weight of calbindin-D9K was found to be similar to that found in other animals. However, the calbindin-D28K from the baboon tissues appears to be slightly smaller than the protein found in other animals and may therefore be of similar size to the human calbindin-D28K (Mr 26,000).
Anat Rec 1990 Dec
PMID:Immunohistochemical localization of calbindins (28K and 9K) in the tissues of the baboon Papio ursinus. 228 58

Gene expression for calbindin-D28k, the 28,000 relative molecular mass vitamin D-dependent calcium-binding protein, was measured in cells of the murine nephron by in situ hybridization on tissue sections (hybridization cytochemistry). Radiolabeled (35S-UTP), single-stranded RNA complementary to calbindin-D28k-mRNA (probe RNA) was prepared from linearized cDNA template and used for the hybridizations. Autoradiography was carried out and cellular levels of hybridization signal (silver grains) were quantified. After correction for background the concentration of silver grains was more than 350% greater in the distal tubule than in either the proximal tubule or the glomerulus. The relative cellular level of mRNA in the cytoplasm, as reflected in silver grains/cell, of the distal tubules with probe RNA was 3.4 times greater than that with control RNA. Cells of the distal tubule were the only apparent sites of specific hybridization with probe RNA. The presence of calbindin-D28k-mRNA in the distal tubule corresponded to the localization of calbindin-D28k by immunocytochemistry.
Anat Rec 1990 Jun
PMID:Cellular gene expression for calbindin-D28k in mouse kidney. 235 3

The calcium-binding protein (CaBP) calbindin has been implicated in the molecular mechanism of placental calcium transfer. Previous light microscopic studies have identified CaBP in visceral (but not parietal) endodermal cells of the yolk sac with the most intense immunocytochemical signal observed in the intraplacental yolk sac. In the present studies, electron microscopy was used to study the localization of CaBP in placenta. Placentas of 17-day pregnant mice were fixed by perfusion in 0.5% glutaraldehyde, embedded in low-temperature Lowicryl K4M, and examined in thin section for specific labeling with a polyclonal antiserum. Antibody to CaBP was localized by using protein A-gold particles which were quantified for subcellular compartmentation by using a Videoplan computer system. A high signal for CaBP was found in the visceral endodermal cells of the intraplacental yolk sac. In these cells, gold particles indicating the location of CaBP were observed over 1) the cytoplasmic matrix where the average number of gold particles per micron 2 was 33; 2) the microvilli (17/micron 2); 3) the mitochondria (17/micron 2); and 4) the nucleus (43/micron 2). Sections from antigen-absorbed controls, by contrast, showed few gold particles: cytosol, 2/micron 2; microvilli, 5/micron 2; mitochondria, 5/micron 2; and nucleus, 4/micron 2. Electron-lucent profiles of the Golgi and endoplasmic reticulum contained no particles in the controls and a low particle count (4/micron 2) in the stained sections. Parietal endodermal cells of the intraplacental yolk sac showed a relatively low signal for CaBP compared with the visceral endodermal cells (5 particles/micron 2 vs. 39).(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1988 Nov
PMID:Ultrastructural localization of the 9-kilodalton vitamin D-dependent calcium-binding protein in the murine intraplacental yolk sac. 321 76

A protein of approximately 28,000 relative molecular mass (Mr) cross-reacting with antiserum against the 28,000-Mr rat renal calcium-binding protein (calbindin-D28k) has been localized in the kidney of a salientian amphibian, Rana catesbeiana. Cells reactive for calbindin-D28k were found in the distal tubule at all stages of metamorphosis by the unlabeled antibody peroxidase-antiperoxidase technique. Adult kidneys appeared to have more calbindin-D28k-positive cells. The renal corpuscle, neck, and proximal tubule were negative. An immunoreactive 28,000-Mr band that comigrated with the band of calbindin-D28k was visualized by the immunoblot technique. The finding of the 28,000-Mr calbindin-D in the anamniotic kidney demonstrates that this calcium-binding protein (CaBP) is phylogenetically older than our previous studies of higher vertebrates had revealed (Rhoten et al., 1985). Although the function of calbindin-D28k in the distal nephron is unknown, this CaBP can now be presumed to have functional significance in the mesonephric as well as the metanephric kidney.
Anat Rec 1986 Oct
PMID:Calcium-binding protein (28,000 Mr calbindin-D28k) in kidneys of the bullfrog Rana catesbeiana during metamorphosis. 349 Aug 5

Specific antisera raised against calbindin-D28K (CaBP), the vitamin D-dependent calcium-binding protein from chick intestine, was used to localize the protein in chick ultimobranchial glands (UB glands) by the peroxidase-antiperoxidase technique. CaBP was localized in secretory cells in the cell cords and in a few cells of the epithelium lining the follicles. It was not found in the fibroblastlike cells in the cell cords nor in islands of parathyroid tissue present in the UB gland. The immunomarker for CaBP was distributed throughout the cytoplasm and nucleus of the secretory cells. The same cells demonstrated a positive reaction in their cytoplasm when reacted with an antiserum specific for salmon calcitonin (CT), thus confirming the presence of CaBP and CT in the same UB-gland secretory cells. In other tissues, the presence of CaBP is regarded as an end-organ marker for actions of the vitamin D endocrine system. This novel demonstration of CaBP in UB-gland cells responsible for secretion of calcitonin suggests a direct effect of the vitamin D endocrine system on those cells in addition to an indirect effect through the stimulation produced by elevated circulating calcium levels.
Anat Rec 1987 Sep
PMID:Localization of calbindin-D28K in calcitonin containing cells of chick ultimobranchial glands. 368 64

Specific antibodies raised against a 28-kilodalton chick intestinal calcium-binding protein (calbindin-D28k) were used to localize the protein immunocytochemically in the developing rabbit kidney. Kidneys taken from rabbits between the 13th embryonic and 17th postnatal day were examined. Calbindin-D28k was observed in the mesonephric duct and the ureteral bud on the 13th embryonic day. During subsequent involution of the mesonephros, the ampullae of the metanephric ureteral buds contained calbindin-D28k. The protein was gradually lost from the ureters and the deep interstitial collecting ducts. Calbindin-D28k was never present in the renal vesicles derived from the nephrogenic blastema, but it was present in the connecting tubule segments during formation of the arcades. The last finding supports the belief that the connecting tubule is derived from the ureteral bud.
Anat Rec 1986 Aug
PMID:Immunohistochemical localization of calbindin-D28k during the development of the rabbit nephron. 374 Apr 72

Calmodulin distribution in the chicken pineal organ was investigated by immunohistochemistry. Calmodulin immunoreactivity was detected in ependymocytes in the follicular zone and in interstitial cells in the parafollicular zone. No calmodulin immunoreactivity was detected in pinealocytes. Lack of calmodulin immunoreactivity in pinealocytes raises questions about its proposed function in melatonin synthesis as suggested by pharmacological studies using calmodulin antagonists. The calmodulin distribution was comparable to that of S100, a glial cell marker. Two other markers, calbindin-D28k and calretinin, which in neuroanatomical studies give excellent cytoarchitectonic staining, in the chick pineal permitted the detection of two subclasses of pinealocytes. One was darkly stained by calbindin-D28k and rare. The other was very abundant and calretinin positive. In the parafollicular zone, calbindin-D28k and/or calretinin antibodies allowed us to visualize cells presenting a neuron-like morphology. Calretinin immunoreactivity was detected in nearly all pinealocytes in which hydroxy-indol-O-methyl transferase was also located. Comparison between the lack of calmodulin and the presence of calretinin, belonging to the same calcium-binding protein family, in chick pinealocytes raises the hypothesis about a possible role of calretinin in melatonin synthesis.
Anat Rec 1994 Feb
PMID:Calmodulin immunoreactivity in the chicken pineal gland: comparison with calbindin-D28k, calretinin, and S100. 751 10

Previous studies have demonstrated the presence of calbindin D28k in the ameloblasts derived from the inner enamel epithelium. The occlusal surfaces of the rodent molars partly lack the enamel covering, which is referred to as enamel-free area (EFA). In the present study, we compared the immunohistochemical localization of calbindin D28k-like immunoreactivity (CB-LI) in the cells at the EFA (EFA cells) and ameloblasts of the rat molar teeth at the light microscopic level. CB-LI was strong in the ameloblasts of the presecretory through the protective stages, while it was faint at the late secretory to transitional stages. However, some mature ameloblasts lacked the immunoreactivity. On the other hand, the majority of EFA cells showed distinct polarization and elongation that were absent in few cells at the early stage of EFA formation. At all stages, the EFA cells adjacent to the ameloblasts showed CB-LI, however, some cells adjacent to the mature ameloblasts lacked the reaction. Intensive CB-LI was demonstrated in EFA cells at the reduced enamel epithelium. These immunohistochemical findings suggest EFA cells have cytochemical properties similar to those of ameloblasts.
Anat Rec 2000 04 01
PMID:Calbindin D28k-like immunoreactivity during the formation of the enamel-free area in the rat molar teeth. 1073 56

The distribution of the calbindin D28k in the laryngeal sensory structures was studied by immunohistochemistry, immunoelectronmicroscopy, and double immunofluorescence with calretinin-immunoreactivity. Moreover, origin of the nerve endings were observed using retrograde tracer, fast blue. Immunoreactivity for calbindin D28k was found in the various types of nerve endings in the larynx, namely, laminar nerve endings, nerve endings associated with the taste buds, intraepithelial nerve endings, and endocrine cells. The laminar endings with calbindin D28k-immunoreactivity were observed in the subepithelial connective tissue. In some endings, terminals were expanded. The laminar endings were also observed in the perichondrium of the epiglottic cartilage. In the epiglottic and arytenoid epithelia, thick nerve fibers with calbindin D28k-immunoreactivity ascending to taste buds and intragemmal nerve fibers were also observed. Within the epithelial layer, intraepithelial free nerve endings with calbindin D28k-immunoreactivity were observed. Furthermore, diffuse endocrine cells were observed within the laryngeal epithelium. By immunoelectron microscopy, immunoreaction products in the endings mentioned above were localized in the cytoplasm of the axon terminals and nerve fibers which contained with numerous mitochondria. Out of the 100 laminar endings, 18 endings were immunopositive for both calbindin D28k and calretinin, 33 were positive for calbindin D28k but negative for calretinin, and 49 were positive for only calretinin in the double immunofluorescence microscopy. The nerve fibers associated with the taste buds and the free nerve endings, which immunostained for calbindin D28k, were not stained with antibody against calretinin. After injection of the fast blue in the laryngeal mucosa, fast blue-labeled cells were mainly observed in the nodose ganglia. Of the total number of labeled cell in the nodose and dorsal root ganglia at the level C1 to Th2, 65.1% occurred in nodose ganglia (572/879, n = 6). In the nodose ganglia, 79.7% of labeled cells (456/572) were immunoreacted for calbindin D28k. The distribution of calbindin D28k-immunoreactivity may be differnt from that of calretinin. It is suggested that calbindin D28k have regulatory role on intracellular calcium concentration in the laryngeal sensory corpuscles.
Anat Rec 2000 07 01
PMID:Calbindin D28k-immunoreactive afferent nerve endings in the laryngeal mucosa. 1086 58


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