Ontogeny of calbindin-D28K and calbindin-D9K in the mouse kidney, duodenum, cerebellum and placenta

Development ◽  
1992 ◽  
Vol 116 (2) ◽  
pp. 491-496 ◽  
Author(s):  
D.R. Shamley ◽  
L.A. Opperman ◽  
R. Buffenstein ◽  
F.P. Ross
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Giant Cells ◽  
Mouse Kidney ◽  
Embryonic Mouse ◽  
Immunohistochemical Assay ◽  
Calbindin D9k ◽  
Early Appearance ◽  
Mesonephric Duct ◽  
Calbindin D28k

The appearance of the calcium-binding proteins (CaBP-D28K and CaBP-D9K) in embryonic mice tissues was determined using a sensitive immunohistochemical assay. CaBP-D28K first appears in myenteric nerve plexuses of the duodenum on day E15, in duodenal villus cells on day E16, in Purkinje cells of the cerebellum on day E19, in cells of the mesonephric duct on day E11 and in the metanephric duct on day E12. CaBP-D9K first appears in enterocytes of the duodenum on day E18, in trophoblastic giant cells (TGC) of the placenta on day E10, and in the metanephric duct on day E15. A differential time of appearance and colocalization of the two CaBPs is demonstrated in the embryonic mouse kidney, suggesting either that vitamin D does not control both CaBPs in the foetus or that the vitamin D control is unequal. The early appearance and location of CaBP-D9K in TGCs may suggest that these cells play an important role in transplacental transfer of calcium.

Trophoblastic giant cells of the mouse placenta contain calbindin-D9k but not the vitamin D receptor

1996 ◽  
Vol 150 (1) ◽  
pp. 25-32 ◽  
Author(s):  
D R Shamley ◽  
G Veale ◽  
J M Pettifor ◽  
R Buffenstein
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Calcium Binding ◽  
Giant Cells ◽  
Yolk Sac ◽  
Vitamin D Status ◽  
Maternal Vitamin ◽  
Calbindin D9k ◽  
Mouse Placenta ◽  
Maternal Vitamin D Status

Abstract The effects of vitamin D deficiency on the ontogeny of calcium-binding proteins (CaBPs) and the vitamin D receptor (VDR) in the placenta and yolk sac of the mouse were examined. Maternal vitamin D status did not affect the time of appearance of CaBP-D9k (9 kDa) in the yolk sac endoderm or trophoblastic giant cells (TGCs) of the placenta. VDRs were undetectable in TGCs and yolk sac endoderm, but were present in the intraplacental yolk sac. Since yolk sac endoderm and TGCs contain CaBP but not VDR, it is unlikely that CaBP synthesis and/or activity in these cells is controlled by vitamin D. The TGCs, therefore, may be involved in vitamin D-independent transplacental transfer of calcium. Journal of Endocrinology (1996) 150, 25–32

RT-PCR microlocalization of mRNAs for calbindin D28k and vitamin D receptor in the murine nephron

1996 ◽  
Vol 270 (4) ◽  
pp. F677-F681 ◽  
Author(s):  
L. Liu ◽  
A. Khastgir ◽  
J. M. McCauley ◽  
S. T. Dunn ◽  
J. H. Morrissey ◽  
...  
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Calcium Binding ◽  
Spatial Relationship ◽  
Pcr Primers ◽  
Rt Pcr ◽  
Calbindin D28k ◽  
Actin Mrna ◽  
Polymerase Chain ◽  
Convoluted Tubules

The spatial relationship between vitamin D receptor (VDR) and calbindin D28k [calcium binding protein D28k (CaBP-D28k)] gene expression within the murine kidney was studied by localizing their mRNAs in discrete nephron structures using reverse transcription-polymerase chain reaction (RT-PCR). Primers for beta-actin mRNA were used as a control for the presence of tissue during RT-PCR for CaBP-D28k mRNA. mRNA for CaBP-D28k was found only in distal convoluted tubules (DCTs), connecting tubules (CNTs), and cortical collecting ducts (CCDs). In contrast, VDR mRNA was detected in glomeruli, S2 proximal convoluted tubules, cortical thick ascending limbs of Henle's loop, DCTs, CNTs, and initial CCDs. The presence of both VDR and CaBP-D28k mRNA in DCTs, CNTs, and CCDs is consistent with the hypothesis that cacitriol acts via the VDR to stimulate CaBP-D28k synthesis. Conversely, the presence of VDR mRNA in other parts of the nephron suggests that calcitriol has genomically mediated actions within the kidney in addition to stimulation of CaBP-D28k synthesis.

Molecular Cloning of Mammalian 28,000 Mr Vitamin D-Dependent Calcium Binding Protein (Calbindin-D28K): Expression of Calbindin-D28K RNAs in Rodent Brain and Kidney

DNA ◽  
1988 ◽  
Vol 7 (9) ◽  
pp. 585-593 ◽  
Author(s):  
TERESA L. WOOD ◽  
YUTAKA KOBAYASHI ◽  
GRETCHEN FRANTZ ◽  
SAMUEL VARGHESE ◽  
SYLVIA CHRISTAKOS ◽  
...  
Keyword(s):  
Vitamin D ◽  
Molecular Cloning ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Rodent Brain ◽  
Calbindin D28k

Elevated Levels of Vitamin D-Dependent Calcium-Binding Protein (Calbindin-D9k) in the Osteosclerotic (oc) Mouse*

Endocrinology ◽  
1988 ◽  
Vol 122 (3) ◽  
pp. 1067-1073 ◽  
Author(s):  
MARK F. SEIFERT ◽  
RICHARD W. GRAY ◽  
M. ELIZABETH BRUNS
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calbindin D9k

Elevated 1,25-dihydroxyvitamin D3 and intestinal calbindin-D9k in the toothless rat

1990 ◽  
Vol 258 (2) ◽  
pp. E377-E381
Author(s):  
M. F. Seifert ◽  
R. W. Gray ◽  
M. E. Bruns
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Morphological Evidence ◽  
Vitamin D Metabolites ◽  
Dihydroxyvitamin D3 ◽  
1,25 Dihydroxyvitamin D3 ◽  
Calbindin D9k ◽  
Plate Morphology ◽  
Circulating Levels ◽  
Phosphorus Levels

The toothless (tl) rat is a nonlethal osteopetrotic mutation characterized by systemic skeletal sclerosis, growth plate morphology suggestive of rickets, and morphological evidence of reduced osteoclastic bone resorption. Vitamin D metabolites, serum calcium and phosphorus levels, and the developmental appearance of vitamin D-dependent intestinal calcium binding protein (calbindin-D9k) was studied in normal and mutant rats of tl stock from 7 to 35 days of age. 1,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] was found to be significantly elevated in mutant animals by 7 days of age (71 +/- 9 pM, tl/tl vs. 24 +/- 8 pM, +/?) and continued to increase to a peak of 428 pM at the time of weaning. This was 240% higher than normals at this period. The elevated levels of 1,25-(OH)2D3 stimulated a significant and precocious appearance of intestinal calbindin-D9k in mutants, beginning by 14 days of age and reaching their peak levels at 21 days postpartum (25.6 +/- 1.7 micrograms/mg protein, tl/tl vs. 16.4 +/- 1.5 micrograms/mg protein, +/?). The cause of the elevated circulating levels of 1,25-(OH)2D3 in tl rats is unknown but may be due to the low serum phosphorus levels present in these animals.

190 EXPRESSION OF APOPTOTIC GENES IS MEDIATED BY CALCIUM-BINDING PROTEINS, CALBINDINS, IN THE UTERUS OF CALBINDIN-D9k AND CALBINDIN-D28k KNOCKOUT MICE

2011 ◽  
Vol 23 (1) ◽  
pp. 196
Author(s):  
E.-M. Jung ◽  
E.-B. Jeung
Keyword(s):  
Calcium Binding ◽  
Wild Type ◽  
Stress Genes ◽  
Protein Levels ◽  
Bax Protein ◽  
Calbindin D9k ◽  
Important Regulator ◽  
Calbindin D28k ◽  
Apoptotic Genes ◽  
Apoptosis Related Gene

Calcium (Ca2+) is known to be an important regulator in apoptotic signalling. The uterine calbindins, calbindin-D9k (CaBP-9k) and calbindin-28k (CaBP-28k), are known to be involved in the regulation of myometrial activities by regulating intracellular Ca2+. In addition, the uterine calbindins are expressed in the mouse endometrium and are highly regulated during implantation and development. The aim of the present study was to evaluate the regulation of apoptosis in the uterus of immature CaBP-9k, CaBP-28k, and CaBP-9k/28k knockout (KO) mouse models. Our findings indicate that Bax protein levels were enhanced in the uterus of CaBP-28k and CaBP-9k/28k KO mice compared with wild-type mice, and no difference was observed in Bcl-2 protein expression. In addition, the levels of caspase 3, 6, and 7 protein were induced in both CaBP-28k and CaBP-9k/28k KO mice compared with wild-type mice. These results suggest that the absence of calbindins may induce an increase in apoptotic signalling. In addition, we investigated the expression of the endoplasmic reticulum stress genes by Western blot analysis in calbindin KO mice. These results showed that CHOP and BiP proteins were increased in CaBP-28k and CaBP-9k/28k KO mice compared with wild-type mice, and no difference was observed in the expression of PDI and IRE1α proteins. It is of interest that the expression of CaBP-28k may block up-regulation of apoptosis-related genes. In summary, this study implies that CaBP-28k may decrease apoptosis-related gene expression in the uterine tissue of immature mice.

Differential regulation of calbindin-D28k mRNA in the intestine and eggshell gland of the laying hen

1990 ◽  
Vol 4 (2) ◽  
pp. 93-99 ◽  
Author(s):  
A. Bar ◽  
S. Striem ◽  
S. Mayel-Afshar ◽  
D. E. M. Lawson
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Egg Production ◽  
Laying Hens ◽  
Deficient Diet ◽  
Dihydroxyvitamin D ◽  
Calbindin D28k ◽  
Calcification Process ◽  
Calbindin D ◽  
Post Transcriptional Regulation

ABSTRACT The effect of shell calcification and 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3) on calbindin-D28k (previously known as vitamin D-dependent calcium-binding protein) and calbindin mRNA was investigated in the intestine and eggshell gland (ESG) of juvenile female chicks, laying hens and non-laying female birds with active gonads. Increasing amounts of 1,25-(OH)2D3 were fed to laying hens and juvenile birds treated with oestradiol to develop the ESG. The intestinal concentration of calbindin was increased 30-fold by 1,25-(OH)2D3 in chicks treated with oestradiol and fed a vitamin D-deficient diet. In these same animals, 1,25-(OH)2D3 had no effect on the formation of calbindin mRNA or calbindin in the ESG even though fully viable 1,25-(OH)2D3 receptors are present in this tissue. In laying birds fed adequate amounts of vitamin D3, intestinal, but not ESG, calbindin was increased by the addition of 1,25-(OH)2D3 to the diet. At the onset of egg production the concentrations of calbindin and calbindin mRNA were increased in the intestine and ESG. This increase occurred within the period of calcification of the first egg, through a process unaffected by vitamin D. Calcification of the first egg increased the concentration of calbindin in the ESG by eight- to tenfold, although the concentration of calbindin mRNA was increased by only two- to threefold. These results suggest that the induction of calbindin synthesis by 1,25-(OH)2D3 or by the egg calcification process is associated with an increase in the concentration of calbindin mRNA in the ESG and intestine. They also suggest that the vitamin D-dependent physiological changes in the ESG occurring during the calcification process do not include an increase in calbindin synthesis, that calbindin is induced and/or regulated by a mechanism requiring additional factors besides 1,25-(OH)2D3, and that post-transcriptional regulation of calbindin synthesis in these tissues may be possible.

In vitro enzyme activation with calbindin-D28k, the vitamin D-dependent 28 kDa calcium binding protein

FEBS Letters ◽  
1992 ◽  
Vol 297 (1-2) ◽  
pp. 127-131 ◽  
Author(s):  
Peter D. Reisner ◽  
Sylvia Christakos ◽  
Thomas C. Vanaman
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Enzyme Activation ◽  
Calbindin D28k

Appearance during chick embryogenesis of vitamin D-dependent calcium-binding protein (calbindin-D28K)

1990 ◽  
Vol 9 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Lynne A. Opperman ◽  
F. Patrick Ross ◽  
Brenda Stein ◽  
Gordon Hirsch
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Chick Embryogenesis ◽  
Calbindin D28k
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