Vitamin D Metabolism and Calbindin (Calcium-Binding Protein) in Aged Laying Hens

1987 ◽  
Vol 117 (10) ◽  
pp. 1775-1779 ◽  
Author(s):  
Arie Bar ◽  
Shmuel Hurwitz
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Laying Hens ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Vitamin D Metabolism

scholarly journals Calcium-binding protein and vitamin D metabolism in experimental protein malnutrition

1974 ◽  
Vol 32 (3) ◽  
pp. 569-578 ◽  
Author(s):  
W. J. Kalk ◽  
B. L. Pimstone
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Protein Deprivation ◽  
Vitamin D Metabolism ◽  
Renal Metabolism ◽  
Acid Substrate ◽  
Amino Acid Substrate ◽  
25 Hydroxycholecalciferol

1. Intestinal and renal vitamin D-dependent calcium-binding protein (CaBP) activity and cholecalciferol metabolism were investigated in the protein-deficient rat (40 g casein/kg diet) and in control animals (200 g casein/kg diet). Compared to control animals, 3 weeks of protein deprivation resulted in consistently reduced intestinal CaBP activity, while renal CaBP activity was not significantly altered.2. Intestinal CaBP activity was greatly reduced in rats fed on diets deficient in both protein and vitamin D. CaBP activity was doubled by cholecalciferol administration, but did not reach control values. The rate of conversion of intravenously injected [3H]cholecalciferol to 25-hydroxycholecalciferol (25-HCC) and the disappearance rates of plasma 25-HCC were similar in the two groups of animals.3. It is concluded that in the protein-deficient rat: (a) intestinal CaBP activity is reduced; (b) coexistent vitamin D deficiency reduces intestinal CaBP activity still further, but the intestinal mucosa retains the potential to respond to administered cholecalciferol: (c) hepatic and probably renal metabolism of cholecalciferol appear to be normal; (d) reduced CaBP is likely to be the result of reduced CaBP synthesis as a consequence of deficient amino acid substrate.

IMMUNOCYTOCHEMISTRY OF VITAMIN D-DEPENDENT CALCIUM BINDING PROTEIN IN CHICK PANCREAS: EXCLUSIVE LOCALIZATION IN B-CELLS.*

Endocrinology ◽  
1982 ◽  
Vol 110 (6) ◽  
pp. 2216-2218 ◽  
Author(s):  
JURGEN ROTH ◽  
SUSAN BONNER-WEIR ◽  
ANTHONY W. NORMAN ◽  
LELIO ORCI
Keyword(s):  
Vitamin D ◽  
B Cells ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein

scholarly journals Vitamin D-dependent Calcium-binding Protein

1968 ◽  
Vol 243 (14) ◽  
pp. 3978-3986 ◽  
Author(s):  
R H Wasserman ◽  
R A Corradino ◽  
A N Taylor
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein

scholarly journals Vitamin D-dependent Calcium-binding Protein

1968 ◽  
Vol 243 (14) ◽  
pp. 3987-3993 ◽  
Author(s):  
R H Wasserman ◽  
A N Taylor
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein

scholarly journals In situ detection of vitamin D-induced calcium-binding protein (9-kDa CaBP) messenger RNA in rat duodenum.

1986 ◽  
Vol 34 (2) ◽  
pp. 277-280 ◽  
Author(s):  
M Warembourg ◽  
O Tranchant ◽  
C Perret ◽  
C Desplan ◽  
M Thomasset
Keyword(s):  
Vitamin D ◽  
In Situ Hybridization ◽  
Calcium Binding ◽  
Binding Protein ◽  
Cdna Probe ◽  
Calcium Binding Protein ◽  
Pbr322 Dna ◽  
Rat Duodenum ◽  
Columnar Cells

We have previously described the molecular cloning of a cDNA fragment synthesized from rat duodenal mRNA coding for a 9000-dalton vitamin D-induced calcium-binding protein (9-kDa CaBP) (3). We now report the use of this cloned cDNA to study the cytological distribution of 9-kDa CaBP mRNA in rat duodenum by in situ hybridization. Tissue sections, fixed in ethanol:acetic acid, were hybridized to the 3H-cDNA probe and processed for autoradiography. The specificity of the CaBP mRNA-DNA hybrid formation was checked using 3H-labeled plasmid pBR322 DNA as a control probe. 9k-Da CaBP mRNA, visualized by silver grains, was found only in the absorptive epithelial cells, and the concentration was greater in the cells at the villous tips than in those of the crypts. The 9k-Da CaBP mRNA was observed mainly in the cytoplasm of the columnar cells and less frequently in the nucleus. Labeling was not seen in the brush border and goblet cells. The submucosa, with Brunner's glands and muscularis, also showed no specific 9-kDa CaBP mRNA concentration. This demonstration of 9-kDa CaBP gene activity in the columnar cells of the rat duodenum illustrates the usefulness of in situ hybridization for characterization of specific cells involved in the expression of 1,25(OH)2 D3 activity.

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