Effect of Intravenous Infusion of Calcium Ions on the Biosynthesis of the Vitamin D-Dependent Calcium Binding Protein

1983 ◽  
Vol 27 (1) ◽  
pp. 78-80
Author(s):  
L.T. Jones
Keyword(s):  
Vitamin D ◽  
Calcium Ions ◽  
Intravenous Infusion ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein

Calcium Binding Proteins in the Duodenal Mucosa of the Chick, Rat, Pig, and Human

1972 ◽  
Vol 50 (7) ◽  
pp. 758-765 ◽  
Author(s):  
A. J. W. Hitchman ◽  
Joan E. Harrison
Keyword(s):  
Molecular Weight ◽  
Vitamin D ◽  
Calcium Ions ◽  
Calcium Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Duodenal Mucosa ◽  
Calcium Binding Proteins ◽  
Calcium Binding Protein ◽  
Electrophoretic Mobilities

A calcium binding protein has been demonstrated in human duodenal mucosa which we believe to be human vitamin D dependent CaBP. Sephadex gel filtration demonstrated that the duodenal mucosa of both the human and pig contained a calcium binding protein with a similar molecular weight to the reported vitamin D dependent rat CaBP (M.W. 12 000–13 000) but dissimilar to chick CaBP (M.W. 24 000–28 000). In addition the rat, pig, and human mucosa contained a high molecular weight calcium binding protein which is probably not vitamin D dependent.A relatively simple procedure, utilizing the tagging of CaBP by 47Ca, has been developed to partially purify normal pig CaBP by Sephadex gel filtration. Further fractionation of the 12 000–13 000 M.W. area, using disc electrophoretic procedures, separated two calcium binding proteins which had similar electrophoretic mobilities and calcium binding formation constants (3.5 and 5.5 × 106, respectively), indicating that both are forms of CaBP but that either one or both have been altered during the procedures. The electrophoretic mobilities of both of these proteins are relatively low in the presence of calcium ions but much greater when calcium ions are removed by chelation with EDTA. This finding should facilitate both the identification and purification of mammalian CaBP.

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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