Duodenal calcium binding protein and active calcium transport in rats: are they functionally related?

1994 ◽  
Keyword(s):  
Calcium Binding ◽  
Calcium Transport ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Active Calcium

Calcium-transport function of the chick embryonic chorioallantoic membrane. II. Functional involvement of calcium-binding protein, Ca2+-ATPase and carbonic anhydrase

1986 ◽  
Vol 82 (1) ◽  
pp. 85-97
Author(s):  
R.S. Tuan ◽  
M.J. Carson ◽  
J.A. Jozefiak ◽  
K.A. Knowles ◽  
B.A. Shotwell
Keyword(s):  
Carbonic Anhydrase ◽  
Calcium Binding ◽  
Calcium Transport ◽  
Calcium Uptake ◽  
Binding Protein ◽  
Chorioallantoic Membrane ◽  
Calcium Binding Protein ◽  
Transport Pathway ◽  
Functional Involvement ◽  
Active Calcium

This study aimed to investigate the mechanism of active calcium transport in the chick embryonic chorioallantoic membrane (CAM) by assessing the functional involvement of three previously identified, putative components of the transport pathway. These components are a calcium-binding protein (CaBP), Ca2+-activated ATPase and carbonic anhydrase. Using specific reagents, including antibodies and enzyme inhibitors in vivo and in vitro in CAM calcium uptake assays, it was shown that these biochemically identified components were all functionally involved. The results of these studies also indicate that active calcium uptake by the CAM requires the presence of the CaBP on the cell surface in a laterally mobile manner, while carbonic anhydrase appeared to be a cytosolic component. We further analysed the subcellular location of the calcium-uptake activity by gel filtration and density-gradient fractionation of cell-free microsomes of the CAM and the results suggest that this activity is associated with the plasma membrane.

scholarly journals Calcium-binding protein of the chick chorioallantoic membrane. I. Immunohistochemical localization

1978 ◽  
Vol 77 (3) ◽  
pp. 743-751 ◽  
Author(s):  
RS Tuan ◽  
WA Scott ◽  
ZA Cohn
Keyword(s):  
Calcium Binding ◽  
Calcium Transport ◽  
External Surface ◽  
Binding Protein ◽  
Chorioallantoic Membrane ◽  
Immunohistochemical Localization ◽  
Calcium Binding Protein ◽  
Transport Function ◽  
Chick Chorioallantoic Membrane

The preparation of a specific antiserum (anti-CaBP) against the calcium-binding protein (CaBP) of the chorioallantoic membrane (CAM) is described. The anti-CaBP appeared to be specific for the CaBP by immunodiffusion and immunoelectrophoresis. Application of the anti-CaBP in immunofluorescence histochemistry revealed that the CaBP is present in the CAM only at developmental ages corresponding with the expression of the calcium transport function of the membrane. Furthermore, the CaBP is localized to the ectoderm of the CAM, appears to be exposed to the entire external surface of the ectoderm, and can be shown to be associated with cells enzymatically dissociated from the CAM. These results are consistent with a functional role of the CaBP in the CAM calcium transport process.

Calcium binding protein and regulation of calcium transport

1975 ◽  
Vol 21 (1) ◽  
pp. 27-38 ◽  
Author(s):  
F. Bronner ◽  
Y. Charnot ◽  
E. E. Golub ◽  
T. Freund
Keyword(s):  
Calcium Binding ◽  
Calcium Transport ◽  
Binding Protein ◽  
Calcium Binding Protein

Intestinal vitamin D-induced calcium-binding protein: time-course of immunocytological localization following 1,25-dihydroxyvitamin D3.

1983 ◽  
Vol 31 (3) ◽  
pp. 426-432 ◽  
Author(s):  
A N Taylor
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Calcium Transport ◽  
Time Course ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Dihydroxyvitamin D3 ◽  
Migration Rates ◽  
1,25 Dihydroxyvitamin D3 ◽  
Free Cells

The vitamin D-induced calcium-binding protein (CaBP) was localized in histological sections of chick duodenum using the peroxidase-antiperoxidase immunocytochemical technique. The time-course of appearance of CaBP in rachitic chicks was investigated from 0 to 120 hr after stimulation by 1,25-dihydroxyvitamin D3 (1,25(OH)2D3). CaBP was not routinely detected at 0 hr after 1,25(OH)2D3 administration. CaBP was first noted in some, but not all, of the samples taken 2 hr following 1,25(OH)2D3 and was detected in all 2 1/2 hr samples. The number of CaBP-containing absorptive cells and the apparent CaBP concentration both increased to a maximum at about 16-24 hr. At later times, as CaBP free cells migrated up the villi, the CaBP-containing cells decreased in number, but even at 120 hr post 1,25(OH)2D3 dose there were significant numbers of CaBP-containing cells present. The relationships between time-course of CaBP location on intestinal villi, enterocyte migration rates, and the time-course of 1,25(OH)2D3 stimulated intestinal calcium transport are discussed.

Vitamin D Dependence of In Vivo Calcium Transport and Mucosal Calcium Binding Protein in Rat Large Intestine

1979 ◽  
Vol 76 (1) ◽  
pp. 99-104 ◽  
Author(s):  
M. Michael Petith ◽  
Helen D. Wilson ◽  
Harold P. Schedl
Keyword(s):  
Vitamin D ◽  
Large Intestine ◽  
Calcium Binding ◽  
Calcium Transport ◽  
Binding Protein ◽  
Calcium Binding Protein
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