Calcium-transport function of the chick embryonic chorioallantoic membrane. II. Functional involvement of calcium-binding protein, Ca2+-ATPase and carbonic anhydrase.
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.
D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002256:Carbonic Anhydrases / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D005591:Chemical Fractionation; D002642:Chick Embryo; D005321:Extraembryonic Membranes / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism
D002135:Calcium-Binding Proteins; D002256:Carbonic Anhydrases; D000252:Calcium-Transporting ATPases; D002118:Calcium