Apical-basal membrane polarity of membrane phosphatases in isolated capillary endothelium: alteration in ultrastructural localisation under culture conditions.
Capillaries from freshly isolated rat epididymal fat were subjected to protocols that allowed ultrastructural localisation of alkaline phosphatase and 5'-nucleotidase. Alkaline phosphatase was almost entirely restricted to the capillary luminal membrane and vesicles associated with this membrane. 5'-nucleotidase was localised on the basal or abluminal membrane and associated vesicles. Arterioles and occasional venules were also present in the cell isolates, and arteriole localisation of 5'-nucleotidase was identical to that in capillaries. In venules, 5'-nucleotidase often failed to exhibit a polarised distribution and was present on both membrane domains. In confluent cultured endothelial cells, 5'-nucleotidase was not expressed in a predominantly polarised arrangement. Alkaline phosphatase was found on apical surfaces and regions of lateral cell contact. The results of these studies show that capillary endothelial cells exhibit enzyme polarity of their surface membranes which is subject to change on introduction of the cells to tissue culture.
Roberts
R L
RL
Department of Anatomy, University of Iowa, Iowa City 52242.
Sandra
A
A
D015720:5'-Nucleotidase / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D006651:Histocytochemistry; D008099:Liver / Q000648:ultrastructure; D008854:Microscopy, Electron; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats
D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; D015720:5'-Nucleotidase