Alternative ultrastructural localization of Dolichos biflorus lectin binding sites in proton secreting parietal cells of mice.
High amount of N-acetyl-D-galactosamine specific lectin binding sites were detected on the canalicular membranes of human parietal cells. Our present model investigations on mice showed that the intracellular distribution of the terminal N-acetyl-D-galactosamine containing glycoprotein highly depends on the actual functional state of the parietal cells. In the normal gastric mucosa 40%-60% of parietal cells react positively after staining with horseradish peroxidase or biotin labelled Dolichos biflorus lectin. Ultrastructurally lectin binding sites occur mainly on the basolateral membrane infoldings in fed animals, while they are present exclusively on the canalicular membranes of fasting mice, suggesting that the alternative appearance of lectin binding sites on the opposite membrane areas of parietal cells is tightly coupled to their main function, to H+ secretion.
Fischer
J
J
Department of Pathology, University Medical School of Pécs, Hungary.
D000818:Animals; D007124:Immunoenzyme Techniques; D051379:Mice; D008807:Mice, Inbred BALB C; D008814:Mice, Inbred NZB; D010295:Parietal Cells, Gastric / Q000378:metabolism* / Q000648:ultrastructure; D011522:Protons; D011975:Receptors, Mitogen / Q000032:analysis*; D013217:Starvation / Q000378:metabolism
C027654:Dolichos biflorus lectin receptor; D011522:Protons; D011975:Receptors, Mitogen