Heterogeneity of apical glycoconjugates in kidney collecting ducts: further studies using simultaneous detection of lectin binding sites and immunocytochemical detection of key transport enzymes.

In the search for a functional role for the polarized glycoconjugates of rat collecting duct epithelial cells, the relation between binding of various lectins and expression of cellular transport enzyme profile of the cells was studied. For this purpose, principal and intercalated cells of rat kidney collecting duct were identified by morphological criteria and by their immunocytochemically determined content of (Na+ + K+)-ATPase and carbonic anhydrase (CA II), respectively. Various N-acetylgalactosamine-specific lectins such as those from Helix pomatia and Maclura pomifera revealed heterogeneity among both principal and intercalated cells, whereas alpha-N-acetylgalactosamine-specific lectin from Dolichos biflorus and Vicia villosa bound preferentially to principal cells. Still another lectin from Arachis hypogaea reacted with most collecting duct cells in the cortex and outer medulla, but only with a subpopulation of cells in the inner medulla. Interestingly, some lectins reacted exclusively with the apical aspect of the collecting duct epithelial cells, whereas others revealed both an apical and basolateral distribution of lectin reactive glycoconjugates. The results thus show subtle differences in the glycocalyx structure of principal and intercalated cells and differences in the intracellular polarization of glycoconjugates of these cells. Thus, lectins may be useful tools in the study of the molecular mechanisms which establish and maintain the polarized functions of principal and intercalated cells.