Cell specialization in collecting tubules of the guinea pig kidney: carbonic anhydrase activity and glycosaminoglycan production in different cells.

Abstract

The distribution of complex carbohydrates has been investigated cytochemically at the light and electron microscope levels in collecting ducts of the guinea pig kidney. The dialyzed iron method demonstrated acidic complex carbohydrate ultrastructurally on the outer surface of the apical and the basolateral plasmalemma of the principal cells and in their maturing Golgi cisternae and secretory granules. Glycoconjugate in these sites stained for sulfate esters with the high iron diamine method but lacked reactivity toward the periodic acid-thiocarbohydrazide-silver proteinate (PA-T-SP) sequence for visualizing vic glycol-containing glycoprotein. Lability to testicular hyaluronidase and resistance to sialidase identified the Glycosaminoglycan (GAG) in principal cell granules and the plasmalemmae as a chondroitin sulfate. In contrast, intercalated cells of the collecting ducts failed to stain with the cationic reagents, but showed light PA-T-SP reactivity demonstrative of neutral glycoprotein in the glycocalyx of the apical plasmalemma. Immunostaining with the immunoglobulin-enzyme bridge procedure localized carbonic anhydrase selectively to the intercalated cells. The ultrastructural and cytochemical observations on the guinea pig collecting ducts implicate intercalated cells in fluid and electrolyte transport and principal cells in secretion of a chondroitin sulfate to the tubule lumen and intercellular space.