The expression of alpha2,6- and alpha2,3-linked sialic acids on N-glycans was studied in embryonic, postnatal, and adult rat kidney. Histochemistry and blotting using Polyporus squamosus and Sambucus nigra lectins for alpha2,6-linked sialic acids and the Maackia amurensis lectin for alpha2,3-linked sialic acids were performed and sialyltransferase activity was assayed. N-glycans with alpha2,6- and alpha2,3-linked sialic acid were differently expressed in the two embryonic anlagen and early stages of nephron. Metanephrogenic mesenchyme was positive for alpha2,3-linked sialic acid but not for the alpha2,6-linked one, which became detectable initially in the proximal part of S-shaped bodies. Collecting ducts were positive for alpha2,6-linked sialic acid, whereas alpha2,3-linked sialic acid was restricted to their ampullae. Although positive in embryonic kidney, S1 and S2 of proximal tubules became unreactive for alpha2,3-linked sialic acid in postnatal and adult kidneys. In adult kidney, intercalated but not principal cells of collecting ducts were reactive for alpha2,3-linked sialic acid. In contrast, alpha2,6-linked sialic acids were detected in all cells of adult kidney nephron. Blot analysis revealed a different but steady pattern of bands reactive for alpha2,6- and alpha2,3-linked sialic acid in embryonic, postnatal, and adult kidney. Activity of alpha2,6 and alpha2,3 sialyltransferases was highest in embryonic kidney and decreased over postnatal to adult kidney with the activity of alpha2,6 sialyltransferase always being three to fourfold that of alpha2,3 sialyltransferase. Thus, alpha2,6- and alpha2,3-linked sialic acids are differently expressed in embryonic anlagen and mesenchyme-derived early stages of nephron and show regional and cell type-specific differences in adult kidney.