Localization of soluble endogenous lectins and their ligands at specific extracellular sites.

Soluble lectins of chicken, rat, frog, and the cellular slime mold, Dictyostelium discoideum, were purified and specific antibodies raised against these proteins were used to immunohistochemically localize the lectins in and around the tissues in which they were synthesized. Within cells, some of these soluble lectins (chicken-lactose-lectin-II in intestinal goblet cells, discoidin II in prespore cells) appear to be concentrated within vesicles whereas others (e.g., rat beta-galactoside lectin in pulmonary alveolar and smooth muscle cells) appear to be free in the cytoplasm. All of these lectins are eventually secreted to extracellular sites in developing or adult tissues. The sites include mucin (chicken-lactose-lectin-II in intestine); developing extracellular matrix (chicken-lactose-lectin-I in muscle; Xenopus laevis lectin in blastula stage embryos); slime (discoidin I); developing spore coat (discoidin II); and a specialized extracellular matrix, elastic fibers (rat beta-galactoside lectin in lung). In cases where this has been studied in detail (discoidin I, discoidin II, and chicken-lactose-lectin-II), the lectin is associated with a complementary extracellular ligand, at least transiently. Lectin-ligand interactions presumably confer specialized properties in these particular extracellular domains.

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