Light and electron microscope analysis of lectin binding to adult rat liver in situ.

作者：Paul N. McMillan, Ferayorni Ls, Gerhardt Co, Jauregui Ho · 发表于：PubMed · 年份：1984 · 被引用次数：36 · 研究领域：Glycosylation and Glycoproteins Research

A comprehensive mapping of lectin receptors on adult rat liver in situ was performed at light and ultrastructural levels by using 12 biotin-labeled lectins and an avidin-biotin-peroxidase complex. In addition, concanavalin A conjugated directly to peroxidase was utilized to study intracellular membrane glycoconjugates. To achieve optimal preservation of these membrane sugar moieties, several fixatives and fixation procedures were evaluated. A periodate-lysin-paraformaldehyde combination provided the best compromise between preservation of ultrastructural details and lectin-binding reactivity. Hepatocyte cell surfaces reacted intensely with concanavalin A, Lens culinaris agglutinin, and Pisum sativum agglutinin (all specific for alpha-D-mannosyl and alpha-D-glucosyl groups) as well as Ricinus communis agglutinin type I (specific for alpha or beta-D-galactose) and wheat germ agglutinin (specific for neuraminic acid and beta-NAc-glucosaminyl groups). In addition, R. communis agglutinin and wheat germ agglutinin exhibited an extremely strong reactivity for bile canaliculi which surpassed the binding of concanavalin A, L. culinaris agglutinin, and P. sativum to these structures. Phaseolus vulgaris agglutinin (specific for beta-D-galactose-glucosyl-NAc and D-mannosyl groups), which exhibited a moderate binding to hepatocyte plasma membranes, reacted more strongly with the endothelium of sinusoids and portal vessels. Although all six of these lectins plus Bandeiraea simplicifolia st...