title: Differences in the lectin-binding patterns of the periportal and perivenous endothelial domains in the liver sinusoids.
abstract: We have studied the distribution patterns of carbohydrate terminals on the endothelial surface of the mouse liver microvasculature. For this purpose, a wide battery of FITC lectins specific to glucose, mannose, galactose, fucose, N-acetyl-neuraminic acid, N-acetyl-galactosamine and N-acetyl-glucosamine residues were incubated on liver cryostat sections or intraportally perfused under physiological conditions. All the resulting hepatic sections were examined under fluorescent microscopy and confocal laser scanning microscopy. With the exception of N-acetyl-galactosamine- and fucose-binding lectins, all the perfused lectins specifically bound to the microvascular wall as confirmed by blocking methods using their corresponding sugars. A wide range of binding was, however, observed among the lectins, and the latter were classified into four groups according to their affinities for the different segments of the hepatic microvasculature: (a) equal affinity for all segments (concanavalin A); (b) different affinities depending on acinar zone (wheat germ agglutinin, Ricinus communis toxin, phytohemagglutinin E, Erythrina cristagalli agglutinin and Pisum sativum agglutinin); (c) preferential binding to the sinusoidal network (Lathyrus odoratus, phytohemagglutinin); and (d) lectins that fail to bind to the hepatic microvasculature (N-acetyl-galactosamine- and fucose-binding lectins). Sinusoidal segment walls in acinar zone 1 expressed a higher concentration of certain lectin-binding carbohydrate residues (N-acetyl-neuraminic acid, N-acetyl-galactosamine, galactose, mannose and glucose) than in acinar zone 3. The labeling patterns obtained through the incubation of liver sections or through in vivo perfusion with the different lectins did not always coincide. Only concanavalin A, wheat germ agglutinin and phytohemagglutinin E lectins proved to be concordant (i.e., they produced identical labeling patterns in both procedures).(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Cell Biology and Morphological Sciences, School of Medicine and Dentistry, University of the Basque Country, Leioa, Vizcaya, Spain.
authors.forename: E
authors.initials: E
authors.lastname: Barberá-Guillem
authors.forename: M
authors.initials: M
authors.lastname: Rocha
authors.forename: A
authors.initials: A
authors.lastname: Alvarez
authors.forename: F
authors.initials: F
authors.lastname: Vidal-Vanaclocha
mesh_terms: D000818:Animals; D001665:Binding Sites; D002469:Cell Separation; D004730:Endothelium, Vascular / Q000166:cytology / Q000378:metabolism*; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D005456:Fluorescent Dyes; D005470:Fluorometry; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism*; D008102:Liver Circulation; D051379:Mice; D008815:Mice, Inbred Strains; D008833:Microcirculation; D013861:Thiocyanates; D014680:Veins / Q000378:metabolism; D014909:Wheat Germ Agglutinins
chemical_list: D005452:Fluoresceins; D005456:Fluorescent Dyes; D037102:Lectins; D013861:Thiocyanates; D014909:Wheat Germ Agglutinins; D016650:Fluorescein-5-isothiocyanate