Differentiated microdomains on the luminal surface of the capillary endothelium. II. Partial characterization of their anionic sites.
To investigate the chemical nature of the cationic ferritin (CF)-binding sites of the differentiated microdomains of the capillary endothelium, the vasculature of the mouse pancreas and intestinal mucosa was perfused in situ with neuraminidase, hyaluronidase, chondroitinase ABC, heparinase, and three proteases: trypsin, papain, and pronase. Proteases of broad specificity removed all anionic sites, suggesting that the latter are contributed by acid glycoproteins or proteoglycans. Neuraminidase, hyaluronidase, and chondroitinase ABC reduced the density of CF-binding sites on the plasmalemma proper, but had no effect on either coated pits or fenestral diaphragms. Heparinase removed CF-binding sites from fenestral diaphragms and had no effect on coated pits. Taken together, these results indicate that the anionic sites of the fenestral diaphragms are contributed primarily by heparan sulfate and/or heparin, whereas those of the plasmalemma proper are of mixed chemical nature. The membranes and diaphragms of plasmalemmal vesicles and transendothelial channels do not bind CF in control specimens; this condition is not affected by the enzymic treatments mentioned above.
D000818:Animals; D000838:Anions / Q000378:metabolism*; D001665:Binding Sites; D002196:Capillaries / Q000032:analysis* / Q000648:ultrastructure; D002412:Cations; D002462:Cell Membrane / Q000032:analysis; D004727:Endothelium / Q000032:analysis / Q000648:ultrastructure; D005293:Ferritins / Q000378:metabolism; D006025:Glycosaminoglycans / Q000032:analysis*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006493:Heparin / Q000032:analysis*; D006497:Heparan Sulfate / Q000032:analysis*; D008297:Male; D051379:Mice; D010447:Peptide Hydrolases / Q000494:pharmacology
D000838:Anions; D002412:Cations; D005293:Ferritins; D006025:Glycosaminoglycans; D006026:Glycoside Hydrolases; D006493:Heparin; D006497:Heparan Sulfate; D010447:Peptide Hydrolases