Nonrandom distribution of sialic acid over the cell surface of bristle-coated endocytic vesicles of the sinusoidal endothelium cells.
Previous studies with protein tracers have shown that the luminal surface of the vascular endothelium of the bone marrow is endocytic. The endocytosis occurs through the formation of large bristle-coated vesicles (LCV). The anionic charge distribution in this process was examined at the luminal surface of the endothelial cell, At pH 1.8, colloidal iron (CI), native ferritin, and polycationic ferritin (PCF) are bound by the luminal surface of the endothelial cell, but not at the sites of LCV formation. PCF used over a pH range of 1.8--7.2 (CI is unstable at higher pH levels) revealed LCV binding of this agent in increasing manner from pH 3.5 upwards. PCF binding at low pH (1.8) at the endothelial cell surface was markedly reduced by neuraminidase. Neuraminidase did not reduce PCF binding by the endothelial cell surface nor by the LCV at higher pH levels. It is concluded that the luminal surface of the endothelial cell has exposed sialic acid groups which are absent or significantly diminished at endocytic sites. The free surface of the endothelial cells as well as the sites of endocytosis have, in addition, anionic material with a pKa higher than that of sialic acid (pKa 2.6). These anionic materials may be different at the sites of endocytosis as compared to those present at the free cell surface.
D000818:Animals; D001665:Binding Sites; D001853:Bone Marrow / Q000098:blood supply*; D002196:Capillaries / Q000648:ultrastructure*; D002462:Cell Membrane / Q000032:analysis; D003102:Colloids; D004705:Endocytosis; D004727:Endothelium / Q000378:metabolism / Q000648:ultrastructure; D005293:Ferritins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism; D008297:Male; D009439:Neuraminidase / Q000494:pharmacology; D051381:Rats; D012794:Sialic Acids / Q000032:analysis*
D003102:Colloids; D012794:Sialic Acids; D005293:Ferritins; D007501:Iron; D009439:Neuraminidase