The role of sialated glycoproteins in endocytosis, permeability and transmural passage in the myeloid endothelium.
Changes in the anionic charge distribution at the luminal face of the endothelium of the sinusoids of the bone marrow have been studied at sites of endocytosis by large bristle coated vesicles and at the sites of molecular permeability through diaphragmed fenestrae. The anionic charge distribution has also been studied at the abluminal aspect of these vessels at sites of transmural blood cell passage. Cationic surface markers such as colloidal iron, native ferritin and polycationic ferritin used at low pH, 1.8, and the use of neuraminidase show that the nonmodified endothelial cell surface has exposed sialic acid groups, which are absent at the sites of these functional specializations. Polycationic ferritin binding over a range of pH levels indicates the prsence of another species of anionic materials present at both the nonmodified cell surface and at the sites of the cell surface modifications. This second group of anionic compounds is neuraminidase resistant and has a pKa higher than that of sialic acid (pKa:2.6).
D001665:Binding Sites; D001853:Bone Marrow / Q000378:metabolism; D004705:Endocytosis; D004727:Endothelium / Q000378:metabolism*; D010539:Permeability; D012795:Sialoglycoproteins / Q000502:physiology*; D013194:Staining and Labeling
D012795:Sialoglycoproteins