Modulation of WGA binding sites on marrow sinus endothelium in state of stimulated erythropoiesis: a possible mechanism regulating the rate of cell egress.
To study the regulation of cellular and molecular traffic across the marrow-blood barrier, rat marrow endothelial surface was incubated with ferritin-conjugated concanavalin A, wheat germ agglutinin (WGA), recinus communis agglutinin I, and phytohemagglutinin. Normal animals were compared with those after erythropoietic stimulation (phenylhydrazine-induced hemolysis, phlebotomy). A selective and significant reduction in the density of WGA receptors, but not other lectins was noted congruent to the degree of reticulocytosis. Neuraminidase treatment also reduced WGA binding sites and the surface negative charge as detected by polycationic ferritin (PCF). Thus, the reduction in WGA binding sites, may reflect a decrease in the density of membrane sialic acid, rendering the endothelial surface charge less negative and providing an electrostatic attraction for the negatively charged surface of reticulocytes. The findings may also be explained by an increase in the frequency of WGA-excluding fenestrae in the endothelium. These areas, lacking sialic acid, may provide unstable areas in the membrane suitable for the passage of cells and molecules in both directions. It is concluded that, by modulating the density of sialic acid residues, the endothelium may regulate the traffic of cells and molecules across the marrow-blood barrier.
D000818:Animals; D001665:Binding Sites; D001853:Bone Marrow / Q000378:metabolism* / Q000648:ultrastructure; D001854:Bone Marrow Cells; D004727:Endothelium / Q000378:metabolism / Q000648:ultrastructure; D004920:Erythropoiesis; D005293:Ferritins / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D009439:Neuraminidase / Q000494:pharmacology; D010659:Phenylhydrazines / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D011975:Receptors, Mitogen / Q000378:metabolism*; D012156:Reticulocytes / Q000166:cytology / Q000648:ultrastructure
D037102:Lectins; D010659:Phenylhydrazines; D011975:Receptors, Mitogen; C027503:wheat germ agglutinin receptor; D005293:Ferritins; D009439:Neuraminidase