Mechanism of binding and uptake of sialidase-treated blood cells and glycoproteins by the galactose-specific receptor of rat peritoneal macrophages.
Sialidase-treated rat erythrocytes, lymphocytes and thrombocytes bind to homologous peritoneal macrophages via demasked, terminal galactose residues on the blood cells and a galactose-specific receptor on macrophages. While erythrocytes and thrombocytes are phagocytosed after binding, vital lymphocytes are released from the phagocytes after several hours of incubation, because their surface sialic acids are resynthesized. Asialoglycoprotein-coated gold-particles are also bound, and the pathway of their internalization and recycling of the receptor was studied using various inhibitors of endocytosis. Sialidase treatment of macrophages abolished their binding capacity.
Schauer
R
R
Biochemisches Institut, Christian-Albrechts-Universität, Kiel, F.R. Germany.
Fischer
C
C
Kluge
A
A
Lee
H
H
Ruch
B
B
D000818:Animals; D001792:Blood Platelets / Q000378:metabolism; D004912:Erythrocytes / Q000201:enzymology*; D006023:Glycoproteins / Q000378:metabolism*; D008214:Lymphocytes / Q000378:metabolism; D008264:Macrophages / Q000378:metabolism*; D009439:Neuraminidase / Q000378:metabolism*; D010529:Peritoneal Cavity; D051381:Rats; D011956:Receptors, Cell Surface / Q000502:physiology*
D006023:Glycoproteins; D011956:Receptors, Cell Surface; C039707:galactose receptor; D009439:Neuraminidase