The binding of D-glucosyl-neoglycoproteins and D-galactose-terminated glycoproteins to the hepatic asialoglycoprotein receptor of rabbit liver membranes were characterized and compared. The binding of both types of glycoproteins showed the same dependence on calcium concentration, sensitivity to neuraminidase, and degree of inhibition by various carbohydrate derivatives. These results, along wi...

creased clearance of the sialic aciddeficient transferrin isoforms (CDT) via the asialoglycoprotein receptor. The underlying mechanism for the increased CDT in our patient might be different from that in viral liver cirrhosis. To explore the etiology of this finding, measurements of neuraminidase and sialyltransferase activity (9 ) and of the sialyltransferase mRNA concentration (10 ) may be us...

increased production of intestinal ALP and the peritoneal dialysis technique, but because the presence of intestinal ALP has also been reported in hemodialysis patients and in patients with advanced liver cirrhosis, there may be other explanations as well. For example, competition for clearance by the asialoglycoprotein receptor of the liver between asialylated intestinal ALP and asialoglycopro...

Virus-like particles with genetically defined envelope proteins were generated from cDNA in order to examine the requirement of Sendai virus haemagglutinin-neuraminidase (HN) protein for particle formation, and the role of fusion protein (F) in receptor binding and membrane fusion. Characterization of particles devoid of HN protein showed that particle formation was unimpaired by the absence of...

The ability of asialo-thyroglobulin to bind the thyroid RHL-1 subunit of the asialoglycoprotein receptor has been investigated. Ligand blot assays show that the recombinant carbohydrate recognition domain of the thyroid RHL-1 subunit specifically interacts with rat desialated thyroglobulin. Moreover, RT-PCR and Western blot assays show that TSH deprivation decreases RHL-1 expression in PC C13 t...

Binding and transport of polymeric Igs (pIgA and IgM) across epithelia is mediated by the polymeric Ig receptor (pIgR), which is expressed on the basolateral surface of secretory epithelial cells. Although an Fc receptor for IgA (FcalphaR) has been identified on myeloid cells and some cultured mesangial cells, the expression of an FcalphaR on epithelial cells has not been described. In this stu...