Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages

P. D. Stahl, J. S. Rodman, M. J. Miller, P. H. Schlesinger

Research output: Contribution to journalArticle

436 Scopus citations

Abstract

Alveolar macrophages have been shown to bind glycoproteins and synthetic glycoconjugates (neoglycoproteins) that have mannose, N-acetylglucosamine, or glucose in the exposed, nonreducing position. Galactose-terminal glycoproteins are not bound. Binding of radiolabeled ligands to cells is nearly completely impaired by the presence of an excess of yeast mannan. Binding is temperature sensitive and proceeds optimally at pH 7.0. Prior treatment of the cells with trypsin severely decreases their capacity to bind ligands. An inhibition assay has been developed, using radioiodinated glucose-albumin conjugate, agalacto-orosomucoid, β-glucuronidase, and RNase B as ligands. Various glycoproteins have been shown to be effective inhibitors of ligand binding, including horseradish peroxidase, agalacto-orosomucoid, β-glucuronidase, ovalbumin, agalacto-fetuin, and RNase B. RNase A and asialo-fetuin are ineffective as antagonists. The results suggest the presence of a cell surface receptor on alveolar macrophages that binds glycoproteins having terminal sugars with the mannose or glucose configuration.

Original languageEnglish
Pages (from-to)1399-1403
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume75
Issue number3
DOIs
StatePublished - Jan 1 1978

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