Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages.
Open accessAbstract
Alveolar macrophages have been shown to bind glycoproteins and synthetic glycoconjugates (neoglycorpoteins) 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, beta-glucuronidase, and RNase B as ligands. Various glycoproteins have been shown to be effective inhibitors of ligand binding including horseradish peroxidase, agalacto-orosomucoid, beta-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.
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- Authors
- Stahl, P. D., Rodman, J. S., Miller, M. J., & Schlesinger, P. H.
- Affiliations
- Washington University in St. Louis (US)
- ORCID
- Schlesinger, P H
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1978-03
- Volume
- 75
- Issue
- 3
- Pages
- 1399-1403
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC411479
- OpenAlex
- W1978105709
- Cited by
- 590
- References
- 24
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 4 · 2023: 2 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 7 · 2016: 4 · 2015: 10 · 2014: 6 · 2013: 3 · 2012: 10
- FWCI
- 15.57
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- alveolar macrophages, CD206, cell surface receptors, glycoprotein binding, glycoconjugates, lysosomal glycosidases, mannose, N-acetylglucosamine, glucose, yeast mannan, trypsin sensitivity, binding inhibition, beta-glucuronidase, RNase B, horseradish peroxidase, ovalbumin, mannose-binding lectin
- MeSH terms
- Animals, Female, Glucose, Glucuronidase, Glycoproteins, Ligands, Macrophages, Mannans, Mannose, Orosomucoid, Pulmonary Alveoli, Receptors, Drug, Ribonucleases, Structure-Activity Relationship, Rats
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