The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver non-parenchymal cells. Studies with β-glucuronidase, N-acetyl-β-d-glucosaminidase, ribonuclease B and agalacto-orosomucoid
Open accessAbstract
Glycoproteins having mannose and/or N-acetylglucosamine in the terminal non-reducing position [Stockert, Morell & Scheinberg (1976) Biochem. Biophys. Res. Commun. 68, 988–993], and various lysosomal enzymes [Stahl, Schlesinger, Rodman & Doebber (1976) Nature (London) 264, 86–8] are rapidly cleared from plasma by the liver after intravenous administration. A liver cell-separation technique was used to determine the cellular localization of 125I-labelled beta-glucuronidase, ribonuclease B, agalacto-orosomucoid and asialo-orosomucoid. On a specific readioactivity basis, all ligands except 125I-labelled asialo-orosomucoid were enriched in the non-parenchymal cell fraction. Isolated cells, fixed and stained for beta-glucuronidase or N-acetyl-beta-D-glucosaminidase activity after intravenous injection of the enzymes, showed enrichment in the non-parenchymal cell fraction (probably Kupffer cells). After uptake by the non-parenchymal cells, liver lysosomal beta-glucuronidase and N-acetyl-beta-D-glucosaminidase showed degradation half-times of 2.2 and 0.4 days respectively.
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Metadata
- Authors
- Schlesinger, P. H., Doebber, T. W., Mandell, B. F., White, R., DeSchryver, C., Rodman, J. S., Miller, M. J., & Stahl, P.
- Affiliations
- University of Namur (BE)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1978-10-15
- Volume
- 176
- Issue
- 1
- Pages
- 103-109
- ISSN
- 0264-6021 (ISSN-L)
- PMC
- PMC1186209
- OpenAlex
- W1717442359
- Cited by
- 209
- References
- 33
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 1 · 2014: 2 · 2012: 1
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- plasma clearance, Kupffer cells, mannose, N-acetylglucosamine, glycoproteins, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, ribonuclease B, lysosomal enzymes, enzyme degradation, liver
- MeSH terms
- Acetylglucosamine, Acetylglucosaminidase, Animals, Female, Glucuronidase, Glycoproteins, Ligands, Liver, Lysosomes, Mannose, Orosomucoid, Ribonucleases, Rats
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