Cited by 209Glycosylation and Glycoproteins ResearchLiver physiology and pathologyCellular transport and secretion

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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

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Schlesinger, P H, Doebber, T W, Mandell, B F, White, R, DeSchryver, C, Rodman, J S, Miller, M J, Stahl, P·1978·Biochemical Journal

DOI 10.1042/bj1760103PMC PMC1186209

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Abstract

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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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)
ORCID: Schlesinger, P H
Mandell, B F
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1978-10-15
Volume: 176
Issue: 1
Pages: 103-109
ISSN: 0264-6021 (ISSN-L)
DOI: 10.1042/bj1760103
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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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

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