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

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 access

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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1042/bj1760103

Cites

33 of 33 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay
Bolton, A. E., & Hunter, W. M. (1973) · Biochemical Journal · doi:10.1042/bj1330529 · Cited by 3,240
Functions of Lysosomes
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
Antigen-antibody crossed electrophoresis
Laurell, C. ‐. (1965) · Analytical Biochemistry · doi:10.1016/0003-2697(65)90278-2 · Cited by 1,420
The Role of Surface Carbohydrates in the Hepatic Recognition and Transport of Circulating Glycoproteins
Ashwell, G., & Morell, A. G. (1974) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122860.ch3 · Cited by 1,212
Distribution of organelles and membranes between hepatocytes and nonhepatocytes in the rat liver parenchyma. A stereological study.
Blouin, A., Bolender, R. P., & Weibel, E. R. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.72.2.441 · Cited by 879
Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages.
Stahl, P. D., Rodman, J. S., Miller, M. J., & Schlesinger, P. H. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.3.1399 · Cited by 590
Self-citation
Human cathepsin B1. Purification and some properties of the enzyme
Barrett, A. J. (1973) · Biochemical Journal · doi:10.1042/bj1310809 · Cited by 324
Mass isolation and culture of rat kupffer cells.
Munthe‐Kaas, A. C., Berg, T., Seglen, P. O., & Seljelid, R. (1975) · The Journal of Experimental Medicine · doi:10.1084/jem.141.1.1 · Cited by 212
Receptors for Immunoglobulin and Complement on Human Alveolar Macrophages
Reynolds, H. Y., Atkinson, J. P., Newball, H. H., & Frank, M. M. (1975) · The Journal of Immunology · doi:10.4049/jimmunol.114.6.1813 · Cited by 201
The Isolation of Ribonuclease B, a Glycoprotein, from Bovine Pancreatic Juice
Plummer, T. H., Hirs, C. H. W., & Tench, A. L. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81195-4 · Cited by 167

Flagged first, then by citations

Show all 33 references

Sorted by citations

Biological roles of glycans
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“was established, and evidence then emerged for a mannose receptor on macrophages (251, 252) and possibly”
Background
Receptor-mediated pinocytosis of mannose glycoconjugates by macrophages: Characterization and evidence for receptor recycling
Stahl, P. D., Schlesinger, P. H., Sigardson, E., Rodman, J. S., & Lee, Y. C. (1980) · Cell · doi:10.1016/0092-8674(80)90402-x · Cited by 569
Self-citation
Glycosylation of Therapeutic Proteins
Solá, R. J., & Griebenow, K. H. (2010) · BioDrugs · doi:10.2165/11530550-000000000-00000 · Cited by 443
Clearance and binding of two electrophoretic “fast” forms of human alpha 2-macroglobulin.
Imber, M. J., & Pizzo, S. V. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43398-4 · Cited by 398
Scavenger functions of the liver endothelial cell
Smedsrød, B. H., Pertoft, H., Gustafson, S., & Laurent, T. C. (1990) · Biochemical Journal · doi:10.1042/bj2660313 · Cited by 328

See all 209

Human β-glucuronidase: In vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells
Achord, D. T., Brot, F. E., Bell, C. E., & Sly, W. S. (1978) · Cell · doi:10.1016/0092-8674(78)90102-2 · Cited by 226
Clearance of lysosomal hydrolases following intravenous infusion
Schlesinger, P. H., Rodman, J. S., Frey, M. J., Lang, S., & Stahl, P. D. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90472-0 · Cited by 54
The effect of α-mannose-terminal oligosaccharides on the survival of glycoproteins in the circulation
Brown, T. L., Henderson, L. A., Thorpe, S. R., & Baynes, J. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(78)80026-5 · Cited by 56
Summary
Cells, S. O. R., Achord, D. T., Brot, F. E., Bell, C. E., & Sly*tf, W. S. (2015)
The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine
Schlesinger, P. H., Rodman, J. S., Doebber, T. W., Stahl, P. D., Lee, Y. C., Stowell, C. P., & Kuhlenschmidt, T. B. (1980) · Biochemical Journal · doi:10.1042/bj1920597 · Cited by 83
Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation
Furbish, F. S., Steer, C. J., Krett, N. L., & Barranger, J. A. (1981) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(81)90474-8 · Cited by 186
Mannose Binding Proteins in the Liver and Blood
Summerfield, J. A. (1986) · Springer eBooks · doi:10.1007/978-1-4684-5185-6_1 · Cited by 1
Endocytosis of lysosomal enzymes by non-parenchymal rat liver cells. Comparative study of lysosomal-enzyme uptake by hepatocytes and non-parenchymal liver cells
Ullrich, K., Gieselmann, V., Mersmann, G., & FIGURA, K. V. (1979) · Biochemical Journal · doi:10.1042/bj1820329 · Cited by 32
Evidence for specific recognition sites mediating clearance of lysosomal enzymes in vivo.
Stahl, P. D., Six, H. R., Rodman, J. S., Schlesinger, P. H., Tulsiani, D. R. P., & Touster, O. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.11.4045 · Cited by 101
Rat liver endothelial cells have a greater capacity than kupffer cells to endocytose N -acetylglucosamine- and mannose-terminated glycoproteins
Dalen, D. P. P.-V., Leeuw, M. A. D., Brouwer, A., & Knook, D. L. (1987) · Hepatology · doi:10.1002/hep.1840070410 · Cited by 60

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Citations

Cites

Cited by

Related

Metadata

Record

About these checks