Cited by 117Glycosylation and Glycoproteins ResearchToxin Mechanisms and ImmunotoxinsGalectins and Cancer Biology

Isolation of a Clone of Chinese Hamster Ovary Cells Deficient in Plant Lectin-Binding Sites

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Gottlieb, Charlene, Skinner, Sister Ann Marie, Kornfeld, Stuart·1974·Proceedings of the National Academy of Sciences

Abstract

Ricin, a galactose-binding lectin with potent cytotoxic activity, was used to select a clone of Chinese hamster ovary cells with altered plant lectin-binding properties. The clone (15B) is 80-fold less sensitive to the toxic action of ricin than the parent line. In the absence of ricin, it grows both in monolayer and suspension culture with a normal generation time. Plating efficiency, however, is significantly reduced. Relative to the parent cells, its binding of the Ricinus communis lectins, Phaseolus vulgaris erythroagglutinating phytohemagglutinin, Abrus precatorius phytohemagglutinin, and soybean phytohemagglutinin is less than 7%, while binding of lentil phytohemagglutinin, wheat-germ agglutinin, and mushroom phytohemagglutinin is 17%, 40%, and 109%, respectively. In contrast, its concanavalin A binding is increased by 70%. Consistent with these alterations, crude membrane preparations of the 15B cells were found to contain the same sugars as the parent-cell membranes but in different proportions. The 15B membranes have 28% less sialic acid, 38% less N -acetylglucosamine, 49% less galactose, the same amount of N -acetylgalactosamine, and 53% more mannose than the membranes of the parent cells.

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Crossref · 10.1073/pnas.71.4.1078

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Authors
Gottlieb, C., Skinner, S. A. M., & Kornfeld, S.
Affiliations
Washington University in St. Louis (US)
Venue
Proceedings of the National Academy of Sciences
Published
1974-04
Volume
71
Issue
4
Pages
1078-1082
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2011296435
Cited by
117
References
24
Citations by year
2021: 1 · 2018: 2 · 2016: 2 · 2013: 3 · 2012: 2
FWCI
5.11
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
  • Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
Keywords
ricin, CHO cells, galactose-specific lectin, cell surface carbohydrates, membrane glycosylation, sialic acid, N-acetylglucosamine, galactose, mannose, concanavalin A binding, phytohemagglutinin
MeSH terms
Animals, Binding Sites, Binding Sites, Antibody, Cell Membrane, Clone Cells, Female, Cricetinae, Iodine Radioisotopes, Ovary, Ricin, Lectins

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