Cited by 222Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsCarbohydrate Chemistry and Synthesis

Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase activity.

Open access
Stanley, P, Narasimhan, S, Siminovitch, L, Schachter, H·1975·Proceedings of the National Academy of Sciences

Abstract

Several clones of Chinese hamster ovary cells resistant to the cytotoxicity of the phytohemagglutinin from Phaseolus vulgaris show decreased binding of 125I-labeled phytohemagglutinin and contain decreased levels of a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase (EC 2.4.1.51; UDP-2-acetamido-2-deoxy-D-glucose:glycoprotein 2-acetamido-2-deoxy-D-glucosyltransferase) activity when compared to wild-type cells. The decrease in transferase activity varies from 45% to 96%, depending on the exogenous acceptor used in the enzyme assay. No differences between lectin-resistant and wild-type cells were noted for several other glycosyltransferases. The absence of a particular N-acetylglucosaminyltransferase in the lectin-resistant cells apparently results in defective glycosylation of lectin-binding glycoproteins on the cell surface. A phytohemagglutinin-resistant clone which shows decreased binding of 125I-labeled phytohemagglutinin but does not exhibit the enzyme deficiency has also been isolated.

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Crossref · 10.1073/pnas.72.9.3323

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Authors
Stanley, P., Narasimhan, S., Siminovitch, L., & Schachter, H.
Affiliations
University of Toronto (CA)
Venue
Proceedings of the National Academy of Sciences
Published
1975-09
Volume
72
Issue
9
Pages
3323-3327
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1999841276
Cited by
222
References
24
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 2 · 2018: 6 · 2017: 1 · 2016: 1 · 2015: 4 · 2014: 7 · 2013: 4 · 2012: 2
FWCI
7.02
Type
journal article
Language
en
Open access
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 › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords
phytohemagglutinin, lectin resistance, N-acetylglucosaminyltransferase, UDP-N-acetylglucosamine, cell surface glycosylation, lectin binding, CHO cells, Phaseolus vulgaris, glycosyltransferase deficiency, cell surface glycoproteins
MeSH terms
Binding Sites, Cell Line, Cell Survival, Cells, Cultured, Glucosyltransferases, Kinetics, Mutation, Lectins

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