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Cited by 224Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsCarbohydrate Chemistry and Synthesis

The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.

Deficient uridine diphosphate-N-acetylglucosamine:glycoprotein N-acetylglucosaminyltransferase activity in a clone of Chinese hamster ovary cells with altered surface glycoproteins

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Gottlieb, C, Baenziger, J, Kornfeld, S·1975·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)41514-7
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Abstract

We have reported the isolation of a clone (termed 15B) of Chinese hamster ovary (CHO) cells which are deficient in certain plant lectin-binding sites and have decreased amounts of sialic acid, galactose, and N-acetylglucosamine in its membranes (Gottlieb et al. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 1078-1082). This study demonstrates that extracts of 15B cells, in contrast to the parent cell line, do not transfer N-acetylglucosamine residues from UDP-GlcNAc to certain glycopeptide and glycoprotein acceptors containing terminal nonreducing alpha-linked mannose residues. The decreased enzyme activity could not be accounted for by the presence of inhibitors, altered pH, or Mn2+ requirements of the glycosyltransferase or increased N-acetylglucosaminidase activity in the extracts. The finding that the 15B cell extracts have significant but reduced N-acetylglucosaminyltransferase activity toward a degraded orosomucoid acceptor suggests that these cells have a selective loss of one of several specific N-acetylglucosaminyltransferases which are present in the parent CHO cells. The sialyl- and galactosyltransferase activities of 15B and parent CHO cells are comparable. Parent CHO and 15B cells were grown in radioactive glucosamine to label the membrane glycoproteins. Solubilization of these glycoproteins and passage over a Ricinus communis agglutinin I (RCA I) Sepharose affinity column revealed that no labeled 15B glycoprotein material bound, whereas 50 percent of the CHO membrane glycoproteins bound and could be eluted with the haptene lactose, demonstrating that 15B cells are virtually devoid of membrane oligosacharides capable of binding to the RCA I lectin. The 15B membrane glycoproteins exhibited a marked shift toward glycoprotein species of lower molecular weight when examined by gel electrophoresis in sodium dodecyl sulfate. It is proposed that this shift in the mobility of the 15B membrane glycoproteins results from a decreased glycosylation of a number of membrane glycoproteins relative to their counterparts in CHO cells. The deficient N-acetylglucosaminyltransferase activity in 15B cells can account for the decreased glycosylation of the 15B cell membrane glycoproteins.

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Crossref · 10.1016/s0021-9258(19)41514-7

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Research works printed but not linked: 2

  1. Adair, 1974, J. Biol. Cuem., 249, 4696
  2. Stewart, 1973, J. Reticuloendothel. Soc., 14, 332

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Metadata

Authors
Gottlieb, C., Baenziger, J., & Kornfeld, S.
Affiliations
Washington University in St. Louis (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1975-05
Volume
250
Issue
9
Pages
3303-3309
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)41514-7
OpenAlex
W1552293911
Cited by
224
References
25
Citations by year
2021: 1 · 2018: 2 · 2016: 2 · 2014: 5 · 2013: 2 · 2012: 2
FWCI
7.80
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • 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
CHO cells, membrane glycoproteins, glycosylation, sialic acid, oligosaccharide structure, sialyltransferase, galactosyltransferase, alpha-1-acid glycoprotein
MeSH terms
Cell Membrane, Chromatography, Affinity, Clone Cells, Female, Galactose, Glycopeptides, Glycoproteins, Hexosyltransferases, Orosomucoid, Ovary, Sepharose, Uridine Diphosphate N-Acetylglucosamine, Uridine Diphosphate Sugars, Lectins

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