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

Gottlieb, C; Baenziger, J; Kornfeld, S

doi:10.1016/s0021-9258(19)41514-7

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

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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Authors: Gottlieb, C., Baenziger, J., & Kornfeld, S.
Affiliations: Washington University in St. Louis (US)
ORCID: Baenziger, J
Kornfeld, S
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: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 16590 d)
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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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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