The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Isolation of wheat germ agglutinin-resistant clones of Chinese hamster ovary cells deficient in membrane sialic acid and galactose
Open accessAbstract
Several clones of Chinese hamster ovary cells have been selected for their resistance to the toxic effects of wheat germ agglutinin. The clones do not bind wheat germ agglutinin as well as parent cells and are 5- to 250-fold more resistant to the toxic effects of the lectin. Of three clones studied in detail, all exhibit a decrease in wheat germ agglutinin binding affinity. Two have normal numbers of wheat germ agglutinin binding sites, while one (Clone 13) has a 65% decrease in binding sites. Crude membrane preparations of the clones have a decrease in sialic acid content relative to parent cells, and Clone 13 membranes are also deficient in galactose, while the mannose and hexosamine contents of all three clones are normal. The membrane sugar deficiencies affect both glycoproteins and glycolipids. Sialyl-lactosylceramide is the major glycolipid in parent cells, while Clones 1 and 1021 have lactosylceramide and Clone 13 has glucosylceramide as the predominant glycolipid. Labeling experiments with N-[G-3H]acetylmannosamine suggest that Clone 1021 cells have a block in the transfer of sialic acid from CMP-sialic acid to glycoprotein and glycolipid acceptors. Yet CMP-sialic acid:glycoprotein sialyl-transferase activity in cell lysates of Clone 1021 cells is 80% of normal. While CMP-sialic acid:lactosylceramide sialyl-transferase activity is only 25% of normal, it can be restored to normal or elevated levels by sodium butyrate induction without an associated increase in cellular sialyl-lactosylceramide content. Similarly, the galactose-deficient Clone 13 can synthesize UDP-galactose and has normal levels of UDP-galactose:glycoprotein galactosyltransferase and UDP-galactose:glucosylceramide galactosyltransferase when assayed in vitro. The glycosyltransferases of both these clones can utilize their own glycoproteins as sugar acceptors in in vitro assays. These data suggest that the variant cells fail to carry out specific glycosyltransferase reactions in vivo despite the fact that they possess the appropriate nucleotide sugars, glycoprotein and glycolipid acceptors, and glycosyltransferases.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,724
The Thiobarbituric Acid Assay of Sialic Acids
Warren, L. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69851-5 · Cited by 6,443
[10] Assay of inorganic phosphate, total phosphate and phosphatases
Ames, B. N. (1966) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(66)08014-5 · Cited by 3,338
A MODIFIED COLORIMETRIC METHOD FOR THE ESTIMATION OF N-ACETYLAMINO SUGARS
Reissig, J. L., Strominger, J. L., & Leloir, L. F. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65959-9 · Cited by 2,592
Handbook of Experimental Immunology.
Denman, A. (1968) · Annals of Internal Medicine · doi:10.7326/0003-4819-68-6-1376_1 · Cited by 2,414
Roseman, S. (1970) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(70)90024-1 · Cited by 1,210
The Use of Sephadex for the Removal of Nonlipid Contaminants from Lipid Extracts*
Wells, M. A., & Dittmer, J. C. (1963) · Biochemistry · doi:10.1021/bi00906a015 · Cited by 419
HAKOMORI, S. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(75)90008-6 · Cited by 383
The Structure of a Phytohemagglutinin Receptor Site from Human Erythrocytes
Kornfeld, R., & Kornfeld, S. A. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63104-7 · Cited by 348
Stanley, P., Caillibot, V., & Siminovitch, L. (1975) · Cell · doi:10.1016/0092-8674(75)90002-1 · Cited by 266
Adair, W. L., & Kornfeld, S. A. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42376-4 · Cited by 260
Studies on the Glycosidases in Jack Bean Meal
Li, Y. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99383-x · Cited by 257
The Structure of the Glycopeptide of Human γG Myeloma Proteins
Kornfeld, R., Keller, J., Baenziger, J., & Kornfeld, S. A. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62222-7 · Cited by 246
Interaction of wheat germ agglutinin and concanavalin A with isolated fat cells
Cuatrecasas, P. (1973) · Biochemistry · doi:10.1021/bi00731a011 · Cited by 234
Gottlieb, C., Baenziger, J., & Kornfeld, S. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41514-7 · Cited by 224
Stanley, P., Narasimhan, S., Siminovitch, L., & Schachter, H. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3323 · Cited by 222
Characterization of the Cell Surface Receptor for the Agaricus bisporus Hemagglutinin
Presant, C. A., & Kornfeld, S. A. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44676-0 · Cited by 166
Studies on the Monosaccharide Sequence of the Serum Glycoprotein Fetuin
Spiro, R. G. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60349-7 · Cited by 154
[44] Soy bean (Glycine max) agglutinin
Lis, H., & Sharon, N. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(72)28046-6 · Cited by 128
The Nature of the Cell Surface Receptor Site for Lens culinaris Phytohemagglutinin
Kornfeld, S. A., ROGERS, J. C., & Gregory, W. T. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34153-5 · Cited by 126
Isolation of a Clone of Chinese Hamster Ovary Cells Deficient in Plant Lectin-Binding Sites
Gottlieb, C., Skinner, S. A. M., & Kornfeld, S. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1078 · Cited by 117
Simmons, J. L., Fishman, P. H., Freese, E., & Brady, R. O. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.66.2.414 · Cited by 107
Ricin resistance in baby hamster kidney cells
Meager, A., UNGKITCHANUKIT, A., NAIRN, R., & Hughes, R. C. (1975) · Nature · doi:10.1038/257137a0 · Cited by 97
ENZYMATIC SYNTHESIS OF SIALIC ACID 9-PHOSPHATES
Roseman, S., Jourdian, G. W., Watson, D., & Rood, R. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.7.958 · Cited by 89
Arce, A., Maccioni, H. J. F., & Caputto, R. (1971) · Biochemical Journal · doi:10.1042/bj1210483 · Cited by 88
Isolation and characterization of two mouse L cell lines resistant to the toxic lectin ricin
Gottlieb, C., & Kornfeld, S. A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)56999-x · Cited by 71
[42] Wheat germ (Triticum vulgaris) agglutinin
Marchesi, V. T. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(72)28044-2 · Cited by 57
The biosynthesis of N-acetylneuraminic acid
Warren, L., & Felsenfeld, H. (1961) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(61)90277-7 · Cited by 52
[31] CMP-sialic acid synthetase (cytidine-5′-monophospho-sialic acid synthetase)
Kean, E. L., & Roseman, S. (1966) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(66)08035-2 · Cited by 51
Determination of molecular weigthof glycopeptides by exclusion chromatography
Bhatti, T., & Clamp, J. R. (1968) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(68)90176-1 · Cited by 50
Greene, W. C., Parker, C. M., & Parker, C. W. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33350-1 · Cited by 49
Warren, L., & Felsenfeld, H. (1961) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(61)90107-3 · Cited by 48
Lectin receptors on the cell surface membrane and the kinetics of lectin-induced cell agglutination
Vlodavsky, I., & Sachs, L. (1975) · Experimental Cell Research · doi:10.1016/0014-4827(75)90429-2 · Cited by 45
Juliano, R. L., & Stanley, P. (1975) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(75)90332-6 · Cited by 43
Structure of two urinary oligosaccharides characteristic of blood group O(H)- and B-secretors
Björndal, H., & Lundblad, A. (1970) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(70)90162-5 · Cited by 36
Smith, W., Nakajima, T., & Ballou, C. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41533-0 · Cited by 34
Localization of enzymes in specialized regions of the microsomal membrane
Winqvist, L., & Dallner, G. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90203-0 · Cited by 23
Research works printed but not linked: 6
- Briles, 1976, Fed. Proc., 35, 1642
- Stewart, 1973, J. Reticuloendothel. Soc., 14, 332
- Hakomori, 1964, J. Biochem. (Tokyo), 55, 205
- Hakomori, 1975, Biochim. Biophys. Acta, 417, 55
- Schächter, 1974, Biochem. Soc. Symp., 40, 57
- Isselbacher, 1972, Proc. Natl. Acad. Sci. U.S.A., 55, 134
Cited by
Sorted by citations
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid.
BHAVANANDAN, V. P., & Katlic, A. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50686-4 · Cited by 597
Compartmental organization of the golgi stack
Dunphy, W. G., & Rothman, J. E. (1985) · Cell · doi:10.1016/s0092-8674(85)80097-0 · Cited by 446
Li, E., Tabas, I., & Kornfeld, S. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34435-6 · Cited by 421
Self-citationHirschberg, C. B., Robbins, P. W., & Abeijón, C. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.49 · Cited by 385
Metadata
- Authors
- Briles, E. B., Li, E., & Kornfeld, S.
- Affiliations
- Washington University in St. Louis (US)
- ORCID
- Kornfeld, S
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1977-02
- Volume
- 252
- Issue
- 3
- Pages
- 1107-1116
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1518753545
- Cited by
- 220
- References
- 38
- Citations by year
- 2022: 1 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 5 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 2
- FWCI
- 5.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- 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
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Keywords
- wheat germ agglutinin, lectin resistance, CHO cells, sialic acid deficiency, galactose deficiency, membrane glycosylation, sialyltransferase, galactosyltransferase, lactosylceramide, glucosylceramide, glycolipids, glycoproteins, CMP-sialic acid, UDP-galactose, sodium butyrate, lectin affinity, cell surface
- MeSH terms
- Carbohydrates, Cell Line, Cell Membrane, Cell Separation, Clone Cells, Drug Resistance, Galactose, Galactosyltransferases, Glycolipids, Glycopeptides, Kinetics, Microscopy, Phase-Contrast, Sialic Acids, Sialyltransferases, Species Specificity, Transferases, Lectins
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