Cited by 171Viral Infectious Diseases and Gene Expression in InsectsProtein purification and stabilityTransgenic Plants and Applications

The DOI matches its Crossref record; its reference list is not available.

Culture pH Affects Expression Rates and Glycosylation of Recombinant Mouse Placental Lactogen Proteins by Chinese Hamster Ovary (CHO) Cells

Abstract

Glycosylation patterns and specific expression rates of the recombinant protein mouse placental lactogen-I (mPL-I) by Chinese hamster ovary (CHO) cells varied significantly over the extracellular pH (pHe) range of 6.1 to 8.7. The maximum specific mPL-I expression rates occurred between pHe 7.6 and 8.0. The pHe effect on protein expression was confirmed using a different CHO cell expressing the unglycosylated recombinant protein mouse placental lactogen-II (mPL-II). Decreases in the extent of glycosylation of mPL-I were observed at low (below 6.9) and high (above 8.2) pHe values. The pHe dependent variations in mPL-I accumulation in the supernatant as well as in glycosylation patterns were not the result of enzymatic degradation in the culture medium.

Overview

Integrity signals

Registry

Crossref · 10.1038/nbt0693-720

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

No citation lists for this paper

No citation lists for this paper yet — checked again daily.

References 42 · Cited by 171

Research works printed but not linked: 44

  1. Musgrove E., 1987, Exp. cell Res., 172, 65, 10.1016/0014-4827(87)90093-0 · DOI
  2. Fellenz M.P., 1988, Radiat. Res., 116, 305, 10.2307/3577466 · DOI
  3. McQueen A., 1991, Eng., 6, 49
  4. Miller W.M., 1988, Biotechnol. Bioeng., 32, 947, 10.1002/bit.260320803 · DOI
  5. Ozturk S.S., 1991, Biotechnol. Prog., 7, 481, 10.1021/bp00012a002 · DOI
  6. Backman P., 1992, J. cell. Physiol., 150, 99, 10.1002/jcp.1041500114 · DOI
  7. Hakimian J., 1991, J. Membrane Biol., 120, 29, 10.1007/BF01868588 · DOI
  8. 10.1016/0006-2952(91)90322-V · DOI
  9. Freshney, R.I. 1987. Culture of Animal cells: a Manual of Basic Technique, second edition, p. 69. Alan R. Liss, Inc. New York.
  10. Arathoon W.R., 1986, Science, 232, 1390, 10.1126/science.2424083 · DOI
  11. 10.1016/0385-6380(88)90082-9 · DOI
  12. Conradt H.S., 1989, J. Biol. Chem., 264, 17368, 10.1016/S0021-9258(18)71502-0 · DOI
  13. Curling E.M.A., 1990, Biochem. J., 272, 333, 10.1042/bj2720333 · DOI
  14. Gottesman, M.M. 1985. Growth properties of Chinese hamster ovary (CHO) cells, p. 145–147. In: Molecular cell Genetics. Gottesman, M.M. (Ed.). Wiley, New York.
  15. 10.1016/0168-1656(90)90054-F · DOI
  16. Wergeland, L., Wallberg, C. and Ericsson, R. 1987. Hybridoma culture for the continuous production of monoclonal antibodies: fractionalized factorial design experiment for optimization, p. 795. In: Modern Approaches to Animal cell Technology. Spier, R.E. and Griffiths, J.B. (Eds.). Butterworths, Boston. · DOI
  17. 10.1016/0168-1656(90)90053-E · DOI
  18. 10.1016/0141-0229(92)90137-D · DOI
  19. 10.1016/0014-5793(90)80061-M · DOI
  20. England B.K., 1991, Am. J. Physiol., 260, C277, 10.1152/ajpcell.1991.260.2.C277 · DOI
  21. Matlin K.S., 1988, J. Biol. Chem., 263, 11478, 10.1016/S0021-9258(18)37982-1 · DOI
  22. Tapper H., 1990, Biochem. J., 272, 407, 10.1042/bj2720407 · DOI
  23. Wang X., 1990, Acta Endo., 123, 218
  24. Rothman R.J., 1989, Biochem., 28, 1377, 10.1021/bi00429a065 · DOI
  25. Goochee C.F., 1990, Bio/Technology, 8, 421
  26. Goochee C.F., 1991, Bio/Technology, 9, 1347, 10.1038/nbt1291-1347 · DOI
  27. Ogren L., 1988, Int. Rev. Cytol., 112, 1, 10.1016/S0074-7696(08)62005-7 · DOI
  28. Colosi P., 1987, Molec. Endo., 1, 767, 10.1210/mend-1-11-767 · DOI
  29. Colosi P., 1988, Endo., 123, 2662, 10.1210/endo-123-6-2662 · DOI
  30. Kobata A., 1979, Anal. Biochem., 100, 1, 10.1016/0003-2697(79)90102-7 · DOI
  31. Tarentino A.L., 1985, Biochem., 24, 4665, 10.1021/bi00338a028 · DOI
  32. Colosi P., 1987, Endo., 120, 2500, 10.1210/endo-120-6-2500 · DOI
  33. van Erp R., 1991, J. Biotech., 20, 249, 10.1016/0168-1656(91)90298-A · DOI
  34. Markoff E., 1988, Endo., 123, 1303, 10.1210/endo-123-3-1303 · DOI
  35. 10.1016/0303-7207(90)90252-4 · DOI
  36. Cole E.S., 1992, J. cell. Biochem., Keystone Symp., 16D, 154
  37. Eagle H., 1973, J. cell. Physiol., 82, 1, 10.1002/jcp.1040820102 · DOI
  38. Gonzalez-Mendez R., 1988, Magn. Reson. Med., 6, 373, 10.1002/mrm.1910060402 · DOI
  39. Jackson L.L., 1986, Proc. Natl. Acad. Sci. USA, 83, 8496, 10.1073/pnas.83.22.8496 · DOI
  40. Lee S.J., 1988, J. Biol. Chem., 263, 3521, 10.1016/S0021-9258(18)69101-X · DOI
  41. Tanaka T., 1980, J. Clin. Endo. Metab., 51, 1058, 10.1210/jcem-51-5-1058 · DOI
  42. Gout P.W., 1986, Biochem. cell Biol., 64, 659, 10.1139/o86-091 · DOI
  43. Russel D.H., 1987, J. Immunol., 138, 276, 10.4049/jimmunol.138.1.276 · DOI
  44. Ogren L., 1989, Endo., 125, 2253, 10.1210/endo-125-5-2253 · DOI

Metadata

Authors
Borys, M. C., Linzer, D. I. H., & Papoutsakis, E. T.
Affiliations
Northwestern University (US)
Venue
Nature Biotechnology
Published
1993-06
Volume
11
Issue
6
Pages
720-724
ISSN
  • 0733-222X (ISSN-L)
  • 1087-0156
  • 1546-1696
OpenAlex
W1981449476
Cited by
171
References
42
Citations by year
2026: 1 · 2025: 3 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 6 · 2017: 7 · 2016: 4 · 2015: 9 · 2014: 7 · 2013: 10 · 2012: 6
FWCI
2.06
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Biotechnology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01hd024518-11)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD24518)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
Keywords
extracellular pH, recombinant protein expression, glycosylation, CHO cells, protein secretion, culture medium pH
MeSH terms
Animals, Carbohydrate Sequence, Glycosylation, Cricetinae, Hydrogen-Ion Concentration, Molecular Sequence Data, Placental Lactogen, Recombinant Proteins, Immunoblotting, Gene Expression, CHO Cells, Culture Media, Conditioned, Mice

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