Immunoglobulin Production Stimulating Factors

  • Hiroki Murakami
  • Takuya Sugahara
  • Hiroto Nakajima
Part of the Serono Symposia, USA book series (SERONOSYMP)


Industrial animal cell technology aims mainly at producing large quantities of cellular bioactive substances of medical significance. This is accomplished by the fusion of biological sciences, including cell physiology and genetics, and many other component technologies.


Immunoglobulin Production Rabbit Reticulocyte Lysate Bioactive Protein HB4C5 Cell Namalwa Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Murakami H. What should be focused in the study of cell culture technology for production of bioactive proteins. Cytotechnology 1990; 3: 3–7.PubMedCrossRefGoogle Scholar
  2. 2.
    Murakami H, Masui H, Sato GH, Sueoka N, Chow TP, Kono-Sueoka T. Growth of hybridoma cells in serum-free medium. Proc Natl Acad Sci USA 1982; 79: 1158.PubMedCrossRefGoogle Scholar
  3. 3.
    Murakami H, Yamada K. Production of cancer specific monoclonal antibodies with human-human hybridomas and their serum-free, high density, perfusion culture. In: Spier R, Griffiths JB, eds. Modern approaches to animal cell technology. Butterworths, 1987: 52–72.Google Scholar
  4. 4.
    Murakami H. Serum-free media used for cultivation of hybridomas. In: Mizrahi A, ed. Monoclonal antibodies: production and application, advances in biotechnological processes; vol. 11. 1989: 107–41.Google Scholar
  5. 5.
    Franek F, Dolnikova J. Hybridoma growth and monoclonal antibody production in iron-rich protein-free medium: effect of nutrient concentration. Cytotechnology 1991; 7: 33–8.PubMedCrossRefGoogle Scholar
  6. 6.
    Murakami H, ed. Trends in animal cell culture technology. Tokyo/Weinheim: Kodansha/VCH, 1990.Google Scholar
  7. 7.
    Sasaki R, Ikura K, eds. Animal cell culture and production of biologicals. Dordrecht: Kluwer Academic, 1991.Google Scholar
  8. 8.
    Griffiths JB. Animal cells-the breakthrough to a dominant technology. Cytotechnology 1990; 3: 109–16.PubMedCrossRefGoogle Scholar
  9. 9.
    Lydersen BK, ed. Large scale cell culture technology. New York: Hanser, 1987.Google Scholar
  10. 10.
    Takazawa T, Tokashiki M, Hamamoto K, Murakami H. High cell density perfusion culture of hybridoma cells recycling high molecular weight compounds. Cytotechnology 1988; 1: 171.PubMedCrossRefGoogle Scholar
  11. 11.
    Murakami H, Shimomura T, Ohashi H, et al. Serum-free stirred culture of human-human hybridoma lines. In: Murakami H, Yamane I, Barnes D, Mather J, Hayashi I, Sato G, eds. Growth and differentiation of cells in defined environment. Tokyo/Berlin: Kodansha/Springer-Verlag, 1985: 111.Google Scholar
  12. 12.
    Hashizume S, Mochizuki K, Murakami H, Yano Y, Yasumoto K, Nomoto K. Serodiagnosis of cancer, using porcine antigens recognized by human monoclonal antibody, HB4C5. Biotherapy 1989; 1: 109–15.PubMedCrossRefGoogle Scholar
  13. 13.
    Neuberger M. Expression and regulation of immunoglobulin heavy chain gene transfected into lymphoid cells. EMBO J 1983; 2: 1373–8.PubMedGoogle Scholar
  14. 14.
    Zinn K, Warren N, Sudgen B. Regulated expression of an extrachromosomal human b-interferon gene in mouse cells. Proc Natl Acad Sci USA 1982; 79: 4897–901.PubMedCrossRefGoogle Scholar
  15. 15.
    Hentschel C. Recent developments in mammalian expression systems. In: Spier R, Griffiths J, Meignier B, eds. Butterworth-Heinemann, 1991:287–301.Google Scholar
  16. 16.
    Warner N. Membrane immunoglobulins and antigen receptors on B and T lymphocytes. Adv Immunol 1974; 19: 67.PubMedCrossRefGoogle Scholar
  17. 17.
    Brenner S, Jacob F, Meselson M. An unstable intermediate carrying information from genes to ribosomes for protein synthesis. Nature 1961; 190: 576.PubMedCrossRefGoogle Scholar
  18. 18.
    Hay R, Macy M, Hamburger A, et al., eds. American type culture collection catalogues of strain II. 4th ed. MD: American Type Culture Collection, 1983: 107.Google Scholar
  19. 19.
    Murakami H, Yamada K. Production of cancer specific monoclonal antibodies with human-human hybridomas and their serum-free, high density, perfusion culture. In: Spier R, Griffiths JB, eds. Modern approaches to animal cell technology. London: Butterworths, 1987: 52.Google Scholar
  20. 20.
    Yamada K, Akiyoshi K, Murakami H, et al. Partial purification and characterization of immunoglobulin production stimulating factor derived from Namalwa cells. In Vitro Cell Dev Biol 1989; 25: 243.PubMedCrossRefGoogle Scholar
  21. 21.
    Sato S, Murakami H, Sugahara T, et al. Stimulation of monoclonal antibody production by human-human hybridoma cells with an elevated concentration of potassium or sodium phosphate in serum-free medium. Cytotechnology 1989; 2: 63.PubMedCrossRefGoogle Scholar
  22. 22.
    Maeda M, Yamada K, Ohta H, Tajima M, Murakami H. Stimulation of IgM production in human-human hybridoma HB4C5 cells and human lymphocytes by soybean hull hemicellulose. J Agri Food Chem 1991; 39: 820–3.CrossRefGoogle Scholar
  23. 23.
    Shinmoto H, Murakami H, Yamada K, Dosako S, Omura H. Immunoglobulin production stimulating and inhibiting factor derived from human lung adenocarcinoma PC-8 cells. Cytotechnology 1988; 1: 295–300.PubMedCrossRefGoogle Scholar
  24. 24.
    Toyoda K, Sugahara T, Inoue K, Yamada K, Shirahata S, Murakami H. Purification and characterization of the immunoglobulin production stimulating factor derived from human B lymphoblastoid cell HO-323. Cytotechnology 1990; 3: 189–97.PubMedCrossRefGoogle Scholar
  25. 25.
    Sugahara T, Shirahata S, Yamada K, Murakami H. Purification of immunoglobulin production stimulating factor-IIa derived from Namalwa cells. Cytotechnology 1991; 5: 255–63.PubMedCrossRefGoogle Scholar
  26. 26.
    Sugahara T, Shirahata S, Akiyoshi K, Isobe T, Okuyama T, Murakami H. Immunoglobulin production stimulating factor-IIa (IPSF-IIa) is glyceraldehyde-3-phosphate dehydrogenase like protein. Cytotechnology 1991; 6: 115–20.PubMedCrossRefGoogle Scholar
  27. 27.
    Arcari P, Martinelli R, Salvatore F. The complete sequence of a full length cDNA for human liver glyceraldehyde 3-phosphate dehydrogenase: evidence for multiple mRNA species. Nucleic Acids Res 1984; 12: 9179–89.PubMedCrossRefGoogle Scholar
  28. 28.
    Nowak K, Wolny M, Banas T. The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Lett 1981; 134: 143–6.PubMedCrossRefGoogle Scholar
  29. 29.
    Harris JI, Perham RN. Glyceraldehyde 3-phosphate dehydrogenase from pig muscle. Nature 1968; 219: 1025–8.PubMedCrossRefGoogle Scholar
  30. 30.
    Panabieres F, Piechaczyk M, Rainer B, et al. Complete nucleotide sequence of the messenger RNA coding for chicken muscle glyceraldehyde 3-phosphate dehydrogenase. Biochem Biophys Res Commun 1984; 118: 767–73.PubMedCrossRefGoogle Scholar
  31. 31.
    Davidson DE, Sajgo M, Noller HF, Harris JI. Amino acid sequence of glyceraldehyde 3-phosphate dehydrogenase from lobster muscle. Nature 1967; 216: 1181–5.PubMedCrossRefGoogle Scholar
  32. 32.
    Holland JP, Labieniec L, Swimmer C, Holland MJ. Homologous nucleotide sequences at the 5’ termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde 3-phosphate dehydrogenase gene families. J Biol Chem 1983; 258: 5291–9.PubMedGoogle Scholar
  33. 33.
    Walker JE, Carne AF, Runswick MJ, Bridgen J, Harris JI. D-glyceraldehyde3-phosphate dehydrogenase, complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. Eur J Biochem 1980; 108: 549–65.PubMedCrossRefGoogle Scholar
  34. 34.
    Murakami H, Yamada K, Shirahata S, Enomoto A, Kaminogawa S. Physiological enhancement of immunoglobulin production of hybridomas in serum-free media. Cytotechnology 1991; 5: 83–94.PubMedCrossRefGoogle Scholar
  35. 35.
    Yamada K, Ikeda I, Nakajima H, Shirahata S, Murakami H. Stimulation of proliferation and immunoglobulin production of human-human hybridoma by various types of caseins and their protease digests. Cytotechnology 1991; 5: 279–85.PubMedCrossRefGoogle Scholar
  36. 36.
    Bienkowski RS. Intracellular degradation of newly synthesized secretory proteins. Biochem J 1983; 1: 214: 1–10.Google Scholar
  37. 37.
    Al-Rubeai MA, Emery AN. Monoclonal antibody accumulation and release observed in sub-cellular structures in synchronous and asynchronous hybridoma culture [Abstract]. Cytotechnology, 1989: S9.Google Scholar
  38. 38.
    Al-Rubeai M, Mills D, Emery AN. Electron microscopy of hybridoma cells with special regard to monoclonal antibody production. Cytotechnology 1990; 4: 13–28.PubMedCrossRefGoogle Scholar
  39. 39.
    Perucho M, Salas J, Salas M. Study of the interaction of glyceraldehyde3-phosphate dehydrogenase with DNA. Biochim Biophys Acta 1980; 606: 181–95.PubMedGoogle Scholar
  40. 40.
    Ryazanov A. Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes. FEBS Lett 1985; 192: 131–4.PubMedCrossRefGoogle Scholar
  41. 41.
    Ryazanov A, Asmaria L, Muronetz V. Association of glyceraldehyde3-phosphate dehydrogenase with mono-and polyribosomes of rabbit reticulocytes. Eur J Biochem 1988; 171: 301–5.PubMedCrossRefGoogle Scholar
  42. 42.
    Mechler B, Vassalli P. Membrane-bound ribosomes of myeloma cells, III. The role of the messenger RNA and the nascent polypeptide chain in the binding of ribosomes to membranes. J Cell Biol 1975; 67: 25–37.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag New York, Inc. 1993

Authors and Affiliations

  • Hiroki Murakami
  • Takuya Sugahara
  • Hiroto Nakajima

There are no affiliations available

Personalised recommendations