Skip to main content
Log in

Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth

  • Rapid Communication
  • Published:
Journal of Cancer Research and Clinical Oncology Aims and scope Submit manuscript

Abstract

Several tumour-forming cell lines are known to secrete the precursor of a lysosomal cysteine proteinase, procathepsin L. The function in tumour growth and proliferation of this neutral-pH-labile proteinase or its precursor outside lysosomes is as yet unknown. Murine myeloma cells (P3X63Ag8.653) secrete procathepsin L and exhibit a high potential for malignant tumour growth and metastasis. Such cells were fused with spleen cells of mice immunized with cathepsin L. Clones of the resulting hybridoma cells continued to secrete procathepsin L, but also secreted the antibody to cathepsin L. Here we show that the hybridoma cells producing an antibody to cathepsin L have, to a great extent, lost the potential that they otherwise exhibit for inducing solid tumours after implantation into mice.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  • Belleli A, Mattioni M, Rusconi V, Sezzi ML, Belleli L (1990) Inhibition of tumor growth, invasion and metastasis in papain-immunized mice. Invasion Metastasis 10:142–169

    Google Scholar 

  • Doria G, Agarossi G, Adorini L (1982) Selective effects of ionizing radiations on immunoregulatory cells. Immunol Rev 65:23–54

    Google Scholar 

  • Gottesman MM (1978) Transformation-dependent secretion of a low molecular weight protein by murine fibroblasts. Proc Natl Acad Sci USA 75:2767–2771

    Google Scholar 

  • Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (1988) Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L: an abundant transcript induced by transformation of fibroblasts. J Clin Invest 81:1621–1629

    Google Scholar 

  • Kane SE, Gottesman MM (1990) The role of cathepsin L in malignant transformation. Semin Cancer Biol 1:127–136

    Google Scholar 

  • Kennett RH (1978) Cell fusion. Methods Enzymol 58:345–359

    Google Scholar 

  • Kirschke H, Langner J, Wiederanders B, Ansorge S, Bohley P (1977) Cathepsin L—a new proteinase from rat liver lysosomes. Eur J Biochem 74:293–301

    Google Scholar 

  • Kobayashi H, Ohi H, Sugimura M, Shinohara H, Fujii T, Terao T (1992) Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B. Cancer Res 52:3610–3614

    Google Scholar 

  • Mason RW, Gal S, Gottesman MM (1987) The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem J 248:449–454

    Google Scholar 

  • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021

    Google Scholar 

  • Troen BR, Gal S, Gottesman MM (1987) Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. Biochem J 246:731–735

    Google Scholar 

  • Wiederanders B, Kirschke H (1986) Antibodies to rat liver cathepsins: characterization and use for the identification of enzyme precursors. Biomed Biochim Acta 45:1421–1431

    Google Scholar 

  • Yagel S, Warner AH, Nellans HN, Lala PK, Waghorne C, Denhardt DT (1989) Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res 49:3553–3557

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

This work was supported by the Bundesministerium für Forschung und Technologie, Bonn, Germany, (BMFT 01 ZZ 9105)

Rights and permissions

Reprints and permissions

About this article

Cite this article

Weber, E., Günther, D., Laube, F. et al. Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth. J Cancer Res Clin Oncol 120, 564–567 (1994). https://doi.org/10.1007/BF01221037

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01221037

Key words

Navigation