Cytotoxic properties of eosinophil granule major basic protein for tumor cells

Int Arch Allergy Immunol. 1999 Feb-Apr;118(2-4):426-8. doi: 10.1159/000024154.

Abstract

Background: Eosinophil granule major basic protein (MBP) mediates many eosinophil-associated immune functions and it adheres eosinophils to parasite targets.

Methods: We compared the toxicities of MBP and melittin to K562 and HL-60 cells using five cytotoxicity methods.

Results: Trypan blue staining, propidium iodide/ CellTrackertrade markGreen staining and incorporation of 14C-leucine assays indicated that MBP damages most cells by 1 h. In contrast, 51Cr and lactic dehydrogenase (LDH) release assays indicated that MBP damages most cells only at 20 h. All five methods indicated that melittin damages nearly all cells by 1 h. To resolve these discrepancies, the procedures were modified. Without cell transfer, dye staining methods showed that MBP produces very little cytotoxicity at 4 h. 51Cr and LDH assays, modified to mimic cell transfer, showed increased cytotoxicities at 4 h. The 14C-leucine assay modified by solubilization of cells with SDS and by trichloroacetic acid precipitation showed increased recovery of labeled protein and, thus, lower cytotoxicity, about 50%, at 4 h.

Conclusion: Overall, MBP's ability to cause molecular and cellular adhesion confounds cytotoxicity measurements. A modified 14C-leucine assay overcame MBP's adhesiveness and provided an accurate measure of cytotoxicity.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Blood Proteins / immunology*
  • Cytoplasmic Granules / immunology
  • Cytotoxicity, Immunologic*
  • Eosinophil Granule Proteins
  • Eosinophils / immunology*
  • Eosinophils / ultrastructure
  • HL-60 Cells
  • Humans
  • K562 Cells
  • Neoplasms / immunology*
  • Ribonucleases*

Substances

  • Blood Proteins
  • Eosinophil Granule Proteins
  • Ribonucleases