Oligodendrocytes lack glycolipid anchored proteins which protect them against complement lysis. Restoration of resistance to lysis by incorporation of CD59

M G Wing, J Zajicek, D J Seilly, D A Compston, P J Lachmann

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47 Citations (Scopus)

Abstract

Rat oligodendrocytes, which activate the classical pathway of complement in the absence of antibody, are highly sensitive in a reactive lysis assay using human C5b6 and EDTA serum. Oligodendrocytes may be relatively deficient in glycolipid-linked complement regulatory protein(s), since digestion with phosphatidylinositol-specific phospholipase C (PI-PLC) failed to increase their sensitivity to serum, whereas complement-insensitive astrocytes, when treated with PI-PLC, became strikingly sensitive. To test the hypothesis that oligodendrocytes lack terminal complement regulatory molecule(s), human erythrocyte CD59, a recently described complement regulatory protein, was purified to homogeneity. The biological activity of the preparation was confirmed by reincorporating the protein into guinea-pig erythrocytes through its glycolipid anchor, which resulted in dose-dependent protection against human C5b6 and EDTA serum. Incorporation of 10(5) molecules of human CD59 into rat oligodendrocytes resulted in good protection against homologous human complement (76%), and significant protection against rat complement homologous to the cell (36%). Protection could be reversed using an antibody to CD59.

Original languageEnglish
Pages (from-to)140-5
Number of pages6
JournalImmunology
Volume76
Issue number1
Publication statusPublished - May 1992

Keywords

  • Animals
  • Antigens, CD
  • Antigens, CD59
  • Cell Membrane
  • Cells, Cultured
  • Complement System Proteins
  • Cytotoxicity, Immunologic
  • Glycolipids
  • Humans
  • Membrane Glycoproteins
  • Oligodendroglia
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphoinositide Phospholipase C
  • Phosphoric Diester Hydrolases
  • Rats
  • Rats, Inbred Strains

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