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Surface expression of immunoglobulin isotypes on primary human B cells: no evidence for glycosyl-phosphatidylinositol linkage.

Authors
  • A C Lankester
  • C J van Noesel
  • G M van Schijndel
  • R A van Lier
Publication Date
Sep 01, 1993
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

Abstract

Surface expression of membrane(m) IgM molecules requires the association of two disulphide-linked transmembrane (TM) glycoproteins, encoded by the B-cell-specific genes mb-1 and B29. We have shown that mIgM, mIgD and mIgG are associated with structurally related heterodimers on primary human B cells. Transfection studies in murine plasmacytoma cells, however, have demonstrated mb-1-independent expression of both mIgD and mIgG. The recent finding that mIgD is expressed on these cells through glycosyl-phosphatidylinositol (GPI) linkage may be interesting in view of the function of mIgD on primary B cells. We therefore investigated whether GPI linkage serves as an additional mechanism for expression of mIgD and the other mIg isotypes on primary human B cells. However, we were unable to demonstrate the release of mIg molecules upon treatment with phosphatidylinositol-specific phospholipase C (PI-PLC) in either immunofluorescence analysis or Ig heavy (H) chain-specific enzyme-linked immunosorbent assay (ELISA). We conclude that primary human B cells, which constitutively express the mb-1 and B29 genes, do not express the mIg isotypes in a GPI-linked manner.

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