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Tyrosine phosphorylation of MB-1, B29, and HS1 proteins in human B cells following receptor crosslinking.

Recent studies of murine and human B lymphocytes have shown that crosslinking of surface IgM (sIgM) and sIgD stimulates tyrosine phosphorylation of a set of proteins involved in signal transduction. We investigated tyrosine phosphorylation of the sIg-associated proteins MB-1 and B29, and p75HS1 (HS1), and the association of HS1 with MB-1/B29 heterodimers in normal human B cells and a human B lymphoma cell line, B104. Using immunoprecipitation with anti-phosphotyrosine antibodies (Abs) followed by immunoblotting with anti-MB-1 Abs, anti-B29 Abs or anti-HS1 Abs, we demonstrated that MB-1, B29 and HS1 were tyrosine-phosphorylated after sIgM or sIgD crosslinking. Immunoprecipitation with anti-B29 Abs followed by anti-HS1 Abs immunoblotting revealed that HS1 was associated with MB-1/B29 heterodimers after sIgM or sIgD crosslinking. The results showed that HS1 may play an important role in signal transduction through sIgM and sIgD on human B cells.

Pubmed ID: 7927516

Authors

  • Hata D
  • Nakamura T
  • Kawakami T
  • Kawakami Y
  • Herren B
  • Mayumi M

Journal

Immunology letters

Publication Data

April 24, 1994

Associated Grants

None

Mesh Terms

  • Antigens, CD
  • Antigens, CD79
  • B-Lymphocytes
  • Base Sequence
  • Blood Proteins
  • DNA Primers
  • Humans
  • Immunoglobulin D
  • Immunoglobulin M
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Phosphoproteins
  • Phosphorylation
  • Receptors, Antigen, B-Cell
  • Receptors, Fc
  • Receptors, IgG
  • Signal Transduction
  • Tumor Cells, Cultured
  • Tyrosine