
Interleukin 3 binds to a 140-kDa phosphotyrosine-containing cell surface protein.
Author(s) -
Robert J. Isfort,
Dennis Stevens,
Win May,
James N. Ihle
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.21.7982
Subject(s) - phosphoprotein , biology , haematopoiesis , growth factor , cell growth , microbiology and biotechnology , binding protein , progenitor cell , surface protein , chemistry , phosphorylation , biochemistry , stem cell , receptor , gene , virology
Interleukin 3 (IL-3) is a hematopoietic growth factor that supports the proliferation and differentiation of early hematopoietic-lineage progenitors. By using growth factor-dependent cell lines, IL-3 has been shown to induce the appearance of several phosphotyrosine-containing proteins, including a 140-kDa cell surface phosphoprotein. Here we demonstrate that the 140-kDa phosphoprotein binds IL-3 and forms a stable complex with an apparent molecular mass of 170 kDa. The possible relationship of the 140-kDa phosphoprotein to the previously described 65-kDa IL-3-binding protein is discussed.