Protein kinase C-dependcnt release of a functional whole extracellular domain of the mast cell growth factor (MGF) receptor by MGF-dependent human myeloid cells

Maria F. Brizzi, Janna M. Blechman, Giuliana Cavalloni, David Givol, Yosef Yarden, Luigi Pegoraro

Research output: Contribution to journalArticlepeer-review

Abstract

The mast cell growth factor (MGF) affects migration, proliferation and differentiation of erythroid and myeloid progenitor cells by binding to a transmembrane receptor tyrosine kinase encoded by the c-Kit proto-oncogene. By using MGF-dependent human myeloid cell lines (M-07e and TF-1), here we show that a Kit-related 100 kDa protein is associated with the cell but it undergoes release into the medium upon treatment with the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C. Immunological analysis with a series of antibodies to Kit indicated that the released protein (p100Kit) contains the whole glycosylated extra-cellular portion of the transmembrane Kit protein (p145Kit). The secreted protein retained the ability to specifically bind MGF. Moreover, p100Kit was able to block the mitogenic effect of MGF on cultured M-07e cells, suggesting that the soluble protein may function as a physiological antagonist of MGF.

Original languageEnglish
Pages (from-to)1583-1589
Number of pages7
JournalOncogene
Volume9
Issue number6
Publication statusPublished - Jun 1994

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

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