Biosynthesis and processing by phorbol ester of the cells surface-associated precursor form of heparin-binding EGF-like growth factor

Biochem Biophys Res Commun. 1994 Oct 28;204(2):592-7. doi: 10.1006/bbrc.1994.2500.

Abstract

Human MDA MB 231 cells were found to synthesize mostly the cell surface-associated precursor form of heparin-binding EGF-like growth factor (HB-EGF), a 27-kDa protein. Evidence for this form of HB-EGF included increased fluorescence intensity when cells were analyzed by flow cytometry using anti-HB-EGF antibodies, lack of HB-EGF in conditioned medium, and sensitivity to diphtheria toxin, for which HB-EGF is the receptor. Phorbol ester treatment of cells resulted, within 30 minutes, in loss of cell surface 27 kDA HB-EGF, lack of interaction with anti-HB-EGF antibodies, accumulation of active 21 kDa HB-EGF in conditioned medium, and the acquisition of diphtheria toxin resistance. It was concluded that cell surface-associated HB-EGF is the precursor of a bioactive growth factor, is biologically active as the receptor for diphtheria toxin, and is susceptible to rapid processing.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Diphtheria Toxin / pharmacology*
  • Heparin-binding EGF-like Growth Factor
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins / biosynthesis*
  • Membrane Proteins / metabolism
  • Protein Processing, Post-Translational*
  • Receptors, Cell Surface / biosynthesis*
  • Receptors, Cell Surface / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology*
  • Tumor Cells, Cultured

Substances

  • Diphtheria Toxin
  • HBEGF protein, human
  • Heparin-binding EGF-like Growth Factor
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Receptors, Cell Surface
  • Tetradecanoylphorbol Acetate