Different transforming growth factor-alpha species are derived from a glycosylated and palmitoylated transmembrane precursor

Cell. 1987 Feb 13;48(3):429-40. doi: 10.1016/0092-8674(87)90194-2.


cDNA analysis has revealed that the 50 amino acid transforming growth factor-alpha (TGF-alpha) is derived from a 160 amino acid precursor. Antibodies to TGF-alpha and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-alpha expression vector secrete high levels of TGF-alpha; a mixture of species of about 18 kd is secreted in addition to the 50 amino acid form. These larger species are N-glycosylated and are derived from the same precursor as the smaller form. The C-terminal segment of the precursor remains anchored in the membrane and has covalently attached palmitate. The newly synthesized TGF-alpha precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-alpha species.

MeSH terms

  • Animals
  • Antibodies
  • Cell Line
  • Cell Membrane / metabolism
  • Cricetinae
  • Glycosylation
  • Membrane Proteins / metabolism*
  • Palmitates / metabolism
  • Peptides / immunology
  • Peptides / metabolism*
  • Protein Precursors / immunology
  • Protein Precursors / metabolism*
  • Protein Processing, Post-Translational
  • Transforming Growth Factors


  • Antibodies
  • Membrane Proteins
  • Palmitates
  • Peptides
  • Protein Precursors
  • Transforming Growth Factors