Rat gro/melanoma growth-stimulating activity. Assessment of the structure responsible for chemotactic activity by use of its fragments prepared by proteolysis and chemical synthesis

Cytokine. 1992 Jan;4(1):12-7. doi: 10.1016/1043-4666(92)90030-u.


Rat gro/melanoma growth-stimulating activity is a dimer composed of two identical subunits. Each subunit consists of 72 amino-acid residues and contains two disulfide bridges. In order to obtain information on the structure responsible for chemotactic activity, various fragments of gro were prepared and tested for their ability to induce chemotaxis. None of the fragments corresponding to residues 1-6, 1-21, 12-31, 36-50 or 52-72 was active as a chemoattractant. Reduced and carboxymethylated gro as well as the tryptic peptide consisting of three peptides, residues 9-21, 28-45 were and 49-61, linked by two disulfide bonds Cys-9-Cys-35 and Cys-11-Cys-51, were inactive. Also, these, peptides did not inhibit the chemotactic activity of gro. Rat gro lacking the N-terminal 6 residues had a reduced activity and the one lacking the C-terminal Lys was as active as intact gro. Therefore, an almost entire portion of the molecule including disulfide cross-links is required for chemotactic activity.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chemokine CXCL1
  • Chemokines, CXC*
  • Chemotactic Factors / chemistry
  • Chemotactic Factors / pharmacology*
  • Chemotaxis, Leukocyte / drug effects*
  • Endopeptidases / metabolism
  • Growth Substances / chemistry
  • Growth Substances / pharmacology*
  • Intercellular Signaling Peptides and Proteins*
  • Molecular Sequence Data
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / pharmacology*
  • Neutrophils / drug effects*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology*
  • Rats
  • Structure-Activity Relationship


  • Chemokine CXCL1
  • Chemokines, CXC
  • Chemotactic Factors
  • Cxcl1 protein, rat
  • Growth Substances
  • Intercellular Signaling Peptides and Proteins
  • Neoplasm Proteins
  • Peptide Fragments
  • Endopeptidases