Identification of the monocyte chemotactic protein from human osteosarcoma cells and monocytes: detection of a novel N-terminally processed form

Biochem Biophys Res Commun. 1990 Mar 30;167(3):904-9. doi: 10.1016/0006-291x(90)90609-q.

Abstract

The chemotactic activity for monocytes in culture supernatants from double-stranded RNA-stimulated human MG-63 osteosarcoma cells and from LPS-stimulated human monocytes was purified to homogeneity and characterized by amino acid sequence analysis. The chemotactic protein derived from the fibroblastoid osteosarcoma cells had a blocked N-terminus but sequencing of tryptic fragments showed that it was identical with a recently identified monocyte chemoattractant designated MCP-1 or MCAF isolated from glioma or myelomonocytic cells, respectively. Preparations of monocyte -derived chemotactic activity appeared to contain not only the blocked protein, but also a novel N-terminally processed form of this molecule, lacking 5 amino acid residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Chemokine CCL2
  • Chemotactic Factors / blood
  • Chemotactic Factors / isolation & purification*
  • Chemotactic Factors / pharmacology
  • Chemotaxis, Leukocyte / drug effects
  • Chromatography, High Pressure Liquid
  • Humans
  • In Vitro Techniques
  • Lipopolysaccharides / pharmacology
  • Molecular Sequence Data
  • Monocytes / analysis*
  • Monocytes / cytology
  • Monocytes / drug effects
  • N-Formylmethionine Leucyl-Phenylalanine / pharmacology
  • Osteosarcoma / analysis*
  • Peptide Fragments / isolation & purification
  • Tumor Cells, Cultured / analysis

Substances

  • Chemokine CCL2
  • Chemotactic Factors
  • Lipopolysaccharides
  • Peptide Fragments
  • N-Formylmethionine Leucyl-Phenylalanine