Characterization of monocyte chemotactic protein-1 binding to human monocytes

Anthony J. Valente, Marius M. Rozek, Colin J. Schwartz, Dana T. Graves

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

Monocyte chemotactic protein-1 (MCP-1) stimulates chemotaxis of peripheral blood monocytes. In order to understand the biologic basis of this specific activity, binding studies of 125I-MCP-1 were undertaken. MCP-1 showed saturable binding to monocytes. Scatchard analysis of the monocyte binding data indicate that there are approximately 1,600 high affinity binding sites per monocyte with a Kd = 1.1 nM. Studies with synthetic peptides constructed according to the MCP-1 amino acid sequence indicate that a synthetic peptide, MCP-1[13-35], stimulates monocyte migration and competes with native MCP-1 for binding sites. Inhibition of MCP-1 binding was tested with chemotactic connective tissue proteins. No inhibition of MCP-1 binding was observed with either collagen, elastin-derived peptides or fibronectin. These results identify a single class of unique high affinity MCP-1 binding sites that are likely to recognize a peptide domain on MCP-1 which include the amino acids within the region, 13-35.

Original languageEnglish (US)
Pages (from-to)309-314
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume176
Issue number1
DOIs
StatePublished - Apr 15 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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