Macrophages secrete a novel heparin-binding protein with inflammatory and neutrophil chemokinetic properties Academic Article uri icon

Overview

MeSH Major

  • Biological Products
  • Carrier Proteins
  • Chemotactic Factors
  • Heparin
  • Inflammation
  • Macrophages

abstract

  • We report the identification and purification of a new inflammatory monokine synthesized by the macrophage tumor cell line RAW 264.7 in response to endotoxin. This monokine, which we term "macrophage inflammatory protein" (MIP), is a doublet with an apparent molecular mass of approximately 8,000 daltons on SDS-PAGE but forms aggregates of greater than 2 x 10(6) daltons as assessed by gel filtration. Partial NH2-terminal amino acid sequence data reveal no significant homology with any previously described protein. Although the monokine is anionic under physiological conditions, it is one of two major macrophage-secreted proteins that bind to heparin at high salt concentrations. At 100 ng/ml or greater, MIP is chemokinetic for human polymorphonuclear cells and triggers hydrogen peroxide production. Subcutaneous injection of 10 ng or greater of MIP into footpads of C3H/HeJ mice elicits an inflammatory response, characterized by neutrophil infiltration. These findings suggest that MIP is an endogenous mediator that may play a role in the host responses that occur during endotoxemia and other inflammatory events.

publication date

  • January 1988

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2188834

PubMed ID

  • 3279154

Additional Document Info

start page

  • 570

end page

  • 81

volume

  • 167

number

  • 2