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MIP-1 gamma: molecular cloning, expression, and biological activities of a novel CC chemokine that is constitutively secreted in vivo

Academic Article
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Overview

authors

  • Poltorak, A. N.
  • Bazzoni, F.
  • Smirnova, II
  • Alejos, E.
  • Thompson, Paul
  • Luheshi, G.
  • Rothwell, N.
  • Beutler, Bruce

publication date

  • 1995

journal

  • Journal of Inflammation  Journal

abstract

  • We have identified a novel CC chemokine family member, herein termed MIP-1 gamma in view of its similarity to existing members of the MIP-1 group. The murine protein has a predicted length of 100 amino acids. Like MIP-1 alpha, recombinant MIP-1 gamma acts as a pyrogen when administered intracerebroventricularly. MIP-1 gamma and MIP-1 alpha engage the same high-affinity receptor on neutrophils, activating calcium release within seconds following cell contact. Pretreatment with either chemokine abolishes responses to the other, and to itself, suggesting utilization of a common signaling pathway. However, unlike MIP-1 alpha or any of the other CC chemokines, MIP-1 gamma is expressed constitutively by a wide variety of tissues, and circulates in the blood of healthy mice at concentrations of approximately 1 microgram/ml (90 nM). It would therefore be predicted that MIP-1 gamma occupies most of the CC chemokine receptors that exist in the intravascular compartment. As such it might, under normal circumstances, markedly influence responses to the inducible CC chemokines.

subject areas

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Chemokine CCL4
  • Cloning, Molecular
  • DNA, Complementary
  • Escherichia coli
  • Fever
  • Gene Expression
  • Macrophage Inflammatory Proteins
  • Male
  • Mice
  • Molecular Sequence Data
  • Monokines
  • Neutrophils
  • RNA, Messenger
  • Rats
  • Rats, Sprague-Dawley
  • Recombinant Proteins
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Research

keywords

  • CC CHEMOKINE
  • MIP-1-ALPHA
  • MIP-1-GAMMA
  • MURINE PROTEIN
  • NEUTROPHILS
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Identity

International Standard Serial Number (ISSN)

  • 1078-7852

PubMed ID

  • 8597875
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Additional Document Info

start page

  • 207

end page

  • 219

volume

  • 45

issue

  • 3

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