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Published ahead of print on June 12, 2003, doi:10.1165/rcmb.2003-0078OC

Am. J. Respir. Cell Mol. Biol., Volume 29, Number 6, December 2003, 743-749

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Submitted on March 18, 2003
Revised on June 11, 2003

Pulmonary and Activation-Regulated Chemokine Stimulates Collagen Production in Lung Fibroblasts

Sergei P Atamas1*, Irina G Luzina2, Jung Choi3, Natalya Tsymbalyuk3, Nicholas H Carbonetti4, Ishwar S Singh2, Maria Trojanowska5, Sergio A Jimenez6, and Barbara White1

1 Department of Medicine, University of Maryland School of Medicine, Baltimore, MD, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD, USA; Research Service, Veterans Affairs Maryland Health Care System, Baltimore, MD, USA, 2 Department of Medicine, University of Maryland School of Medicine, Baltimore, MD, USA; Research Service, Veterans Affairs Maryland Health Care System, Baltimore, MD, USA, 3 Department of Medicine, University of Maryland School of Medicine, Baltimore, MD, USA, 4 Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD, USA, 5 Division of Rheumatology and Immunology, Medical University of South Carolina, Charleston, SC, USA, 6 Department of Medicine, Thomas Jefferson University, Philadelphia, PA, USA

* To whom correspondence should be addressed. E-mail: satamas{at}umaryland.edu.

Levels of pulmonary and activation-regulated chemokine (PARC) mRNA and protein are increased in the lungs of patients with pulmonary fibrosis. The purpose of this work was to establish whether PARC could be directly involved in development of pulmonary fibrosis by stimulating collagen production in lung fibroblasts. Exposure to PARC increased production of collagen mRNA and protein by three to four fold in normal adult lung and dermal fibroblast cells. Collagen mRNA transiently increased after 3 to 6 hours of activation with PARC, with an increase in collagen protein detected after 24 hours of activation. At the same time, PARC had less pronounced effect on fibroblast proliferation, not exceeding 50% increase over control non-stimulated cells. PARC intracellular signaling led to activation of ERK 1/2, but not p38, in fibroblasts; pharmacological inhibition of ERK, but not p38, also blocked PARC's effect on collagen production. Inhibition experiments with pertussis toxin suggested that PARC receptor is G protein-coupled. Thus, PARC is a member of the CC chemokine family that acts directly as a profibrotic factor.




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