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Published ahead of print on December 23, 2004, doi:10.1164/rccm.200311-1535OC

Am. J. Respir. Crit. Care Med., Volume 171, Number 8, April 2005, 899-907

A more recent version of this article appeared on April 15, 2005
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Submitted on November 12, 2003
Accepted on December 17, 2004

Characterization of Fibroblast Specific Protein 1 in Pulmonary Fibrosis

William E Lawson1, Vasiliy V Polosukhin2, Ornella Zoia2, Georgios T Stathopoulos2, Wei Han2, David Plieth3, James E Loyd2, Eric G Neilson4, and Timothy S Blackwell5*

1 Department of Medicine, Division of Allergy, Pulmonary and Critical Care Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA; Department of Veterans Affairs Medical Center, Nashville, TN, USA, 2 Department of Medicine, Division of Allergy, Pulmonary and Critical Care Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA, 3 Department of Medicine, Division of Nephrology, Vanderbilt University School of Medicine, Nashville, TN, USA, 4 Department of Medicine, Division of Nephrology, Vanderbilt University School of Medicine, Nashville, TN, USA; Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA, 5 Department of Medicine, Division of Allergy, Pulmonary and Critical Care Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA; Department of Veterans Affairs Medical Center, Nashville, TN, USA; Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA

* To whom correspondence should be addressed. E-mail: timothy.blackwell{at}vanderbilt.edu.

Since fibroblasts produce collagen and other extracellular matrix components that are deposited during tissue fibrosis, defining the behavior of these cells is critical to understanding the pathogenesis of fibrotic diseases. We investigated the utility of fibroblast specific protein 1 (FSP1), a member of the calmodulin S100 troponin C superfamily, for identifying lung fibroblasts in a murine model of pulmonary fibrosis induced by intratracheal administration of bleomycin. Protein and mRNA expression of FSP1 was minimal in untreated lungs, but increased by 1 week following bleomycin administration and remained increased at 2 and 3 weeks after treatment. By immunohistochemistry, the number of FSP1+ cells increased in a dose dependent manner in the lungs following bleomycin treatment. Co-localization of {alpha}1 procollagen and FSP1 in interstitial cells demonstrated that FSP1+ fibroblasts contribute to the deposition of collagen following bleomycin administration. In primary lung cell cultures, lung fibroblasts, but not macrophages or type II alveolar epithelial cells, expressed FSP1. FSP1 also identified fibroblasts in lung biopsy specimens from patients with documented usual interstitial pneumonitis. Therefore, FSP1 is an improved marker for lung fibroblasts that could be useful for investigating the pathogenesis of pulmonary fibrosis.
Key words: lung, bleomycin, mouse, collagen, alpha smooth muscle actin




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