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Am J Physiol Lung Cell Mol Physiol 287: L1-L23, 2004; doi:10.1152/ajplung.00301.2003
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Invited Review

Proteomics: current techniques and potential applications to lung disease

Jan Hirsch,1 Kirk C. Hansen,2 Alma L. Burlingame,2 and Michael A. Matthay1

1Cardiovascular Research Institute and 2Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143

Proteomics aims to study the whole protein content of a biological sample in one set of experiments. Such an approach has the potential value to acquire an understanding of the complex responses of an organism to a stimulus. The large vascular and air space surface area of the lung expose it to a multitude of stimuli that can trigger a variety of responses by many different cell types. This complexity makes the lung a promising, but also challenging, target for proteomics. Important steps made in the last decade have increased the potential value of the results of proteomics studies for the clinical scientist. Advances in protein separation and staining techniques have improved protein identification to include the least abundant proteins. The evolution in mass spectrometry has led to the identification of a large part of the proteins of interest rather than just describing changes in patterns of protein spots. Protein profiling techniques allow the rapid comparison of complex samples and the direct investigation of tissue specimens. In addition, proteomics has been complemented by the analysis of posttranslational modifications and techniques for the quantitative comparison of different proteomes. These methodologies have made the application of proteomics on the study of specific diseases or biological processes under clinically relevant conditions possible. The quantity of data that is acquired with these new techniques places new challenges on data processing and analysis. This article provides a brief review of the most promising proteomics methods and some of their applications to pulmonary research.

mass spectrometry; proteome; lung


Address for reprint requests and other correspondence: J. Hirsch, Cardiovascular Research Institute, Univ. of California, San Francisco, 505 Parnassus Ave. HSW 825, San Francisco, CA 94143-0130 (E-mail: jhirsch{at}itsa.ucsf.edu).




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