Abstract
A pleural effusion is the abnormal accumulation of fluid between the two layers of pleura that line the chest cavity and surround the lung. Pleural effusion can be the result of several causes. Proteomic analysis may be useful in indicating the pathogenic mechanisms involved in pleural fluid accumulation and might pinpoint specific diagnosis. Differential gel electrophoresis (DIGE) has been employed to compare directly the proteome profile of serum and pleural effusion of mesothelioma patients to identify unique proteins by observing concentration changes and modifications on the single protein level. This technique involves the preelectrophoretic labeling of complex protein samples using different cyanine-based fluorescent tags prior to carrying out separation by 2D polyacrylamide gel electrophoresis. Several proteins have been found to be differentially or uniquely expressed in the serum or pleural effusion of patients.
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References
Noppen M, De Waele M, Li R, et al. Volume and cellular content of normal pleural fluid in humans examined by pleural lavage. Am J Respir Crit Care Med 2000; 162:1023–1026.
Miserocchi G. Physiology and pathophysiology of pleural fluid turnover. Eur Respir J 1997;10:219–225.
Light RW, Macgregor MI, Luchsinger PC, Ball WC Jr. Pleural effusions: the diagnostic separation of transudates and exudates. Ann Intern Med 1972;77: 507–513.
Bartter T, Santarelli R, Akers SM, Pratter MR. The evaluation of pleural effusion. Chest 1994;106:1209–1214.
Hoogsteden HC, Langerak AW, van der Kwast TH, Versnel MA, van Gelder T. Malignant pleural mesothelioma. Crit Rev Oncol Hematol 1997;25:97–126.
Celis JE, Ostergaard M, Jensen NA, Gromova I, Rasmussen HH, Gromov P. Human and mouse proteomic databases: novel resources in the protein universe. FEBS Lett 1998;430:64–72.
Duncan R, McConkey EH. How many proteins are there in a typical mammalian cell? Clin Chem 1982;28:749–755.
Mann M, Jensen ON. Proteomic analysis of post-translational modifications. Nat Biotechnol 2003;21:255–261.
Miklos GL, Maleszka R. Protein functions and biological contexts. Proteomics 2001;1:169–178.
Wold F. In vivo chemical modification of proteins (post-translational modification). Annu Rev Biochem 1981;50:783–814.
Wold F, Moldave K. A short stroll through the posttranslational zoo. Methods Enzymol 1984;107:xiii–xvi.
Tonge R, Shaw J, Middleton B, et al. Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001; 1:377–396.
Von Eggeling F, Gawriljuk A, Fiedler W, et al. Fluorescent dual colour 2D-protein gel electrophoresis for rapid detection of differences in protein pattern with standard image analysis software. Int J Mol Med 2001;8:373–377.
Yan JX, Devenish AT, Wait R, Stone T, Lewis S, Fowler S. Fluorescence twodimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2002;2:1682–1698.
Nordvarg H, Flensburg J, Ronn O, et al. A proteomics approach to the study of absorption, distribution, metabolism, excretion, and toxicity. J Biomol Tech 2004; 15:265–275.
Alban A, David SO, Bjorkesten L, et al. A novel experimental design for comparative two-dimensional gel analysis: two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003;3:36–44.
Unlu M, Morgan ME, Minden JS. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997;18: 2071–2077.
Patton WF. Detection technologies in proteome analysis. J Chromatogr B Analyt Technol Biomed Life Sci 2002;771:3–31.
Lilley KS, Friedman DB. All about DIGE: quantification technology for differentialdisplay 2D-gel proteomics. Expert Rev Proteomics 2004;1:401–409.
Venter JC, Adams MD, Myers EW, et al. The sequence of the human genome. Science 2001;291:1304–1351.
Tyan YC, Wu HY, Su WC, Chen PW, Liao PC. Proteomic analysis of human pleural effusion. Proteomics 2005;5:1062–1074.
Pieper R, Gatlin CL, Makusky AJ, et al. The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 2003; 3:1345–1364.
Sloane AJ, Duff JL, Wilson NL, et al. High throughput peptide mass fingerprinting and protein macroarray analysis using chemical printing strategies. Mol Cell Proteomics 2002; 1:490–499.
Wu SL, Amato H, Biringer R, Choudhary G, Shieh P, Hancock WS. Targeted proteomics of low-level proteins in human plasma by LC/MSn: using human growth hormone as a model system. J Proteome Res 2002; 1:459–465.
Choudhary G, Wu SL, Shieh P, Hancock WS. Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS. J Proteome Res 2003;2:59–67.
Sanchez JC, Appel RD, Golaz O, et al. Inside SWISS-2DPAGE database. Electrophoresis 1995;16:1131–1151.
Adkins JN, Varnum SM, Auberry KJ, et al. Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. Mol Cell Proteomics 2002;1:947–955.
Nayak SS, Kamath SS, Kundaje GN, Aroor AR. Diagnostic significance of estimation of serum apolipoprotein A along with alpha-fetoprotein in alcoholic cirrhosis and hepatocellular carcinoma patients. Clin Chim Acta 1988; 173: 157–164.
Matsuura T, Koga S, Ibayashi H. Increased proportion of proapolipoprotein A-I in HDL from patients with liver cirrhosis and hepatitis. Gastroenterol Jpn 1988;23:394–400.
Fujii S, Koga S, Shono T, Yamamoto K, Ibayashi H. Serum apoprotein A-I and A-II levels in liver diseases and cholestasis. Clin Chim Acta 1981;115:321–331.
Steel LF, Shumpert D, Trotter M, et al. A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma. Proteomics 2003;3:601–609.
Tachibana M, Ohkura Y, Kobayashi Y, et al. Expression of apolipoprotein A1 in colonic adenocarcinoma. Anticancer Res 2003;23:4161–4167.
Hellman K, Alaiya AA, Schedvins K, Steinberg W, Hellstrom AC, Auer G. Protein expression patterns in primary carcinoma of the vagina. Br J Cancer 2004;91:319–326.
Zhang Z, Bast RC Jr, Yu Y, et al. Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer. Cancer Res 2004; 64:5882–5890.
Kuesel AC, Kroft T, Prefontaine M, Smith IC. Lipoprotein(a) and CA125 levels in the plasma of patients with benign and malignant ovarian disease. Int J Cancer 1992;52:341–346.
Gade D, Thiermann J, Markowsky D, Rabus R. Evaluation of two-dimensional difference gel electrophoresis for protein profiling. Soluble proteins of the marine bacterium Pirellula sp. strain 1. J Mol Microbiol Biotechnol 2003;5:240–251.
Zhou G, Li H, DeCamp D, et al. 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers. Mol Cell Proteomics 2002;1:117–124.
Gharbi S, Gaffney P, Yang A, et al. Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol Cell Proteomics 2002; 1:91–98.
Friedman DB, Hill S, Keller JW, et al. Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry. Proteomics 2004;4:793–811.
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© 2007 Humana Press Inc., Totowa, NJ
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Hegmans, J., Hemmes, A., Lambrecht, B. (2007). Proteomics of Pleural Effusion. In: Thongboonkerd, V. (eds) Proteomics of Human Body Fluids. Humana Press. https://doi.org/10.1007/978-1-59745-432-2_13
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DOI: https://doi.org/10.1007/978-1-59745-432-2_13
Publisher Name: Humana Press
Print ISBN: 978-1-58829-657-3
Online ISBN: 978-1-59745-432-2
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