Identification of Proteins Overexpressed in Papillary Thyroid Tumors

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L. V. Sipina^1*, Yu. A. Bukurova², I. G. Nikitina², G. S. Krasnov², S. A. Sergeev³, N. A. Lisitsyn², V. L. Karpov², and S. F. Beresten²

¹Clinical Research Center PreMed, ul. Veresaeva 1, 121357 Moscow, Russia; fax: (495) 443-9031; E-mail: larsipina@rambler.ru

²Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, 119991 Moscow, Russia; fax: (499) 135-0468; E-mail: sberesten@gmail.com; niklisitsyn@yahoo.com

³City Oncology Hospital No. 62, 143423 Stepanovskoe, Krasnogorsk District, Moscow Region, Russia; fax: (495) 561-2312; E-mail: info@onco62.ru

^* To whom correspondence should be addressed.

Received December 8, 2009; Revision received March 26, 2010

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A modified method of proteome comparative analysis based on preliminary removal of cell structural proteins by extraction using salt buffer and subsequent separation of extracts by two-dimensional gel electrophoresis was developed. Identification of differentially expressed proteins by mass spectrometry has revealed three proteins with noticeably increased level of synthesis in most samples of papillary thyroid tumors compared to normal tissues. An increase in ubiquitin content was found for the first time. Oncomarker search efficiencies by two-dimensional gel electrophoresis and bioinformatic search were compared.

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KEY WORDS: differential proteomics, two-dimensional gel electrophoresis, thyroid cancer, protein oncomarkers

DOI: 10.1134/S0006297910090087

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