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Expression of Different Proteoglycans in Human Breast Tumors


T. Yu. Eshchenko1*, V. I. Rykova2, A. E. Chernakov3, S. V. Sidorov3, and E. V. Grigorieva1

1Institute of Molecular Biology and Biophysics, Siberian Branch of the Russian Academy of Medical Sciences, ul. Akademika Timakova 2, 630117 Novosibirsk, Russia; fax: (383) 332-3147; E-mail: Tatiana_E@ngs.ru

2Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, ul. Akademika Lavrentieva 10, 630090 Novosibirsk, Russia; fax: (383) 333-1277; E-mail: Dymshits@niboch.nsc.ru

31st Municipal Clinical Hospital, ul. Zalesskogo 6, 630047 Novosibirsk, Russia

* To whom correspondence should be addressed.

Received April 18, 2007; Revision received May 15, 2007
The composition of proteoglycans and their changes during malignant transformation are important factors influencing adhesive properties and mitotic activity of tumor cells. In this study, expression level of different proteoglycans (decorin, syndecan-1, lumican, glypican-1, and aggrecan) in tumors and normal human breast tissue was investigated. Multiplex RT-PCR data revealed different expression changes for different proteoglycans in human breast tumors--syndecan expression was activated compared to almost no expression in normal breast tissue, expression of decorin and lumican decreased 2-5- and 2-3-fold, respectively, and aggrecan transcription seems to be unaffected. A change of expression level of decorin correlated with expression of D-glucuronyl-C5-epimerase, a key enzyme responsible for the biosynthesis of idurone-containing glycosaminoglycans, possessing antimitotic activity. The results suggest that changes in decorin, lumican, and syndecan-1 expession in tumor tissue could induce a distortion of proteoglycan composition and mitotic activity of cells in human breast tumor.
KEY WORDS: breast cancer, proteoglycans, D-glucuronyl-C5-epimerase, proteoglycan biosynthesis

DOI: 10.1134/S0006297907090143