Isolation and Characterization of Proteoglycans Synthesized by Rat Myoblasts L6J1 in Culture

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I. I. Ermakova^1*, A. L. Mokrushin^1,2, T. A. Chertkova¹, G. A. Sakuta¹, A. V. Romaniouk³, and V. I. Morozov^1,2

¹Department of Cell Cultures, Institute of Cytology, Russian Academy of Sciences, Tikhoretskii pr. 4, 194064 St. Petersburg, Russia; fax: (812) 297-0341; E-mail: irinabiochem@mail.ru; sakuta@mail.cytspb.rssi.ru

²St. Petersburg Research Institute of Physical Culture, pr. Dynamo 2, 197110 St. Petersburg, Russia; fax: (812) 237-0461; E-mail: office@spbniifk.ru

³Department of Biochemistry, St. Petersburg State University, Universitetskaya Nab. 7/9, 199034 St. Petersburg, Russia; fax: (812) 328-9788; E-mail: avr@hotmail.com

^* To whom correspondence should be addressed.

Received November 27, 2006; Revision received January 15, 2007

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Proteoglycans synthesized by rat myoblasts L6J1 in culture were isolated using sorbent Q-Sepharose from culture medium, extracellular matrix (ECM), and cells. Elution of the sorbed material in a NaCl gradient separated proteoglycans from the bulk of proteins eluted at low concentration of the salt. Four fractions (fractions I-IV) were obtained for each component of the cell culture, including two proteoglycan fractions for the ECM and culture medium and one fraction for the myoblasts. Proteoglycans of the culture medium were virtually completely represented by proteoglycans of fetal calf serum. With enzymes chondroitinase ABC and heparinase III chondroitin/dermatan sulfate proteoglycans were shown to prevail in all components of the myoblast culture. The core proteins of proteoglycans were characterized by electrophoresis.

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KEY WORDS: proteoglycans, myoblasts

DOI: 10.1134/S000629790704013X

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