PROTEOGLYCANS OF L6J1 MYOBLAST EXTRACELLULAR MATRIX. CHARACTERISTICS AND EFFECT ON MYOBLAST ADHESION
I. I. Ermakova,1, 2, * T. A. Chertkova,1 A. L. Mokrushin,1
A. V. Romaniouk,3 G. A. Sakuta,1 V. I. Morozov 1, 4
1 Institute of Cytology RAS, 2 I. P. Pavlov Institute of Physiology RAS, St. Petersburg,
3 Department of Biochemistry, St. Petersburg State University, and
4 St. Petersburg Scientific Research Institute of Physical Culture;
e-mail: * irinabiochem@mail.ru
Proteoglycans were isolated from extracellular matrix of L6J1 rat myoblasts and their influence on myoblast adhesion was studied. Proteoglycan digestion with
chondroitinase AC and heparinase III degrading the polysaccharide moieties revealed that chondroitin sulfate proteoglycans are the main class of myoblast
extracellular matrix proteoglycans. Electrophoresis of enzymatically processed proteoglycans was used to examine their core proteins. Myoblast adhesion was
suppressed by proteoglycans or the mixture of proteoglycans and fibronectin/extracellular matrix. When being processed with chondroitinase AC the combined
substrate of fibronectin and proteoglycans lost the capability of myoblast adhesion suppression. Thus, as a result of presented work the proteoglycans of L6J1 rat
myoblast extracellular matrix were isolated and purified. The main class of prote-oglycans was chondroitin sulphate proteoglycans. Isolated proteoglycans
suppressed myoblast adhesion and this effect was mediated by polysaccharide moieties of proteoglycans.
Key words: myoblasts, extracellular matrix, proteoglycans, chondroitin sulfate, adhesion
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