TY - JOUR AU - Milcheva, Rositsa S. AU - Georgieva, Any K. AU - Todorova, Katerina S. AU - Petkova, Svetlozara L. PY - 2022/02/23 Y2 - 2024/03/28 TI - Expression of sialyltransferases from the St3gal, St6gal and St6galnac families in mouse skeletal muscle and mouse C2C12 myotubes JF - Acta Biologica Szegediensis JA - Acta Biol Szeged VL - 65 IS - 2 SE - Articles DO - 10.14232/abs.2021.2.253-261 UR - https://abs.bibl.u-szeged.hu/index.php/abs/article/view/3250 SP - 253-261 AB - <p style="text-align: justify;">In skeletal muscles, the sialic acids have a great significance for their functional maintenance and proper structural organization. Our work described the expressions of <em>St3gal</em>, <em>St6gal</em> and <em>St6galnac</em> sialyltransferases specific for glycoproteins in mouse skeletal muscles and murine C2C12 myotubes. Lectin histochemistry, cytochemistry and lectin blot were used to demonstrate the membrane localization and the electrophoretic profiles of α-2,3- and α-2,6-sialylated glycoproteins. The expression levels of sialyltransferases were analysed by real time RT-PCR and western blot. The enzymes <em>St6gal2</em> and<em> St6galnac1</em> were not expressed in skeletal muscle tissue and C2C12 myotubes. In both experimental groups, mRNAs of the <em>St3gal</em> family prevailed over the mRNA expressions of the <em>St6gal</em> and <em>St6galnac</em> families. The profiles of sialyltransferase expressions showed differences between the two experimental groups, illustrated by the absence of expressions of the mRNA for the <em>St3gal6</em> and <em>St6galnac3</em> genes in the C2C12 cell samples and by the different shares of the enzymes <em>St3gal3</em> and <em>St3gal4</em> in both experimental groups. The different patterns of enzyme expressions in both experimental groups corresponded with differences between their α-2,3- and α-2,6-sialylated glycoprotein profiles. These results could be a useful addendum to the knowledge concerning the glycosylation of the skeletal muscle tissue.</p> ER -