TURKISH JOURNAL OF BIOCHEMISTRY-TURK BIYOKIMYA DERGISI, vol.40, no.1, pp.31-36, 2015 (SCI-Expanded)
Objective: ST6 beta galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), the major alpha 2,6-sialyltransferase responsible for the broad synthesis of glycoproteins and glycolipids, is another physiological substrate of Beta site APP-cleaving enzyme 1 (BACE1) other than amyloid-beta precursor protein (AbetaPP). We have previously shown that AbetaPP overexpression in C2C12 mouse myoblast cell line increased the expression and secretion of ST6GAL1 enzyme under in vitro conditions. Since the secretion of ST6GAL1 is known to be enhanced during inflammation, we investigated whether AbetaPP induced ST6GAL1 secretion from C2C12 cells affected proinflammatory cytokine production by J774 mouse macrophage cell line.