Abstract
Objective: ST6 beta-galactosamide α-2,6-sialyltranferase 1 (ST6GAL1), the major α2,6- sialyltransferase responsible for the broad synthesis of glycoproteins and glycolipids, is another physiological substrate of Beta site APP-cleaving enzyme 1 (BACE1) other than amyloidbeta 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.
Highlights
Skeletal muscle is one of the known tissues marked by the intracellular accumulation of the amyloid-beta (Abeta) peptide [1]
In this study we investigated whether amyloid-beta precursor protein (AbetaPP) induced ST6GAL1 secretion from C2C12 cells affect proinflammatory cytokine production by J774 mouse macrophage cell line
Our previous studies revealed that AbetaPP overexpression in C2C12 cells increased the expression and secretion of ST6GAL1 enzyme, another physiological substrate of Beta site APP-cleaving enzyme 1 (BACE1) enzyme other than AbetaPP, under in vitro conditions [15]
Summary
Skeletal muscle is one of the known tissues marked by the intracellular accumulation of the amyloid-beta (Abeta) peptide [1]. Beta secretase-1 (BACE1) known as Beta site APP-cleaving enzyme 1 is one of the glycosylated transmembrane β-secretases that mediates the primary amyloidogenic cleavage of AbetaPP [6,7]. It has been involved in the proteolytic processing of a Golgi-resident sialyltransferase, namely, ST6 beta-galactosamide α-2,6-sialyltranferase 1 (ST6GAL1) which is probably the most extensively studied sialyltransferase among the eukaryotic sialyltransferases [8,9]
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