Overexpression of amyloid beta precursor protein enhances expression and secretion of ST6Gal1 in C2C12 myogenic cell line.


BALCI-HAYTA B., Erdem-Ozdamar S. , DINCER P. R.

Cell biology international, vol.35, no.1, pp.9-13, 2011 (Journal Indexed in SCI Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 35 Issue: 1
  • Publication Date: 2011
  • Doi Number: 10.1042/cbi20100159
  • Title of Journal : Cell biology international
  • Page Numbers: pp.9-13

Abstract

The Abeta (amyloid-beta) peptide is derived from the sequential cleavage of AbetaPP (amyloid-beta precursor protein) by two enzymes, the beta- and gamma-secretases. The major beta-secretase, identified as the novel transmembrane aspartic protease BACE1 (beta site APP-cleaving enzyme 1), mediates the primary amyloidogenic cleavage of AbetaPP and initiates the production of Abeta. It has been implicated in the proteolytic processing of another substrate, namely ST6Gal1 (beta galactoside alpha 2,6-sialyltransferase 1), which is the major alpha 2,6-sialyltransferase responsible for the broad synthesis of glycoproteins and glycolipids. The present study investigated the effect of overexpression of AbetaPP on expression and secretion of ST6Gal1 in skeletal muscle cells by inducing overexpression of wild-type full-length 751-AbetaPP in the mouse myogenic cell line C2C12. Expression and secretion of the ST6Gal1 enzyme were analysed by Western blot and/or immunofluorescence staining. The results of our study demonstrated that AbetaPP overexpression in 02012 cells increased the expression and the secretion of ST6Gal1 enzyme in vitro.