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J Biol Chem, Vol. 273, Issue 51, 34586-34593, December 18, 1998
From the Department of Biochemistry and Molecular Biology,
University of Illinois College of Medicine,
Chicago, Illinois 60612
A select group of mammalian proteins have been
shown to possess 
2,8-polysialylated oligosaccharide chains. The best
studied of these proteins is the neural cell adhesion molecule (NCAM). Polysialylation of NCAM has been shown to decrease
NCAM-dependent and independent cell adhesion. PST (ST8Sia
IV) and STX (ST8Sia II) are the two polysialyltransferases responsible
for NCAM polysialylation. Recent studies revealed that PST itself is
autopolysialylated in vitro (Muhlenhoff, M., Eckhardt, M.,
Bethe, A., Frosch, M., and Gerardy-Schahn, R. (1996) EMBO J. 15, 6943-6950). Here we report studies on the biosynthesis and
localization of the PST and STX polysialyltransferases. Both PST and
STX are expressed as high molecular mass, polydisperse forms that are
associated with the cell and found soluble in the medium. Analysis of
these high molecular mass forms by glycosidase digestion and serial immunoprecipitation/immunoblot experiments demonstrated that PST and
STX are autopolysialylated in vivo. Indirect
immunofluorescence microscopy and immunoprecipitation analyses
demonstrated that autopolysialylated PST and STX are localized in the
Golgi, on the cell surface, and in the extracellular space. The cell
surface and extracellular localization of these polysialylated
polysialyltransferases suggest that their polysialic acid chains, like
those of NCAM, may modulate cell interactions.
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