ALTERATION OF TERMINAL GLYCOSYLATION SEQUENCES ON N-LINKED OLIGOSACCHARIDES OF CHINESE-HAMSTER OVARY CELLS BY EXPRESSION OF BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE

  • 15 August 1989
    • journal article
    • research article
    • Vol. 264  (23) , 13848-13855
Abstract
In this report we describe the alteration of the N-linked oligosaccharide terminal sequences of Chinese hamster ovary cell glycoproteins by expression of a .beta.-galactoside .alpha.2,6-sialyltransferase cDNA. While wild type cells normally produce sugar chains terminating in the NeuAc.alpha.2,3Gal linkage, the expressed enzyme competes with the endogenous sialyltransferase to attach an alternative terminal sequence, NeuAc.alpha.2,6Gal. Subcellular localization of the NeuAc.alpha.2,6Gal product by lectin-gold electron microscopy revealed localization throughout the Golgi apparatus cis to trans, post-Golgi membranes and vesicular structures. The results demonstrate the potential for purposefully altering terminal carbohydrate structures in vivo by "mis-expressing" terminal glycosyltransferases that compete with the endogenous enzyme normally produced by the cells.

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