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Title: A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina

Journal Article · · Cell; (United States)

A subclass of cell-surface glycoproteins from embryonic chicken neural retina contains a high mannose-type oligosaccharide that terminates with glucose linked via a phosphodiester bond to penultimate mannose. This unusual oligosaccharide seems responsible for the glycoprotein attachments to the cell-surface baseplate ligatin. Using beta-/sup 32/P-UDP-/sup 3/H-glucose, we demonstrate in retinal homogenates the existence of a UDP-glucose:glycoprotein glucose-1-phosphotransferase (GlcPTase) that catalyzes the synthesis of such a linkage. Characterization of the doubly labeled product resulting from activity of the transferase reveals a family of endoglycosidase H-sensitive oligosaccharides displaying a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo. Further analysis confirms that the incorporation of label is due to a terminal /sup 3/H-glucose joined via a /sup 32/P-phosphodiester linkage to carbon 6 of a penultimate mannose. We propose that GlcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface.

Research Organization:
Department of Anatomy, Duke University Medical Center, Durham, North Carolina
OSTI ID:
6225819
Journal Information:
Cell; (United States), Vol. 31:3
Country of Publication:
United States
Language:
English