A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina
Abstract
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.
- Authors:
- Publication Date:
- Research Org.:
- Department of Anatomy, Duke University Medical Center, Durham, North Carolina
- OSTI Identifier:
- 6225819
- Resource Type:
- Journal Article
- Journal Name:
- Cell; (United States)
- Additional Journal Information:
- Journal Volume: 31:3
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; PHOSPHORUS 32; TRACER TECHNIQUES; PHOSPHOTRANSFERASES; ENZYME ACTIVITY; RETINA; BIOCHEMISTRY; TRITIUM COMPOUNDS; CHICKENS; EMBRYOS; NERVE CELLS; OLIGOSACCHARIDES; STRUCTURAL CHEMICAL ANALYSIS; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BIRDS; BODY; BODY AREAS; CARBOHYDRATES; CHEMISTRY; DAYS LIVING RADIOISOTOPES; ENZYMES; EYES; FACE; FOWL; HEAD; ISOTOPE APPLICATIONS; ISOTOPES; LABELLED COMPOUNDS; LIGHT NUCLEI; NUCLEI; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; RADIOISOTOPES; SACCHARIDES; SENSE ORGANS; SOMATIC CELLS; TRANSFERASES; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Koro, L A, and Marchase, R B. A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina. United States: N. p., 1982.
Web. doi:10.1016/0092-8674(82)90328-2.
Koro, L A, & Marchase, R B. A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina. United States. https://doi.org/10.1016/0092-8674(82)90328-2
Koro, L A, and Marchase, R B. 1982.
"A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina". United States. https://doi.org/10.1016/0092-8674(82)90328-2.
@article{osti_6225819,
title = {A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina},
author = {Koro, L A and Marchase, R B},
abstractNote = {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.},
doi = {10.1016/0092-8674(82)90328-2},
url = {https://www.osti.gov/biblio/6225819},
journal = {Cell; (United States)},
number = ,
volume = 31:3,
place = {United States},
year = {Wed Dec 01 00:00:00 EST 1982},
month = {Wed Dec 01 00:00:00 EST 1982}
}