Effects of UDP-glucose addition on the synthesis of mannosyl lipid-linked oligosaccharides by cell-free fibroblast preparations.

Robbins, Phillips W.; Krag, Sharon S.; Liu, T

doi:10.1016/s0021-9258(17)40618-1

Cited by 81 publications

(3 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taken together with the above data, the results indicate a Glc3Man7GlcNAc structure as presented in Figure 11. This structure is consistent with the structure proposed for the Glc3Man9GlcNAc2 isolated from the lipid-linked oligosaccharides (Li & Kornfeld, 1979;Robbins et al, 1977) and also with our observation that castanospermine inhibits glucosidase I, in vitro (see below).…”

Section: Resultssupporting

confidence: 92%

Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutinin

Pan¹,

Hori²,

Saul³

et al. 1983

Biochemistry

252

128

View full text Add to dashboard Cite

Castanospermine (1,6,7,8-tetrahydroxyoctahydroindolizine) is a plant alkaloid that inhibits alpha- and beta-glucosidase in fibroblast extracts [Saul, R., Chambers, J. P., Molyneux, R. J., & Elbein, A. D. (1983) Arch. Biochem. Biophys. 221, 593-597]. In the present study, castanospermine also proved to be a potent inhibitor of glycoprotein processing by virtue of the fact that it inhibits glucosidase I. Thus, when influenza virus was raised in the presence of castanospermine, at 10 micrograms/mL or higher, 80-90% of the viral glycopeptides were susceptible to the action of endoglucosaminidase H, whereas in the normal virus 70% of the glycopeptides are resistant to this enzyme. The major oligosaccharide released by endoglucosaminidase H from castanospermine-grown virus migrated like a hexose10GlcNac on a calibrated Bio-Gel P-4 column. This oligosaccharide was characterized as a Glc 3 Man 7 GlcNAc on the basis of various enzymatic treatments, as well as by methylation analysis of the [2-3H]-mannose-labeled or [6-3H]galactose-labeled oligosaccharide. The presence of three glucose residues in the oligosaccharide was also confirmed by periodate oxidation studies of the [6-3H]galactose-labeled hexose10GlcNAc. Castanospermine did not inhibit the incorporation of [3H]leucine or [14C]alanine into protein in MDCK cells at levels as high as 50 micrograms/mL. In addition, influenza virus produced in the presence of this alkaloid were fully infective and apparently produced in similar amounts to that of control cells, as determined by plaque counts. Castanospermine did, however, cause considerable changes in cell surface properties, since MDCK cells grown in 10 micrograms/mL castanospermine were able to bind twice as much [3H]concanavalin A as were control cells.

show abstract

Section: Resultssupporting

confidence: 92%

Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutinin

Pan¹,

Hori²,

Saul³

et al. 1983

Biochemistry

252

128

View full text Add to dashboard Cite

show abstract

“…Glucose was detected in similar amounts in two separate preparations of the CSP multimer. It should be of interest to determine its structural significance, since glucose is generally found only in collagen-like proteins or in precursor oligosaccharides (Spiro et al, 1976;Robbins et al, 1977). It is likely that the glucose or mannose residues account for the ability of CSP to bind concanavalin A (Olden and Yamada, 1977a;Burridge, 1976).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a major fibroblast cell surface glycoprotein

Yamada¹,

Schlesinger²,

Kennedy³

et al. 1977

Biochemistry

178

View full text Add to dashboard Cite

“…These structures are basically in agreement with the biosynthetic scheme proposed earlier by Behrens et al (1973) in which the lipid-linked mannosylated oligosaccharide was elongated by the addition of two glucose residues. In a related experiment Robbins et al (1977) have obtained evidence for the incorporation of glucose into a mannosylated oligosaccharide lipid formed by cell-free preparations from fibroblasts. Enzymatic studies with rat liver microsomes (Parodi et al, 1972) and pulse-chase experiments…”

mentioning

confidence: 98%

Biosynthesis of glucosylated derivatives of dolichol: possible intermediates in the assembly of white matter glycoproteins

Scher¹,

Jochen²,

Waechter³

1977

Biochemistry

View full text Add to dashboard Cite

Effects of UDP-glucose addition on the synthesis of mannosyl lipid-linked oligosaccharides by cell-free fibroblast preparations.

Cited by 81 publications

References 13 publications

Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutinin

Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutinin

Characterization of a major fibroblast cell surface glycoprotein

Biosynthesis of glucosylated derivatives of dolichol: possible intermediates in the assembly of white matter glycoproteins

Contact Info

Product

Resources

About