Inhibition of protein synthesis also inhibits synthesis of lipid-linked oligosaccharides.
Studies were initiated to determine whether the formation of lipid-linked oligosaccharides was coupled to the synthesis of protein. Canine kidney cells were grown with [2-3H]mannose or [3H]leucine in the presence of cycloheximide or puromycin and the effect of these inhibitors on the synthesis of proteins and lipid-linked oligosaccharides was measured. In all cases, the inhibition of protein synthesis resulted in a substantial inhibition in the incorporation of mannose into the lipid-linked oligosaccharides, although the synthesis of mannosyl-phosphoryl-dolichol was only slightly inhibited. Cycloheximide had no effect on the in vitro incorporation of mannose into lipid-linked oligosaccharides when GDP-[14C]mannose was incubated with aorta microsomal preparations. The inhibition of lipid-linked oligosaccharides was apparently not due to a decrease in the amount of glycosyltransferases as a result of protein degradation in the absence of protein synthesis, nor was it the result of a more rapid degradation of lipid-linked oligosaccharides. The inhibition also did not appear to be due to limitations in the available dolichyl-phosphate. The results suggest that the formation of lipid-linked oligosaccharides may be regulated by end product inhibition.
Duke Scholars
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Related Subject Headings
- Puromycin
- Protein Biosynthesis
- Polyisoprenyl Phosphate Sugars
- Oligosaccharides
- Mannose
- Leucine
- Kinetics
- Kidney
- Glycoproteins
- Glycolipids
Citation
Published In
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Puromycin
- Protein Biosynthesis
- Polyisoprenyl Phosphate Sugars
- Oligosaccharides
- Mannose
- Leucine
- Kinetics
- Kidney
- Glycoproteins
- Glycolipids