PMID: 6413506Oct 10, 1983Paper

Abnormal glycosylation of human cellular fibronectin in the presence of swainsonine.

The Journal of Biological Chemistry
R G Arumugham, M L Tanzer

Abstract

The relationship between post-translational modifications of macromolecules and their intracellular routing is of fundamental importance. The availability of the indolizidine alkaloid, swainsonine, which interferes with glycoprotein processing, provides a new probe for studying relationships between glycosylation of proteins and their cellular routing. Using fibronectin as a model glycoprotein, we have explored the effect of swainsonine upon oligosaccharide structure, glycoprotein synthesis, and secretion. Confluent human fibroblasts were labeled with radioactive mannose or glucosamine in the presence or absence of swainsonine. Fibronectin was secreted into the medium of swainsonine-treated cultures and found to contain endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharides, instead of the normal complex endo-beta-N-acetylglucosaminidase H-resistant oligosaccharides. Pronase-released glycopeptides and hydrazine-released oligosaccharides of isolated fibronectin from the culture media were analyzed using endo-beta-N-acetylglucosaminidase H and specific exoglycosidase digestions in conjunction with calibrated gel filtration chromatography. The structure of the swainsonine-modified endo-beta-N-acetylglucosaminidase H-sensit...Continue Reading

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