PMID: 7372591May 25, 1980Paper

Synthesis of a novel class of sulfated glycoproteins in embryonic liver and lung.

The Journal of Biological Chemistry
A HeifetzW J Lennarz

Abstract

Slices from various organs and tissues of 14-day-old chick embryos synthesize a novel class of glycoproteins containing sulfated oligosaccharide chains that are not released from the polypeptides under conditions that cleave O-glycosidically linked chains. Of the tissues examined, embryonic lung and liver were the most active in incorporating [35S]O4 into these oligosaccharide chains, which were analyzed as glycopeptides following Pronase digestion. These low molecular weight sulfated glycopeptides were resistant to several chemical and enzymatic treatments that degrade a variety of high molecular weight sulfated glycosaminoglycans. The incorporation of both [3H]glucosamine and [35S]O4 into the glycopeptides was inhibited by tunicamycin, an antibiotic which inhibits the N-glycosylation of proteins. These observations, coupled with the finding that these chains were resistant to beta elimination, suggest that this novel type of sulfated oligosaccharide is N-glycosidically linked to protein. The sulfated glycopeptides from chick embryonic lung were characterized as containing terminal fucose and sialic acid residues as well as O-sulfated N-acetylglucosamine residues. Comparable studies with slices of adult liver and lung indicate...Continue Reading

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