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Requirement of N-glycosylation for the Secretion of Recombinant Extracellular Domain of Human Fas in HeLa Cells

Requirement of N-glycosylation for the Secretion of Recombinant Extracellular Domain of Human Fas in HeLa Cells

Yi Li, Xiaojing Yang, Alana H T Nguyen, Inka Brockhausen

Int J Biochem Cell Biol. 2007;39(9):1625-36.

PMID: 17544837

Abstract:

Apoptosis has been shown to be associated with altered glycosylation patterns and biosynthesis of glycoproteins. A major cell surface receptor involved in the induction of apoptosis is Fas that is activated by binding Fas ligand but can also be activated by binding anti-Fas antibody. In order to determine whether the Fas receptor is glycosylated, the extracellular domain of human Fas (shFas) was expressed as a cleavable fusion protein (shFas-Fc) in HeLa cells. These cells were shown to express activities of glycosyltransferases involved in N- and O-glycan biosynthesis. The secreted shFas-Fc was shown to be a glycoprotein with heterogeneous glycan chains. MALDI mass spectrometry revealed a disperse molecular weight of shFas with an average of 23.4kDa. Western blots of shFas-Fc secreted from tunicamycin treated transfected HeLa cells showed that only N-glycosylated glycoforms were secreted, while the unglycosylated shFas-Fc remained intracellular. The results suggest that both N-glycosylation sites of the extracellular domain of Fas are occupied with large N-glycans that play a role in the expression of the glycoprotein.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42412938	Fas Intracellular Domain human			Price

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