Glycobiology Advance Access published online on July 19, 2006
Glycobiology, doi:10.1093/glycob/cwl024
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1 Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India
* To whom correspondence should be addressed. GlycodelinA, a multi functional glycoprotein secreted at high concentrations by the uterine endometrium during the early phases of pregnancy, carries glycan chains on asparagines at positions N28 and N63. GlycodelinA purified from amniotic fluid is known to be a suppressor of T cell proliferation, an inducer of T cell apoptosis and an inhibitor of sperm-zona binding in contrast to its glycoform, glycodelinS, which is secreted by the seminal vesicles into the seminal plasma. The oligosaccharide chains of glycodelinA terminate in sialic acid residues while those of glycodelinS are not sialylated but are heavily fucosylated. Our previous work has shown that the apoptogenic activity of glycodelinA resides in the protein backbone and we have also demonstrated the importance of sialylation for the manifestation of glycodelinA induced apoptosis. Recombinant glycodelin expressed in the Sf21 insect cell line yielded an apoptotically active glycodelin; however, the same gene expressed in the insect cell line Tni produced apoptotically inactive glycodelin, as observed with the gene expressed in the Chinese hamster ovary cell line, and earlier in Pichia pastoris. Glycan analysis of the Tni and Sf21 cell line expressed glycodelin proteins reveals differences in their glycan structures, which modulate the manifestation of apoptogenic activity of glycodelin. Through apoptotic assays carried out with the wild type and glycosylation mutants of glycodelin expressed in Sf21 and Tni cells before and after mannosidase digestion, we conclude that the accessibility to the apoptogenic region of glycodelin is influenced by the size of the glycans.
Received March 31, 2006
Revised July 10, 2006
Accepted July 11, 2006
Article
Oligosaccharides modulate the apoptotic activity of glycodelin
Rajesh Jayachandran 1, Catherine M Radcliffe 2, Louise Royle 2 
, David J Harvey 2 , Raymond A Dwek 2 , Pauline M Rudd 2 , and Anjali A Karande 1 *
2 Glycobiology Institute, Oxford University, Oxford, OX1 3QU, United Kingdom
Anjali A Karande, E-mail: anjali{at}biochem.iisc.ernet.in
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