Differential sialylation regulates the apoptotic activity of glycodelin A.
Glycodelin A (GdA), a dimeric lipocalin, expressed by the uterine endometrium, is an immunomodulatory agent and induces apoptosis in T-cells. In this study we demonstrate that two populations of GdA with subtle differences in their net ionic charge are present in the amniotic fluid and that, apoptotic activity is exhibited only by the population with more sialic acid residues. Significantly, removal of sialic acid residues from the active populations of GdA abrogates the activity of the molecule, suggesting that the extent of sialylation might be a factor regulating the activity of GdA.
Poornima
B Lakshmanamurthy
BL
Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India.
Karande
Anjali A
AA
D000653:Amniotic Fluid / Q000737:chemistry; D017209:Apoptosis / Q000187:drug effects; D003956:Dialysis; D005260:Female; D000071816:Glycodelin; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D019169:Jurkat Cells; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism; D011257:Pregnancy Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D013601:T-Lymphocytes / Q000166:cytology / Q000187:drug effects
D000071816:Glycodelin; D006023:Glycoproteins; C045246:PAEP protein, human; D011134:Polysaccharides; D011257:Pregnancy Proteins; D019158:N-Acetylneuraminic Acid