Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma

Abstract

Background: The degree of branching and types of fucosylation of glycans on alpha(1)-acid glycoprotein (AGP) have been found to be associated with alpha(1)-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of alpha(1)-acid glycoprotein in seminal plasma obtained from men living in infertile couples can undergo alterations in relation to sperm analysis and/or alpha(1)-acid glycoprotein concentrations.

Methods: The glycosylation of alpha(1)-acid glycoprotein was studied upon the reactivity with specific lectins by crossed affinity immunoelectrophoresis (concanavalin A), and by glycoprotein lectin immunosorbent assay (Maackia amurensis and Sambucus nigra lectins), as well as high pH anion-exchange chromatography with pulsed amperometric detection.

Results: Nonsignificant differences in alpha(1)-acid glycoprotein glycan branching and degree of its sialylation were observed among the AGP derived from seminal plasmas in relation to spermiogram and sperm morphology. However, significant concentration-dependent differences were found in extent of branching and type of sialylation.

Conclusions: The presence in seminal plasma of high concentrations of aberrantly glycosylated AGP molecules might be indicative for a chronic inflammatory condition in the reproductive tract, and can be used as additional tool to subdivide the seminal plasmas of men living in infertile couples.