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Localization and structural characterization of an oligosaccharide O‐linked to bovine PDC‐109 Quantitation of the glycoprotein in seminal plasma and on the surface of ejaculated and capacitated spermatozoa
Author(s) -
Calvete Juan J.,
Raida Manfred,
Sanz Libia,
Wempe Frank,
Scheit Karl-Heinz,
Romero Antonio,
Töpfer-Petersen Edda
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00768-3
Subject(s) - capacitation , spermatozoon , glycoprotein , sperm , chemistry , semen , heparin , oligosaccharide , glycosaminoglycan , incubation , andrology , biochemistry , biology , in vitro , anatomy , medicine
PDC‐109 (13 kDa) is the most abundant component, and the major heparin‐binding protein, of bovine ( Bos taurus ) seminal plasma. Here, we show that PDC‐109 contains a single O‐linked oligosaccharide (NeuNAcα(2–6)‐Galβ(1–3)‐GalNAc‐) attached to Thr 11 . Immunoquantitation of PDC‐109 indicates that its concentration in seminal plasma is 15–20 mg/ml. Though PDC‐109 is not present on epididymal sperm, ejaculated spermatozoa on average are coated with (9.5 ± 0.3) × 10 6 molecules of PDC‐109/cell. This value remained constant in swim‐up sperm and decreased to (7.7 ± 0.4) × 10 6 /spermatozoon after incubation for 24 h in capacitation medium at 39°C. These data substantiate the hypothesis that PDC‐109 may be one of the seminal plasma components that enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin‐like glycosaminoglycans present in the female genital tract.