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

FEBS Letters

Töpfer-Petersen, Edda⁴  Sanz, Libia⁴  Calvete, Juan J.⁴  Scheit, Karl-Heinz¹  Raida, Manfred³  Wempe, Frank¹  Romero, Antonio² 

[1] Max-Plank-Institut für biophysikalische Chemie, Göttingen, Germany;Instituto de Química-Física ‘Rocasolano’ CSIC, Madrid, Spain;Niedersächsisches Institut für Peptid-Forschung GmbH, Hannover, Germany;Institut für Reproduktionsmedizin, Tierärztliche Hochschule, Hannover, Germany

关键词: Bovine seminal plasma;    PDC-109;    Heparin-binding protein;    O-Glycosylation;    Mass spectrometry;   

DOI  :  10.1016/0014-5793(94)00768-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Thr¹¹. 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) × 10⁶ molecules of PDC-109/cell. This value remained constant in swim-up sperm and decreased to (7.7 ± 0.4) × 10⁶/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.

【 授权许可】

Unknown