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 Lett. 1994 Aug 22;350(2-3):203-6. doi: 10.1016/0014-5793(94)00768-3.

Abstract

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 (NeuNAc alpha(2-6)-Gal beta(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) x 10(6) molecules of PDC-109/cell. This value remained constant in swim-up sperm and decreased to (7.7 +/- 0.4) x 10(6)/spermatozoon after incubation for 24 h in capacitation medium at 39 degrees 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbohydrate Sequence
  • Cattle
  • Gas Chromatography-Mass Spectrometry
  • Glycoproteins / chemistry
  • Male
  • Molecular Sequence Data
  • Oligosaccharides / chemistry
  • Peptide Fragments / chemistry
  • Prostatic Secretory Proteins*
  • Proteins / chemistry*
  • Semen / chemistry
  • Seminal Plasma Proteins
  • Spermatozoa / chemistry*

Substances

  • Glycoproteins
  • Oligosaccharides
  • Peptide Fragments
  • Prostatic Secretory Proteins
  • Proteins
  • Seminal Plasma Proteins
  • beta-microseminoprotein