The Pattern of Tyrosine Phosphorylation in Human Sperm in Response to Binding to Zona Pellucida or Hyaluronic Acid


Creative Commons License

Sati L., Cayli S., Delpiano E., Sakkas D., Huszar G.

REPRODUCTIVE SCIENCES, cilt.21, sa.5, ss.573-581, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 21 Sayı: 5
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1177/1933719113504467
  • Dergi Adı: REPRODUCTIVE SCIENCES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.573-581
  • Anahtar Kelimeler: human sperm, phosphotyrosine, capacitation, zona pellucida, hyaluronic acid, HUMAN-SPERMATOZOA, ACROSOME REACTION, CREATINE-PHOSPHOKINASE, GAMETE INTERACTION, HEMIZONA ASSAY, CAPACITATION, KINASE, MOUSE, PROTEINS, IDENTIFICATION
  • Akdeniz Üniversitesi Adresli: Evet

Özet

In mammalian species, acquisition of sperm fertilization competence is dependent on the phenomenon of sperm capacitation. One of the key elements of capacitation is protein tyrosine phosphorylation (TP) in various sperm membrane regions. In previous studies performed, the pattern of TP was examined in human sperm bound to zona pellucida of oocytes. In the present comparative study, TP patterns upon sperm binding to the zona pellucida or hyaluronic acid (HA) were investigated in spermatozoa arising from the same semen samples. Tyrosine phosphorylation, visualized by immunofluorescence, was localized within the acrosomal cap, equatorial head region, neck, and the principal piece. Tyrosine phosphorylation has increased in a time-related manner as capacitation progressed, and the phosphorylation pattern was identical within the principal piece and neck, regardless of the sperm bound to the zona pellucida or HA. Thus, the data demonstrated that the patterns of sperm activation-related TP were similar regardless of the spermatozoa bound to zona pellucida or HA. Further, sperm with incomplete development, as detected by excess cytoplasmic retention, failed to exhibit TP.