[1]Shanghai Jiaotong University, School of Medicine,Shanghai,China
[2]Shanghai Jiao Tong University School of Medicine, Department of Endocrinology,Shanghai,China
[3]Fudan University, School of Life Sciences,Shanghai,China
[4]Tongji University, Department of Hematology and Oncology,Shanghai,China
[5]Shanghai Jiaotong University, Department of Anatomy,Shanghai,China
[6]Anhui Medical University, College of Basic Medicine,Hefei,China
[7]Shanghai Jiaotong University, Department of Histology and Embryology,Shanghai,China
Oocyte meiotic maturation is a developmental transition that starts during germinal-vesicle breakdown and ends at the arrest in metaphase of meiosis II. This transition is associated with changes to both the proteins that are synthesized and the abundance/distribution of post-translational modifications that are crucial for subsequent fertilization and embryogenesis. Here, we isolated and cultured rat oocytes in vitro during both metaphase of meiosis I (MI) and meiosis II (MII) stages, respectively, and then compared their proteomic profiles by high-resolution, two-dimensional gel electrophoresis (2DE) followed by mass spectrometry. We found that the expression of five proteins was up-regulated while six proteins were down-regulated when comparing MI to MII oocytes. The expression of ERp57, an endoplasmic reticulum chaperone, underwent a dramatic increase between MI and MII oocytes, and became concentrated in a dome-shaped area of the cell surface within the microvillar region. A similar profile was observed during spermatogenesis, and sperm ERp57 eventually localized to the head and flagellum surfaces, finally ending in the equatorial region of acrosome-reacted sperm. Given the localization pattern, we tested and found that a polyclonal antiserum created against recombinant rat ERp57 significantly inhibited spermatozoa from penetrating zona pellucida-free oocytes without affecting either sperm motility or the acrosome reaction. These results indicate that ERp57 expression on oocytes, and possibly sperm, plays an important physiological role during sperm-egg fusion. ? 2014 Wiley Periodicals, Inc.