Secretory mouse quiescin sulfhydryl oxidase 1 aggregates defected human and mouse spermatozoa in vitro and in vivo
Tse-En Wang,
Ling-Yu Yeh,
Robert Kuo-Kuang Lee,
Chung-Hao Lu,
Tsung-Hsien Yang,
Yu-Wen Kuo,
Radhika Joshi,
Pei-Shiue Tsai,
Sheng-Hsiang Li
Affiliations
Tse-En Wang
Department of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Graduate Institute of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Department of Cellular and Molecular Physiology, Yale School of Medicine, New Haven, USA
Ling-Yu Yeh
Department of Medical Research, MacKay Memorial Hospital, Tamsui, Taiwan
Robert Kuo-Kuang Lee
Department of Medical Research, MacKay Memorial Hospital, Tamsui, Taiwan; Department of Obstetrics and Gynecology, MacKay Memorial Hospital, Taipei, Taiwan
Chung-Hao Lu
Department of Obstetrics and Gynecology, MacKay Memorial Hospital, Taipei, Taiwan
Tsung-Hsien Yang
Department of Medical Research, MacKay Memorial Hospital, Tamsui, Taiwan
Yu-Wen Kuo
Department of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Graduate Institute of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Department of Clinical Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden
Radhika Joshi
Graduate Institute of Veterinary Medicine, National Taiwan University, Taipei, Taiwan
Pei-Shiue Tsai
Department of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Graduate Institute of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Research Center for Developmental Biology and Regenerative Medicine, National Taiwan University, Taipei, Taiwan; Corresponding author
Sheng-Hsiang Li
Department of Medical Research, MacKay Memorial Hospital, Tamsui, Taiwan; MacKay Junior College of Medicine, Nursing, and Management, Taipei, Taiwan; Corresponding author
Summary: A flavin-dependent enzyme quiescin Q6 sulfhydryl oxidase 1 (QSOX1) catalyzes the oxidation of thiol groups into disulfide bonds. QSOX1 is prominently expressed in the seminal plasma. However, its role in male reproduction is elusive. Here, we purified the secreted form of QSOX1, i.e., QSOX1c, from mouse seminal vesicle secretions and revealed for the first time its function involved in sperm physiology. Exogenous addition of QSOX1c time-dependently promoted the in vitro aggregation of thiol-rich, oxidative stressed, and apoptotic mouse and human sperm cells. Also, in vivo aggregated sperm cells collected from mouse uterine and human ejaculates also showed high levels of QSOX1c, intracellular reactive oxygen species, annexin V, and free thiols. In summary, our studies demonstrated that QSOX1c could agglutinate spermatozoa susceptible to free radical attack and apoptosis. This characteristic may provide an opportunity to separate defective sperm cells and improve sperm quality before artificial insemination in humans and animals.
