(s)-α-chlorohydrin inhibits protein tyrosine phosphorylation through blocking cyclic amp - protein kinase a pathway in spermatozoa(s)-α-chlorohydrin抑制蛋白质酪氨酸磷酸化通过阻断环腺苷酸蛋白激酶精子的途径.pdfVIP

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(s)-α-chlorohydrin inhibits protein tyrosine phosphorylation through blocking cyclic amp - protein kinase a pathway in spermatozoa(s)-α-chlorohydrin抑制蛋白质酪氨酸磷酸化通过阻断环腺苷酸蛋白激酶精子的途径.pdf

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(s)-α-chlorohydrin inhibits protein tyrosine phosphorylation through blocking cyclic amp - protein kinase a pathway in spermatozoa(s)-α-chlorohydrin抑制蛋白质酪氨酸磷酸化通过阻断环腺苷酸蛋白激酶精子的途径

(S)-a-Chlorohydrin Inhibits Protein Tyrosine Phosphorylation through Blocking Cyclic AMP - Protein Kinase A Pathway in Spermatozoa 1. 2. 1. 1 3,4 3 1 Hao Zhang , Huan Yu , Xia Wang , Weiwei Zheng , Bei Yang , Jingbo Pi , Gengsheng He *, Weidong Qu1* 1 Key Laboratory of the Public Health Safety, Ministry of Education, Department of Environmental Health, School of Public Health, Fudan University, Shanghai, China, 2 Neurology Department of Huashan Hospital, Fudan University, Shanghai, China, 3 Institutes for Chemical Safety Sciences, The Hamner Institutes for Health Sciences, Research Triangle Park, North Carolina, United States of America, 4 Department of Histology and Embryology, Basic Medical College, China Medical University, Shenyang, China Abstract a-Chlorohydrin is a common contaminant in food. Its (S)-isomer, (S)-a-chlorohydrin (SACH), is known for causing infertility in animals by inhibiting glycolysis of spermatozoa. The aim of present work was to examine the relationship between SACH and protein tyrosine phosphorylation (PTP), which plays a critical role in regulating mammalian sperm capacitation. In vitro exposure of SACH 50 mM to isolated rat epididymal sperm inhibited PTP. Sperm-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) activities, the intracellular adenosine 59-triphosphate (ATP) levels, 39-59-cyclic adenosine monophosphate (cAMP) levels and phosphorylation of protein kinase A (PKA) substrates in rat sperm were diminished dramatically, indicating that both glycolysis and the cAMP/PKA signaling pathway were impaired by SACH. The inhibition of both PTP and phosphorylation of PKA substrates by SACH could be restored by addition of cAMP a