Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation.
Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation.
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DOI：
10.1093/molehr/4.1.17
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发表时间：
1998
影响因子：
4
通讯作者：
Claudia N. Tomes;Rosa Carballada;Daniel F. Moses;David F. Katz;Patricia M. Saling
中科院分区：
文献类型：
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作者：
Claudia N. Tomes;Rosa Carballada;Daniel F. Moses;David F. Katz;Patricia M. Saling
长期以来，人们都知道精浆中含有以多种不同方式影响精子活力的因子。然而，很少有人了解的生化级联反应时，精子和精浆相互作用。在这项研究中，我们研究了如何孵育精浆影响蛋白酪氨酸磷酸化的人精子。蛋白质酪氨酸磷酸化的增加是包括人类在内的几种哺乳动物精子获能的标志。精浆加入洗涤过的非获能精子中可阻断蛋白酪氨酸磷酸化。去除精浆并在获能培养基中孵育导致酪氨酸磷酸化级联的部分恢复。在获能条件下，将精浆加入预先孵育5 h的精子悬浮液中，以剂量依赖性方式降低了所有蛋白质的酪氨酸磷酸化水平。在这种情况下，去除精浆后在新鲜获能培养基中孵育过夜，磷酸酪氨酸信号并未增加，这表明去除精浆对于蛋白质酪氨酸磷酸化的发生是必要的，但还不足以。这些结果表明，人类精浆中含有影响人类精子酪氨酸磷酸化状态的因素。
It has long been known that seminal plasma contains factors that influence the fertilizing capacity of spermatozoa in many different ways. However, little is understood of the biochemical cascades triggered when spermatozoa and seminal plasma interact. In this study, we examined how incubation with seminal plasma affected protein tyrosine phosphorylation in human spermatozoa. Increased protein tyrosine phosphorylation is a hallmark of sperm capacitation in several mammalian species, including human. Seminal plasma blocks protein tyrosine phosphorylation when added to washed, non-capacitated spermatozoa. Removal of seminal plasma and incubation in capacitating medium led to partial recovery of the tyrosine phosphorylation cascade. Addition of seminal plasma to a suspension of spermatozoa previously incubated for 5 h under capacitating conditions decreased the level of tyrosine phosphorylation on all proteins in a dose-dependent manner. In this case, the phosphotyrosine signal did not increase upon removal of seminal plasma followed by overnight incubation in fresh capacitating media, indicating that removal of seminal plasma was necessary but not sufficient for protein tyrosine phosphorylation to occur. These results indicate that human seminal plasma contains factors that influence the tyrosine phosphorylation status of human spermatozoa.