de Lamirande E, Yoshida K, Yoshiike T M, Iwamoto T, Gagnon C
Urology Research Laboratory, Royal Victoria Hospital and McGill University, Montréal, Québec, Canada.
J Androl. 2001 Jul-Aug;22(4):672-9.
Semenogelin (Sg), the major protein of the human semen coagulum, is present at high concentrations in seminal vesicle secretions. It is degraded by the prostate-specific antigen (PSA) to generate peptides of various biological activities that were found on and inside spermatozoa. Our aim was to determine the effect of Sg on capacitation, which is the series of transformations that spermatozoa must undergo to become fertile. At concentrations of 0.1 to 1.0 mg/mL (600- to 20-fold lower than those of semen), Sg did not affect sperm motility (%) but completely prevented capacitation induced by fetal cord serum ultrafiltrate; a partial inhibition of capacitation was noted with 0.03 mg Sg/mL. There was also a dose-dependent decrease in the tyrosine phosphorylation of fibrous sheath proteins and in the O2-.-related chemiluminescence. Ribonuclease (RNase), which has as high an isoelectric point (pI = 9.7) as Sg (pI = 9.5), also prevented sperm capacitation and O2-.-related chemiluminescence but to a lower extent, suggesting that one mechanism of Sg action on spermatozoa could be related to its positive charge at physiological pH. Sg at 1, but not 0.3 or 0.1 mg/mL, scavenged the O2-. generated by the mix of xanthine + xanthine oxidase and modified the kinetics of the reaction; RNase did not have such effects. Therefore, Sg is a potential scavenger for O2-. but probably also affects the sperm oxidase. Spermatozoa rapidly processed Sg; a high proportion of Sg was degraded after 15 minutes of incubation. The resulting polypeptide patterns were reminiscent of those obtained with PSA as a proteolytic enzyme. These data suggest that Sg, its degradation products, or both may be natural regulators of sperm capacitation and could prevent this process from occurring prematurely. One mechanism by which Sg acts could involve an interference with the O2-. that is normally generated during this process.
精浆蛋白(Sg)是人类精液凝块的主要蛋白质,在精囊分泌物中含量很高。它被前列腺特异性抗原(PSA)降解,产生各种具有生物活性的肽,这些肽存在于精子表面和内部。我们的目的是确定Sg对精子获能的影响,精子获能是精子为具备受精能力而必须经历的一系列转变过程。在浓度为0.1至1.0毫克/毫升(比精液浓度低600至20倍)时,Sg不影响精子活力(%),但能完全阻止由胎儿脐带血清超滤物诱导的精子获能;在0.03毫克Sg/毫升时观察到对精子获能有部分抑制作用。纤维鞘蛋白的酪氨酸磷酸化以及与超氧阴离子(O2-·)相关的化学发光也呈剂量依赖性降低。核糖核酸酶(RNase)的等电点(pI = 9.7)与Sg(pI = 9.5)一样高,也能阻止精子获能和与O2-·相关的化学发光,但程度较低,这表明Sg对精子作用的一种机制可能与其在生理pH值下的正电荷有关。1毫克/毫升的Sg能清除由黄嘌呤+黄嘌呤氧化酶混合物产生的O2-·,并改变反应动力学;而RNase没有这种作用。因此,Sg是一种潜在的O2-·清除剂,但可能也会影响精子氧化酶。精子能快速处理Sg;孵育15分钟后,很大一部分Sg被降解。产生的多肽模式让人联想到用PSA作为蛋白水解酶时所获得的模式。这些数据表明,Sg、其降解产物或两者可能是精子获能的天然调节因子,并可防止这一过程过早发生。Sg发挥作用的一种机制可能涉及干扰在此过程中正常产生的O2-·。