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通过核肌动蛋白聚合使人类精子染色质解聚。

Decondensation of human spermatozoal chromatin by nuclear actin polymerization.

作者信息

Jamil K

出版信息

Arch Androl. 1984;13(2-3):137-46. doi: 10.3109/01485018408987512.

DOI:10.3109/01485018408987512
PMID:6443253
Abstract

A critical relationship exists between nuclear actin polymerization and decondensation of sperm chromatin. Characteristic decondensation phenomena were brought about by the protein S-1 of heavy meromyosin of rabbit skeletal muscle in sperm that had undergone the acrosome reaction. Sperm treated with only calcium or only ionophore were not affected by the S-1 trigger, and the nucleus remained in the condensed state. Since S-1 specifically binds to actin, it was possible to demonstrate this phenomenon at the ultrastructural level. Maybe there are switches that operate at different steps for events leading to syngamy and fertilization. No switch can be operative until the preceding event has prepared the sperm for entering the next phase. The operations are performed in a perfect sequential order. This investigation leads to the conclusion that decondensation of sperm chromatin is brought about by nuclear actin polymerization.

摘要

核肌动蛋白聚合与精子染色质解聚之间存在关键关系。兔骨骼肌重酶解肌球蛋白的蛋白质S-1在经历顶体反应的精子中引发了特征性的解聚现象。仅用钙或仅用离子载体处理的精子不受S-1触发的影响,细胞核保持凝聚状态。由于S-1特异性结合肌动蛋白,因此可以在超微结构水平上证明这一现象。也许在导致配子融合和受精的事件的不同步骤中存在开关。在前面的事件使精子为进入下一阶段做好准备之前,没有开关能够起作用。这些操作以完美的顺序进行。这项研究得出的结论是,精子染色质的解聚是由核肌动蛋白聚合引起的。

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