Possible involvement of the membrane-bound form of peroxiredoxin 4 in acrosome formation during spermiogenesis of rats.
Possible involvement of the membrane-bound form of peroxiredoxin 4 in acrosome formation during spermiogenesis of rats.
复制标题
DOI：
10.1046/j.1432-1327.2001.02200.x
复制
发表时间：
2001-05
期刊：
影响因子：
--
通讯作者：
I. Sasagawa;S. Matsuki;Y. Suzuki;Y. Iuchi;K. Tohya;M. Kimura;T. Nakada;J. Fujii
中科院分区：
文献类型：
--
作者：
I. Sasagawa;S. Matsuki;Y. Suzuki;Y. Iuchi;K. Tohya;M. Kimura;T. Nakada;J. Fujii
过氧化物酶是一类具有不同生物学功能的新型过氧化物酶。第四个成员Prx 4与信号序列一起合成，并在加工后在大多数组织中以27 kDa的形式分泌。一个31-kDa的Prx 4对应于未加工的，膜结合的形式，只在睾丸中发现。本研究旨在探讨膜结合Prx 4在大鼠精子发生过程中的作用。Prx 4转录本在14日龄（青春期前的年龄）的睾丸中观察到，其水平在衰老过程中仅略有增加。只有分泌形式的Prx 4是目前在30日龄之前，但膜结合的Prx 4成为检测在成年睾丸，虽然这两种形式的总和似乎是相同的21日龄后。虽然弱的免疫反应性Prx 4抗体检测在生精细胞的所有年龄段，观察到一个强大的免疫反应性在伸长的精子细胞和成人睾丸的残留体。Prx 4存在于年轻大鼠睾丸的内质网腔、高尔基体和核周间隙中。然而，本地化的Prx 4仅限于膜的顶体囊泡的细长的精子细胞，并没有检测到精子。一旦精子发生完成，含有膜结合Prx 4的囊泡与残留的膜组分一起沿着释放到残留体内。因此，在精子发生的囊泡重组过程中，可溶性形式向膜结合形式的转化可能在顶体形成中起作用。
Peroxiredoxins are novel peroxidases that exhibit divergent biological functions. The fourth member, Prx4, is synthesized with a signal sequence and, after processing, secreted as a 27-kDa form in most tissues. A 31-kDa Prx4 which corresponds to the unprocessed, membrane-bound form is found only in testis. This study was undertaken in order to investigate the role of the membrane-bound Prx4 during spermiogenesis in rats. The Prx4 transcript was observed in testes at 14 days of age, the age before puberty, and its level increased only slightly during aging. Only the secretable form of Prx4 was present before 30 days of age, but the membrane-bound Prx4 became detectable in adult testes, although sum of the two forms appeared to be the same after 21 days old. While weak immunoreactivity to the Prx4 antibody was detected in spermatogenic cells for all ages, a strong immunoreactivity was observed in the elongating spermatid and residual body of adult testis. Prx4 was present in the lumen of the endoplasmic reticulum, Golgi bodies, and the perinuclear space in young rat testes. However, the localization of Prx4 was restricted to membranes of the acrosomal vesicle of the elongated spermatid and was not detected in spermatozoon. Once spermiogenesis is accomplished, vesicles containing the membrane-bound Prx4 were released into the residual body, along with residual membranous components. Thus the conversion of the soluble form to the membrane-bound form may have a role in the acrosome formation during vesicular reorganization during spermiogenesis.