Role of heat shock protein HSP70-2 in spermatogenesis

Role of heat shock protein HSP70-2 in spermatogenesis
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DOI:
10.1530/ror.0.0040023
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发表时间:
1999-01-01
期刊:
REVIEWS OF REPRODUCTION
影响因子:
--
通讯作者:
Eddy, EM
Eddy, EM
中科院分区:
其他
文献类型:
--
作者:
Eddy, EM

文献摘要

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HSP 70热休克蛋白是一种分子伴侣,它能帮助其他蛋白质折叠、转运和组装成复合物。这些蛋白质中的大多数是组成型表达的,或者它们的表达是由热休克和其他应激诱导的。然而,Hsp 70家族的两个成员(小鼠中的HSP 70 -2和HSC 70 T)在发育过程中受到调节,并在生精细胞中特异性表达。HSP 70 -2蛋白在精子发生的减数分裂期合成,在粗线期精母细胞中含量丰富。敲除方法用于确定HSP 70 -2是否是参与减数分裂的蛋白质的伴侣。HSP 70 -2缺失的雄性小鼠不育,而HSP 70 -2缺失的雌性小鼠可生育。生精细胞的发育在减数分裂I前期的G2-M期转变被阻止,粗线期晚期的精母细胞通过凋亡被消除,导致精子细胞的缺失。HSP 70 -2是Cdc 2与细胞周期蛋白B1形成异源二聚体所必需的,这表明它是雄性小鼠生殖细胞减数分裂进程所必需的伴侣。HSP 70 -2也与联会复合体相关,缺乏这种蛋白质的雄性小鼠的突触融合被破坏。HSP 70 -2的同源物存在于许多动物的睾丸中,表明这种生精细胞伴侣的作用在各个门中是保守的。
The HSP70 heat-shock proteins are molecular chaperones that assist other proteins in their folding, transport and assembly into complexes. Most of these proteins are either constitutively expressed or their expression is induced by heat shock and other stresses. However, two members of the Hsp70 family (HSP70-2 and HSC70T in mice) are regulated developmentally and expressed specifically in spermatogenic cells. The HSP70-2 protein is synthesized during the meiotic phase of spermatogenesis and is abundant in pachytene spermatocytes. The knockout approach was used to determine whether HSP70-2 is a chaperone for proteins involved in meiosis. Male mice lacking HSP70-2 were infertile while females lacking HSP70-2 were fertile. Spermatogenic cell development was arrested in prophase of meiosis I at the G2-M-phase transition and late pachytene spermatocytes were eliminated by apoptosis, resulting in an absence of spermatids. HSP70-2 is required for Cdc2 to form a heterodimer with cyclin B1, suggesting that it is a chaperone necessary for the progression of meiosis in the germ cells of male mice. HSP70-2 is also associated with the synaptonemal complex and desynapsis is disrupted in male mice lacking this protein. Homologues of HSP70-2 are present in the testes of many animals, suggesting that the role of this spermatogenic cell chaperone is conserved across phyla.