Actin-binding properties and colocalization with actin during spermiogenesis of mammalian sperm calicin

被引:49
作者
Lécuyer, C
Dacheux, JL
Hermand, E
Mazeman, E
Rousseaux, J
Rousseaux-Prévost, R
机构
[1] Inst Rech Canc, EA 1719, F-59045 Lille, France
[2] CNRS, INRA, URA 1291, Stn Physiol Mammiferes Domest, F-37380 Monnaie, France
[3] CHRU Lille, Hop Claude Huriez, Lab Cytol & Biol Reprod, F-59037 Lille, France
[4] CHRU Lille, Hop Claude Huriez, Serv Urol, F-59037 Lille, France
关键词
sperm; spermatid; spermatogenesis; testes;
D O I
10.1095/biolreprod63.6.1801
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The nucleus of mammalian spermatozoa is surrounded by a rigid layer, the perinuclear theca, which is divided into a subacrosomal layer and a postacrosomal calyx. Among the proteins characterized in the perinuclear theca, calicin is one of the main components of the calyx. Its sequence contains three kelch repeats and a BTB/POZ domain. We have studied the association of boar calicin with F-actin and the distribution of boar and human calicin during spermiogenesis compared with the distribution of actin. Calicin was purified from boar sperm heads under nondenaturating conditions. The molecule bound actin with high affinity (K-d = similar to5 nM), and a stoichiometry of approximately one calicin per 12 actin monomers was observed. Gel filtration studies showed that calicin forms homomultimers (tetramers and higher polymers). According to immunocytochemical results, calicin is present (together with actin) in the acrosomal region of round spermatids and is mainly localized in the postacrosomal region of late spermatids and spermatozoa. Taken together, the results suggest that the affinity of calicin to F-actin allows targeting of calicin at the subacrosomal space of round spermatids, and that its ability to form homomultimers contributes to the formation of a rigid calyx.
引用
收藏
页码:1801 / 1810
页数:10
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