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1 December 2000 Actin-Binding Properties and Colocalization with Actin During Spermiogenesis of Mammalian Sperm Calicin
Christophe Lécuyer, Jean-Louis Dacheux, Eric Hermand, Etienne Mazeman, Jean Rousseaux, Roselyne Rousseaux-Prévost
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Abstract

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 (Kd = ∼5 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.

Christophe Lécuyer, Jean-Louis Dacheux, Eric Hermand, Etienne Mazeman, Jean Rousseaux, and Roselyne Rousseaux-Prévost "Actin-Binding Properties and Colocalization with Actin During Spermiogenesis of Mammalian Sperm Calicin," Biology of Reproduction 63(6), 1801-1810, (1 December 2000). https://doi.org/10.1095/biolreprod63.6.1801
Received: 25 February 2000; Accepted: 1 August 2000; Published: 1 December 2000
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