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Regular Article |
a Biologie et Pathologie du Spermatozoïde Humain, EA 1719, Institut de Recherches sur le Cancer, 59045 Lille, France
b URA 1291 INRA-CNRS Institut National de la Recherche Agronomique, Station de Physiologie des Mammifères Domestiques, 37380 Monnaie, France
c Laboratoire de Cytologie et Biologie de la Reproduction, Hôpital Claude Huriez, CHRU de Lille, 59037 Lille, France
d Service d'Urologie, Hôpital Claude Huriez, CHRU de Lille, 59037 Lille, France
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.
1 Supported in part by a grant from the CHRU de Lille and by the Université de Lille II.
2 Correspondence: Roselyne Rousseaux-Prévost, Institut de Recherches sur le Cancer, Place de Verdun, F-59045 Lille, France. FAX: 33 320169229.
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