アワビ精子先体反応と細胞骨格系蛋白質

概要

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Changes in cytoskeletal structures which occur during the acrosome reaction of abalone sperm was analyzed by fluorescence and electron microscopies. Fluorescence staining with NBD-phallacidin indicated that the axial rod consists of actin filament bundle, which elongates to form the acrosomal process. Decoration with S1 further revealed that the actin filaments are organized in such a way that the barbed end is distal to the nucleus. This polarity did not change after the formation of the acrosomal process. The truncated cone in the acrosome found by the authors in 1982 was composed of helically coiled filaments with a diameter of about 10 nm. The truncated cone extended three times the original height transforming into the cylindrical structure by further coiling up of the filaments and by stretching of the coil. The helical filaments consisted mainly of 60,000 molecular weight protein which cross-reacted with the antibody against an intermediate filament protein, vimentin. Localization of this protein in the truncated cone was demonstrated by immunofluorescence and immunoelectron microscopies. It was suggested that the 60kD protein as well as actin filament play roles in fertilization of abalone.
和洋女子大学の論文
1989-03-31