Immunochemical localization of contractile proteins in mammalian meiotic chromosomes |
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Authors: | Prof. C. De Martino E. Capanna M. R. Nicotra P. G. Natali |
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Affiliation: | (1) Laboratories of Electron Microscopy Regina Elena Institute for Cancer Research, Rome, Italy;(2) Comparative Anatomy Institute, University of Rome, Italy;(3) Laboratories of Immunology, Regina Elena Institute for Cancer Research, Rome, Italy;(4) Istituto Regina Elena, Laboratorio di Microscopia Elettronica, Viale Regina Elena 291, 00161 Roma, Italy |
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Abstract: | Summary Smooth muscle heavy myosin and actin have been detected in mouse and rat meiotic chromosomes, by indirect immunofluorescence performed on testis cryostat sections and isolated germ cells. Both contractile proteins are detectable in the nuclei of meiotic cells during the first prophase. The appearance and disappearance time of myosin and actin, however, is not synchronous. While actin is visible in small spots from resting to late diplotene spermatocytes, myosin appears as filaments in the primary spermatocytes from the zygotene to the early stage of diplotene. The number of myosin filaments in the pachytene spermatocytes corresponds to the number of bivalent chromosomes, whereas actin spots constantly outnumber the pairing chromosomes by two units. These immunochemical observations suggest that the two contractile proteins are associated with the synaptonemal complex (SC). Myosin seems to be associated with the central region of the SC, while actin is present in its basal knob which is in connection with the nuclear membrane. The difference in number between myosin filaments and actin spots appears to be related to the peculiar behaviour of the pairing sex chromosomes. The presence of contractile proteins in the nuclei of primary spermatocytes seems to suggest that they might play a role in the process of pairing of homologous chromosomes. |
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Keywords: | Testis Meiotic nuclei Myosin Actin |
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