Sudhakar, L and Rao, MR (1990) Stage-dependent changes in localization of a germ cell-specific lamin during mammalian spermatogenesis. In: Journal of Biological Chemistry, 265 (36). pp. 22526-22532.
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Abstract
We had earlier identified a 110/120-kDa protein specific to nuclear matrix of rat pachytene spermatocytes (Behal, A., Prakash, K., and Rao, M.R.S. (1987) J. Biol. Chem. 262, 10898-10902). This protein is now shown to be a disulfide-linked homodimer of a 60-kDa polypeptide. Indirect immunofluorescence and Western blot analyses using anti-120- kDa polyclonal antibodies have shown that this protein is a component of the pore-complex lamina structure of spermatogonia. As germ cells enter meiotic prophase and the lamina structure disassembles, this polypeptide is redistributed in the nucleus and can be isolated as a component of synaptonemal complexes. Following meiotic division, this 60-kDa protein is relocalized in the lamina, then representing the sole major component of the lamina structure of round spermatids. The identity of the 60-kDa protein in the pore-complex lamina fraction and synaptonemal complexes was further confirmed by two-dimensional analysis of iodinated tryptic peptides. Such an analysis has also shown that the germ cell-specific 60-kDa protein is related but not identical to somatic lamin B.
Item Type: | Journal Article |
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Publication: | Journal of Biological Chemistry |
Publisher: | American Society for Biochemistry and Molecular Biology |
Additional Information: | Copyright of this article belongs to American Society for Biochemistry and Molecular Biology |
Keywords: | mammalian spermatogenesis |
Department/Centre: | Division of Biological Sciences > Biochemistry |
Date Deposited: | 29 Jan 2008 |
Last Modified: | 19 Sep 2010 04:41 |
URI: | http://eprints.iisc.ac.in/id/eprint/12595 |
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