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Journal of Cell Science, Vol 109, Issue 7 1775-1785, Copyright © 1996 by Company of Biologists
JOURNAL ARTICLES |
D Lourim, A Kempf and G Krohne
Department of Electron Microscopy, Theodor Boveri Institute, University of Wurzburg, Germany.
We have previously shown that Xenopus oocytes, eggs, and early embryos contain lamins LII and LIII, and that portions of each are associated with distinct egg vesicle populations. We now report that a lamin similar or identical to the B-type lamin LI is also present in oocyte nuclei and in egg extracts. We have quantitated the three B-type lamins per oocyte nucleus, and have calculated relative ratios of LI:LIII = 1:100, and LII:LIII = 1:10. Similar to lamin LII, 5-15% of lamin LI is associated with egg membranes in a biochemically stable manner. Egg vesicles absorbed with lamin isoform-specific antibodies to magnetic beads indicate that lamin LI-associated egg membranes are of heterogenous morphology, and are independent from the lamin LII and LIII vesicle populations. Compared to other nuclear envelope proteins, the synthesis of lamin LI protein is specifically elevated during meiotic maturation, resulting in a 4- to 12-fold higher amount of lamin LI in eggs than is present in oocyte nuclei. Immunofluorescence and immunoblot analysis demonstrated that lamins LI, LII, and LIII are associated with the nuclear envelope formed on demembranated sperm when added to activated egg extract. These results strongly suggest that three different lamin-associated vesicle populations are involved in the formation of a nuclear envelope in egg extracts.
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