The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
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DOI：
10.1007/bf00337226
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发表时间：
1996-01-01
期刊：
影响因子：
1.6
通讯作者：
Rouleau, L
中科院分区：
文献类型：
--
作者：
PaulinLevasseur, M;Blake, DL;Rouleau, L
对指定的人抗血清的鉴定导致了从人到鱼的所有脊椎动物细胞类型中唯一位于核外围的非层粘连蛋白的子集的鉴定。免疫活性蛋白种类由M(R)78000、58000和40000三个主要多肽组成。在从层蛋白A/C阳性和阴性的哺乳动物细胞中原位分离核基质时，这些抗原与核板共分割。利用双重免疫荧光技术，进一步研究了在整个细胞周期中层粘连蛋白A/C阳性的哺乳动物细胞中人类抗原与A型和B型粘连蛋白的空间关系。在间期HeLa和3T3细胞中，MAN抗原与这两种类型的Lam蛋白共存于核的外围，但在Lam in B的核内灶中没有MAN抗原。随着HeLa细胞进入有丝分裂，MAN抗原与Lam in A/C分离并与Lam in B重新分布。Lam A/C在晚期前期/早期中期解体，在末期/胞质分裂时与染色质重新结合。相反，人的抗原和层蛋白B在前中期分散较晚，在后期在染色体上重组。总之，我们的数据表明，人类抗原可能在维持脊椎动物细胞核室结构完整性方面发挥关键作用。
The characterization of the human antiserum designated MAN has led to the identification of a subset of non-lamin proteins that are exclusively located at the nuclear periphery in all vertebrate cell types examined, from human to fish. Immunoreactive protein species were shown to comprise three major polypeptides of M(r) 78000, 58000 and 40000. These antigens co-partitioned with the nuclear lamina during in situ isolation of nuclear matrices from lamin A/C-positive and -negative mammalian cells. Using double immunofluorescence, the spatial relationship of MAN antigens to type-A and type-B lamins was further examined throughout the cell cycle of lamin A/C-positive mammalian cells. In interphase HeLa and 3T3 cells, MAN antigens colocalized with both types of lamins at the periphery of the nucleus, but were absent from intranuclear foci of lamin B. As HeLa cells proceeded into mitosis, MAN antigens were seen to segregate from lamins A/C and coredistribute with lamin B. Lamins A/C disassembled during late prophase/early prometaphase and reassociated with chromatin in telophase/cytokinesis. In contrast, MAN antigens and lamin B dispersed late during prometaphase and reassembled on chromosomes in anaphase. Altogether, our data suggest that MAN antigens may play key functions in the maintenance of the structural integrity of the nuclear compartment in vertebrate cells.