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- W1569061529 abstract "The nuclear lamina, a structure closely apposed to the inner nuclear membrane, is believed to provide a framework important for nuclear envelope integrity and interphase chromatin organization. So far, in mammalian and avian species three major constituents of the lamina, lamins A, B, and C, have been identified. These proteins migrate to characteristic positions on two-dimensional gels, being more acidic than lamins A and C. Here, we show that the composition of the nuclear lamina in avian and mammalian cells is more complex than previously assumed. When analyzed on two-dimensional gels, the major 66-kDa chicken lamin B protein can readily be identified. However, an additional 68-kDa protein migrates to a similarly acidic position. Based on the following evidence, both proteins can be considered as two distinct members of the protein family. First, peptide mapping experiments and immunological criteria demonstrate that these two proteins are not related to each other or to A via postsynthetic modifications or precursor-product relationships. Second, as determined by immunocytochemical techniques, both proteins are located exclusively at the nuclear periphery. Third, both proteins display the biochemical properties characteristic of proteins, i.e. they are resistant to extraction of nuclei with nonionic detergents, nucleases, and high salt. Fourth, both proteins are immunologically related to previously characterized proteins: the major 66-kDa chicken lamin B protein shares at least two epitopes with A. However, contrary to what current nomenclature might suggest, this 66-kDa chicken lamin B protein is not related to rat liver B, but to a minor component of rat liver pore-complex lamina preparations that had not previously been recognized as a protein. Conversely, the minor 68-kDa component of chicken lamina preparations that had not previously been considered to be a protein is immunologically related to rat liver B. Thus, in addition to demonstrating the existence of quantitatively minor proteins in higher vertebrates, our results caution against assigning structural homologies between proteins from different species on the basis of gel electrophoresis analyses." @default.
- W1569061529 created "2016-06-24" @default.
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- W1569061529 date "1986-10-01" @default.
- W1569061529 modified "2023-09-30" @default.
- W1569061529 title "The nuclear lamin protein family in higher vertebrates. Identification of quantitatively minor lamin proteins by monoclonal antibodies." @default.
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- W1569061529 doi "https://doi.org/10.1016/s0021-9258(18)69303-2" @default.
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