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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Jun;83(11):3839–3843. doi: 10.1073/pnas.83.11.3839

Keratin-like proteins that coisolate with intermediate filaments of BHK-21 cells are nuclear lamins.

A E Goldman, G Maul, P M Steinert, H Y Yang, R D Goldman
PMCID: PMC323619  PMID: 2424013

Abstract

Four proteins of Mr approximately equal to 60,000, 65,000, 67,000, and 70,000 coisolate with the major intermediate filament (IF) structural proteins of BHK-21 cells. These proteins are keratin-like, they form distinctive paracrystals in vitro, and they are concentrated at the nuclear surface. Since these properties indicate similarities with the nuclear lamins, we have prepared conventional fractions of BHK-21 nuclei from which the same type of paracrystal is obtained. Furthermore, biochemical and immunological data demonstrate that the lamins are identical to the Mr 60,000-70,000 proteins found in IF preparations, and both sets of proteins are similar to keratin. These results suggest that an IF-like protein network is present in the nuclear lamina. We speculate that in some unknown way this network connects to the cytoplasmic IF network that courses from the juxtanuclear region to the cell surface. These proposed interconnecting networks may form part of the infrastructure of cytoskeletal-nuclear matrix-connecting links involved in signal transmission between the nuclear and cytoplasmic compartments of eukaryotic cells.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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