Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes

Barboro, Paola; D'Arrigo, Cristina; Repaci, Erica; Patrone, Eligio; Balbi, Cecilia

doi:10.1016/J.YEXCR.2009.12.010

Title: Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes

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Abstract

Nuclear lamins are among the more abundant proteins making up the internal nuclear matrix, but very little is known about their structure in the nucleoplasm. Using immunoelectron microscopy, we demonstrate the organization of lamins in the nuclear matrix isolated from rat hepatocytes for the first time. Lamin epitopes are arrayed both in locally ordered clusters and in quasi-regular rows. Fourier filtering of the images demonstrates that the epitopes are placed at the nodes and halfway between the nodes of square or rhombic lattices that are about 50 nm on each side, as well as along rows at regular {approx}25-nm intervals. In addition, we have compared this structure with that of the internal nuclear matrix isolated from persistent hepatocyte nodules. In transformed hepatocytes, the islands of lamin lattice are lost, and only a partial regularity in the rows of gold particles remains. We suggest that orthogonal lattice assembly might be an intrinsic property of lamin molecules, and that the disassembly may be triggered by simple molecular events such as phosphorylation.

Authors:

Barboro, Paola ^[1]; D'Arrigo, Cristina ^[2]; Repaci, Erica ^[1]; Patrone, Eligio ^[2]; Balbi, Cecilia ^[1]

Istituto Nazionale per la Ricerca sul Cancro, Largo Rosanna Benzi, 10-16132 Genova (Italy)
CNR, Istituto per lo Studio delle Macromolecole, ISMAC-Genova, Via De Marini, 6-16149 Genova (Italy)

Publication Date:: Thu Apr 01 00:00:00 EDT 2010

OSTI Identifier:: 22212057

Resource Type:: Journal Article

Journal Name:: Experimental Cell Research

Additional Journal Information:: Journal Volume: 316; Journal Issue: 6; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; FOURIER TRANSFORMATION; LIVER CELLS; NUCLEAR MATRIX; PHOSPHORYLATION; PROTEINS; RATS

Citation Formats


                    Barboro, Paola, D'Arrigo, Cristina, Repaci, Erica, Patrone, Eligio, and Balbi, Cecilia. Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes.  United States: N. p., 2010. 
        Web.  doi:10.1016/J.YEXCR.2009.12.010.

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                    Barboro, Paola, D'Arrigo, Cristina, Repaci, Erica, Patrone, Eligio, & Balbi, Cecilia. Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes.  United States.  https://doi.org/10.1016/J.YEXCR.2009.12.010

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                    Barboro, Paola, D'Arrigo, Cristina, Repaci, Erica, Patrone, Eligio, and Balbi, Cecilia. 2010.  
        "Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes".  United States.  https://doi.org/10.1016/J.YEXCR.2009.12.010.

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@article{osti_22212057,

  title        = {Organization of the lamin scaffold in the internal nuclear matrix of normal and transformed hepatocytes},

  author       = {Barboro, Paola and D'Arrigo, Cristina and Repaci, Erica and Patrone, Eligio and Balbi, Cecilia},

  abstractNote = {Nuclear lamins are among the more abundant proteins making up the internal nuclear matrix, but very little is known about their structure in the nucleoplasm. Using immunoelectron microscopy, we demonstrate the organization of lamins in the nuclear matrix isolated from rat hepatocytes for the first time. Lamin epitopes are arrayed both in locally ordered clusters and in quasi-regular rows. Fourier filtering of the images demonstrates that the epitopes are placed at the nodes and halfway between the nodes of square or rhombic lattices that are about 50 nm on each side, as well as along rows at regular {approx}25-nm intervals. In addition, we have compared this structure with that of the internal nuclear matrix isolated from persistent hepatocyte nodules. In transformed hepatocytes, the islands of lamin lattice are lost, and only a partial regularity in the rows of gold particles remains. We suggest that orthogonal lattice assembly might be an intrinsic property of lamin molecules, and that the disassembly may be triggered by simple molecular events such as phosphorylation.},

  doi          = {10.1016/J.YEXCR.2009.12.010},

  url          = {https://www.osti.gov/biblio/22212057},
  journal      = {Experimental Cell Research},

  issn         = {0014-4827},

  number       = 6,

  volume       = 316,

  place        = {United States},

  year         = {Thu Apr 01 00:00:00 EDT 2010},

  month        = {Thu Apr 01 00:00:00 EDT 2010}

}

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