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

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

Research output: Contribution to journalArticlepeer-review


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 ∼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.

Original languageEnglish
Pages (from-to)992-1001
Number of pages10
JournalExperimental Cell Research
Issue number6
Publication statusPublished - Apr 1 2010


  • Fast Fourier transform
  • Hepatocytes
  • Immunoelectron microscopy
  • Internal nuclear matrix
  • Lamin assembly
  • Persistent hepatocyte nodules

ASJC Scopus subject areas

  • Cell Biology


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