Literature DB >> 9393599

Differential phosphorylation of lamin B2 in normal and leukemic cells.

R Meier1, P R Müller, A Hirt, K Leibundgut, A Ridolfi-Lüthy, H P Wagner.   

Abstract

Lamins constitute the nuclear lamina, which underlie the inner membrane of the cell nucleus. Phosphorylation of lamins is a key factor in the regulation of nuclear structure during the cell cycle and of gene transcription. Since an uncontrolled cell cycle and altered gene transcription are major characteristics of neoplasms, we looked for differences in lamin B2 phosphorylation between PBMC, ALL and AML cells. Using different lamin B2-specific antibodies, we detected two different lamin B2 species termed lamin B2 and B2A. Although phosphorylation of lamin B2 in leukemic cells was reminiscent of resting cells, the majority of ALL and AML samples showed significantly higher and more altered lamin B2A phosphorylation compared to PBMC. It remains to be elucidated which mechanism leads to these alterations and whether it could explain the extended G1-phase frequently observed in ALL cells.

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Year:  1997        PMID: 9393599     DOI: 10.1016/s0145-2126(97)00076-3

Source DB:  PubMed          Journal:  Leuk Res        ISSN: 0145-2126            Impact factor:   3.156


  2 in total

Review 1.  Partners and post-translational modifications of nuclear lamins.

Authors:  Dan N Simon; Katherine L Wilson
Journal:  Chromosoma       Date:  2013-03-12       Impact factor: 4.316

2.  Global phosphoproteome analysis of human bone marrow reveals predictive phosphorylation markers for the treatment of acute myeloid leukemia with quizartinib.

Authors:  C Schaab; F S Oppermann; M Klammer; H Pfeifer; A Tebbe; T Oellerich; J Krauter; M Levis; A E Perl; H Daub; B Steffen; K Godl; H Serve
Journal:  Leukemia       Date:  2013-11-19       Impact factor: 11.528

  2 in total

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