Differential phosphorylation of lamin B2 in normal and leukemic cells.

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.

• Authors: R Meier, P R Müller, A Hirt, K Leibundgut, A Ridolfi-Lüthy, H P Wagner
• Journal: Leukemia research (Leuk Res) Vol. 21 Issue 9 Pg. 841-7 (Sep 1997) ISSN: 0145-2126 [Print] England
• PMID: 9393599 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies, Monoclonal
• Lamin Type B
• Lamins
• Neoplasm Proteins
• Nuclear Proteins
• Phosphoproteins
• lamin B2

Topics

• Acute Disease
• Antibodies, Monoclonal (immunology)
• Bone Marrow (pathology)
• Burkitt Lymphoma (metabolism, pathology)
• Cell Cycle
• Humans
• Lamin Type B
• Lamins
• Leukemia (metabolism, pathology)
• Leukemia, Myeloid (metabolism, pathology)
• Neoplasm Proteins (immunology, metabolism)
• Nuclear Proteins (immunology, metabolism)
• Peptide Mapping
• Phosphoproteins (immunology, metabolism)
• Phosphorylation
• Precursor B-Cell Lymphoblastic Leukemia-Lymphoma (metabolism, pathology)
• Protein Processing, Post-Translational
• Tumor Cells, Cultured