Proteomic analysis of the nuclear matrix in the early stages of rat liver carcinogenesis: Identification of differentially expressed and MAR-binding proteins
Autor: | Cecilia Balbi, Paola Barboro, Erica Repaci, Cristina D'Arrigo, Luca Bagnasco, Paola Orecchia, Barbara Carnemolla, Eligio Patrone |
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Rok vydání: | 2009 |
Předmět: |
Male
Proteomics Keratins Type II Time Factors Blotting Western Cell Cycle Proteins Plasma protein binding Biology Heterogeneous-Nuclear Ribonucleoproteins chemistry.chemical_compound Nuclear Matrix-Associated Proteins Tandem Mass Spectrometry Animals Electrophoresis Gel Two-Dimensional Nuclear Matrix Scaffold/matrix attachment region Heat-Shock Proteins RNA Nuclear Liver Neoplasms Nuclear Proteins RNA-Binding Proteins RNA Matrix Attachment Region Binding Proteins Cell Biology Matrix Attachment Regions Nuclear matrix Molecular biology Lamins Rats Inbred F344 Rats Chromatin Microscopy Electron chemistry Hepatocytes Ribonucleosides Vanadates DNA Lamin Protein Binding |
Zdroj: | Experimental cell research 315 (2009): 226–239. doi:10.1016/j.yexcr.2008.10.017 info:cnr-pdr/source/autori:Barboro P.; D'Arrigo C.; Repaci E.; Bagnasco L.; Orecchia P.; Carnemolla B.; Patrone E.; Balbi C./titolo:Proteomic analysis of the nuclear matrix in the early stages of rat liver carcinogenesis: identification of differentially expressed and MAR-binding proteins/doi:10.1016%2Fj.yexcr.2008.10.017/rivista:Experimental cell research/anno:2009/pagina_da:226/pagina_a:239/intervallo_pagine:226–239/volume:315 |
ISSN: | 0014-4827 |
DOI: | 10.1016/j.yexcr.2008.10.017 |
Popis: | Tumor progression is characterized by definite changes in the protein composition of the nuclear matrix (NM). The interactions of chromatin with the NM Occur via specific DNA sequences called MARS (matrix attachment regions). In the present study, we applied a proteomic approach along with a Southwestern assay to detect both differentially expressed and MAR-binding NM proteins, in persistent hepatocyte nodules (PHN) in respect with normal hepatocytes (NH). In PHN, the NM undergoes changes both in morphology and in protein composition. We detected over 500 protein spots in each two dimensional map and 44 spots were identified. Twenty-three proteins were differentially expressed; among these, 15 spots were under-expressed and 8 spots were over-expressed in PHN compared to NH. These changes were synchronous with several modifications in both NM morphology and the ability of NM proteins to bind nuclear RNA and/or DNA containing MARS sequences. In PHN, we observed a general decrease in the expression of the basic proteins that bound nuclear RNA and the over-expression of two species of Mw 135 kDa and 81 kDa and pl 6.7-7.0 and 6.2-7.4, respectively, which exclusively bind to MARS. These results suggest that the deregulated expression of these species might be related to large-scale chromatin reorganization observed in the process of carcinogenesis by modulating the interaction between MARs and the scaffold structure. (C) 2008 Elsevier Inc. All rights reserved. |
Databáze: | OpenAIRE |
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