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Título

Histone carbonylation occurs in proliferating cells

AutorGarcía-Giménez, José Luis; Velázquez Ledesma, Ana María; Esmoris, Isabel; Romá-Mateo, Carlos ; Sanz, Pascual ; Viña, José; Pallardó, Federico V.
Palabras claveEpigenetics
Histones
Carbonylation
Poly(ADP-ribosyl)ation
Cell proliferation
Free radicals
Fecha de publicación15-abr-2012
EditorElsevier
CitaciónFree Radical Biology and Medicine; 52(8):1453-64. (2012)
ResumenChromatin is a dynamic structure formed mainly by DNA and histones, and chemical modifications on these elements regulate its compaction. Histone posttranslational modifications (PTMs) have a direct impact on chromatin conformation, controlling important cellular events such as cell proliferation and differentiation. Redox-related posttranslational modifications may have important effects on chromatin structure and function, offering a new intriguing area of research termed "redox epigenetics." Little is known about histone carbonylation, a PTM that may be related to modifications in the cellular redox environment. The aim of our study was to determine the carbonylation of the various histones during cell proliferation, a moment in cell life during which important redox changes take place. Here, we describe changes in histone carbonylation during cell proliferation in NIH3T3 fibroblasts. In addition, we have studied the variations of poly(ADP-ribosyl)ation and phospho-H2AX at the same time, because both modifications are related to DNA damage responses. High levels of carbonylation on specific histones (H1, H1(0), and H3.1 dimers) were found when cells were in an active phase of DNA synthesis. The modification decreased when nuclear proteasome activity was activated. However, these results did not correlate completely with poly(ADP-ribosyl)ation and phospho-H2AX levels. Therefore, histone carbonylation may represent a specific event during cell proliferation. We describe a new methodology named oxy-2D-TAU Western blot that allowed us to separate and analyze the carbonylation patterns of the histone variants. In addition we offer a new role for histone carbonylation and its implication in redox epigenetics. Our results suggest that histone carbonylation is involved in histone detoxification during DNA synthesis
Descripción12 páginas, 10 figuras (que no es encuentran en este documento, se pueden ver en: http://www.sciencedirect.com/science/article/pii/S0891584912000664)
Versión del editorhttp://dx.doi.org/10.1016/j.freeradbiomed.2012.01.022
URIhttp://hdl.handle.net/10261/116940
DOI10.1016/j.freeradbiomed.2012.01.022
ISSN0891-5849
E-ISSN1873-4596
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