Changes in vimentin, lamin A/C and mitofilin induce aberrant cell organization in fibroblasts from Fanconi anemia complementation group A (FA-A) patients.
Biochimie
; 95(10): 1838-47, 2013 Oct.
Article
en En
| MEDLINE
| ID: mdl-23831462
Growing number of publication has proved an increasing of cellular function of the Fanconi anemia proteins. To chromosome stability and DNA repair new roles have been attributed to FA proteins in oxidative stress response and homeostasis, immune response and cytokines sensibility, gene expression. Our work shows a new role for FA-A protein: the organization of the cellular structure. By 2D-PAGE of FA-A and correct fibroblasts treated and untreated with H2O2 we identify different expression of protein involved in the structural organization of nucleus, intermediate filaments and mitochondria. Immunofluorescence and electronic microscopy analysis clearly show an already altered cellular structure in normal culture condition and this worsted after oxidative stress. FA-A cell appears structurally prone to physiologic stress and this could explain part of the phenotype of FA cells.
Palabras clave
2D-PAGE; AML; BM; Cell structure; DSBs; ER; Fanconi anemia; GRP94; H(2)O(2); HSC; IFs; LMNA; N-acetyl cysteine; NAC; Oxidative stress; ROS; WB; acute myeloid leukemia; bone marrow; double strand breaks; endoplasmic reticulum; glucose response protein 94; human stem cells; hydrogen peroxide; intermediate filaments; lamin A; reactive oxygen species; two dimensional polyacrylamide gel electrophoresis; western blot
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Vimentina
/
Citoesqueleto
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Proteínas Mitocondriales
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Lamina Tipo A
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Anemia de Fanconi
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Fibroblastos
/
Proteínas Musculares
Límite:
Humans
Idioma:
En
Revista:
Biochimie
Año:
2013
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Francia