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La leucemogenicidad de AML1-ETO depende de la acetilación de lisina específica del sitio
Lan Wang1, Alexander Gural, Xiao-Jian Sun
1Molecular Pharmacology and Chemistry Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Science (New York, N.Y.)
|July 19, 2011
Resumen
La acetilación de la proteína de fusión AML1-ETO por p300 es crucial para el desarrollo de la leucemia mielógena aguda (LMA). La inhibición de p300 bloquea esta acetilación, ofreciendo una estrategia terapéutica potencial para los pacientes con LMA.
Área de la Ciencia:
- Oncología Oncología.
- Biología Molecular Biología Molecular
- Hematología Hematología.
Sus antecedentes:
- Las translocaciones cromosómicas en la leucemia mielógena aguda (LMA) crean proteínas de fusión.
- Dirigirse a estas proteínas de fusión es un desafío, pero sus modificaciones post-traducionales son objetivos potenciales.
Objetivo del estudio:
- Para investigar el papel de las modificaciones post-traduccionales en la patogénesis de la LMA.
- Explorar el potencial terapéutico de dirigirse a estas modificaciones en la LMA.
Principales métodos:
- Análisis de la acetilación AML1-ETO en células de leucemia derivadas de pacientes.
- Estudios funcionales utilizando células CD34 ((+) de la sangre del cordón umbilical humano.
- Ensayos de leucemogenicidad en modelos de ratón.
- La inhibición de p300 para evaluar su efecto sobre la acetilación y la función de AML1-ETO.
Principales resultados:
- AML1-ETO, la proteína de fusión en la LMA, es acetilada por p300.
- Esta acetilación es esencial para la promoción de la auto-renovación de AML1-ETO y la leucemogenicidad.
- La inhibición de p300 impide la acetilación de AML1-ETO y perjudica la transformación leucémica.
Conclusiones:
- Las lisina acetiltransferasas, como p300, son reguladores críticos de la patogénesis de la LMA.
- Dirigirse a las lisina acetiltransferasas representa una estrategia terapéutica prometedora para la LMA.
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