Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros

Base de dados
Ano de publicação
Tipo de documento
Intervalo de ano de publicação
1.
Brain ; 141(3): 673-687, 2018 03 01.
Artigo em Inglês | MEDLINE | ID: mdl-29415205

RESUMO

Peripheral nerve axons require a well-organized axonal microtubule network for efficient transport to ensure the constant crosstalk between soma and synapse. Mutations in more than 80 different genes cause Charcot-Marie-Tooth disease, which is the most common inherited disorder affecting peripheral nerves. This genetic heterogeneity has hampered the development of therapeutics for Charcot-Marie-Tooth disease. The aim of this study was to explore whether histone deacetylase 6 (HDAC6) can serve as a therapeutic target focusing on the mutant glycyl-tRNA synthetase (GlyRS/GARS)-induced peripheral neuropathy. Peripheral nerves and dorsal root ganglia from the C201R mutant Gars mouse model showed reduced acetylated α-tubulin levels. In primary dorsal root ganglion neurons, mutant GlyRS affected neurite length and disrupted normal mitochondrial transport. We demonstrated that GlyRS co-immunoprecipitated with HDAC6 and that this interaction was blocked by tubastatin A, a selective inhibitor of the deacetylating function of HDAC6. Moreover, HDAC6 inhibition restored mitochondrial axonal transport in mutant GlyRS-expressing neurons. Systemic delivery of a specific HDAC6 inhibitor increased α-tubulin acetylation in peripheral nerves and partially restored nerve conduction and motor behaviour in mutant Gars mice. Our study demonstrates that α-tubulin deacetylation and disrupted axonal transport may represent a common pathogenic mechanism underlying Charcot-Marie-Tooth disease and it broadens the therapeutic potential of selective HDAC6 inhibition to other genetic forms of axonal Charcot-Marie-Tooth disease.


Assuntos
Doença de Charcot-Marie-Tooth/genética , Doença de Charcot-Marie-Tooth/terapia , Glicina-tRNA Ligase/genética , Desacetilase 6 de Histona/metabolismo , Mutação/genética , Animais , Transporte Axonal/genética , Células Cultivadas , Doença de Charcot-Marie-Tooth/fisiopatologia , Modelos Animais de Doenças , Inibidores Enzimáticos/uso terapêutico , Gânglios Espinais/citologia , Desacetilase 6 de Histona/genética , Ácidos Hidroxâmicos/uso terapêutico , Indóis/uso terapêutico , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Transgênicos , Neurônios Motores/efeitos dos fármacos , Neurônios Motores/metabolismo , Condução Nervosa/genética , Junção Neuromuscular/patologia , Junção Neuromuscular/fisiopatologia , Desempenho Psicomotor/fisiologia , RNA Interferente Pequeno/genética , RNA Interferente Pequeno/metabolismo , Tubulina (Proteína)/metabolismo
2.
ACS Chem Neurosci ; 7(2): 240-58, 2016 Feb 17.
Artigo em Inglês | MEDLINE | ID: mdl-26599234

RESUMO

Charcot-Marie-Tooth (CMT) disease is a disorder of the peripheral nervous system where progressive degeneration of motor and sensory nerves leads to motor problems and sensory loss and for which no pharmacological treatment is available. Recently, it has been shown in a model for the axonal form of CMT that histone deacetylase 6 (HDAC6) can serve as a target for the development of a pharmacological therapy. Therefore, we aimed at developing new selective and activity-specific HDAC6 inhibitors with improved biochemical properties. By utilizing a bicyclic cap as the structural scaffold from which to build upon, we developed several analogues that showed improved potency compared to tubastatin A while maintaining excellent selectivity compared to HDAC1. Further screening in N2a cells examining both the acetylation of α-tubulin and histones narrowed down the library of compounds to three potent and selective HDAC6 inhibitors. In mutant HSPB1-expressing DRG neurons, serving as an in vitro model for CMT2, these inhibitors were able to restore the mitochondrial axonal transport deficits. Combining structure-based development of HDAC6 inhibitors, screening in N2a cells and in a neuronal model for CMT2F, and preliminary ADMET and pharmacokinetic profiles, resulted in the selection of compound 23d that possesses improved biochemical, functional, and druglike properties compared to tubastatin A.


Assuntos
Doença de Charcot-Marie-Tooth/tratamento farmacológico , Doença de Charcot-Marie-Tooth/enzimologia , Inibidores de Histona Desacetilases/uso terapêutico , Histona Desacetilases/metabolismo , Acetilação/efeitos dos fármacos , Animais , Linhagem Celular Tumoral , Células Cultivadas , Modelos Animais de Doenças , Gânglios Espinais/citologia , Desacetilase 6 de Histona , Inibidores de Histona Desacetilases/química , Inibidores de Histona Desacetilases/farmacologia , Histona Desacetilases/genética , Humanos , Interleucina-2/genética , Camundongos , Camundongos Transgênicos , Mutação/genética , Neuroblastoma/patologia , Neurônios/efeitos dos fármacos , Neurônios/enzimologia , Tubulina (Proteína)/genética , Tubulina (Proteína)/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA