Huntington's disease: Neuroprotection

Huntington's disease is caused by an expanded glutamine repeat in the abnormal protein huntingtin. The protein domain containing this sequence has been found to bind to CREB-binding protein and an associated factor, inhibiting their ability to transfer acetyl groups to other proteins. This reduces levels of acetylated histones, an effect associated with Huntington's disease. Histone deacetylase (HDAC) inhibitors restore acetylated histone levels, and also prevent neurodegeneration in a Drosophila model. Several HDAC inhibitors are approved for clinical uses, such as cancer therapy, raising the prospect that these drugs might be used to treat neurodegenerative diseases.

Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
JOAN S. STEFFAN, LASZLO BODAI, JUDIT PALLOS, MARNIX POELMAN, ALEXANDER MCCAMPBELL, BARBARA L. APOSTOL, ALEXSEY KAZANTSEV, EMILY SCHMIDT, YA-ZHEN ZHU, MARILEE GREENWALD, RIKI KUROKAWA, DAVID E. HOUSMAN, GEORGE R. JACKSON, J. LAWRENCE MARSH & LESLIE M. THOMPSON
Nature 413, 739-743 (18 October 2001)
| First Paragraph | Full Text | PDF (211 K) |

Huntington's disease: Exploiting expression
GILLIAN P. BATES
Huntington's disease results from defects in the huntingtin protein, but the exact mechanism has been unclear. Researchers now have a better idea, and the knowledge has proved beneficial — for flies at least.
Nature 413, 691-694 (18 October 2001)
| Full Text | PDF (269 K) |

18 October 2001 table of contents