Neurodegeneration in the age of molecular biology

BMJ 2002; 324 doi: https://doi.org/10.1136/bmj.324.7352.1467 (Published 22 June 2002) Cite this as: BMJ 2002;324:1467

Abnormal protein folding holds the key to specific treatment

  1. Lawrence I Golbe, professor of neurology
  1. UMDNJ-Robert Wood Johnson Medical School, New Brunswick, NJ 08901, USA

    Clinicians still think of neurodegenerative disorders in terms of nonspecific, 19th century style palliation. For a few disorders, we can temporarily relieve symptoms by pharmacological or surgical manipulation of the neurotransmitters emitted by the degenerating neurones. In the past decade, thinking about these disorders has been reordered by the discovery that most of them feature excessive protein misfolding and intracellular protein aggregation. This insight could permit us to interrupt the process of neuronal loss itself.

    Tau, an important component of cytoskeletal physiology, is the protein that aggregates most commonly in neurodegenerative diseases, both in terms of number of disorders and numbers of patients affected. It forms the neurofibrillary tangles of Alzheimer's disease, Pick's disease, progressive supranuclear palsy, frontotemporal dementia, corticobasal degeneration, postencephalitic parkinsonism, and a handful of others.

    Next most common, at least in terms of population prevalence, is β-amyloid, principal component of the amyloid plaques of Alzheimer's disease. Another protein with epidemiological importance is α-synuclein, which forms …

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