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NOTCH3 mutation involving three cysteine residues in a family with typical CADASIL

M Dichgans1, J Herzog, T Gasser

  • 1Department of Neurology, Klinikum Grosshadern, Ludwig-Maximilians-Universität, Munich, Germany. mdichgans@nefo.med.uni-muenchen.de

Neurology
|November 14, 2001
PubMed

Insights

Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL) is caused by NOTCH3 mutations. A new deletion causing an odd number of cysteine residues supports a unifying molecular hypothesis for CADASIL.

Area of Science:

  • Neurology
  • Genetics
  • Molecular Biology

Background:

  • Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukencephalopathy (CADASIL) is a hereditary cerebrovascular disorder.
  • It is characterized by recurrent strokes and progressive vascular dementia.
  • Mutations in the NOTCH3 gene are the known cause of CADASIL.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying CADASIL.
  • To identify novel mutations in the NOTCH3 gene associated with CADASIL.
  • To test the hypothesis that an altered cysteine residue count in EGF-like repeats is critical for CADASIL pathogenesis.

Main Methods:

  • Genetic analysis of patients with CADASIL.
  • Identification and characterization of NOTCH3 gene mutations.
  • Analysis of the impact of mutations on cysteine residue number in EGF-like repeats.

Main Results:

  • A novel in-frame deletion in NOTCH3 was identified, leading to the loss of three cysteine residues in EGF repeat 6.
  • This mutation results in an odd number of cysteine residues within this specific EGF-like repeat domain.
  • Previously identified CADASIL mutations also alter the cysteine count, typically resulting in an odd number.

Conclusions:

  • The findings support the hypothesis that an imbalance in cysteine residues (odd number) within NOTCH3 EGF-like repeats is a common critical event in CADASIL.
  • This alteration likely leads to unpaired, reactive cysteine residues, contributing to the disease pathology.
  • Understanding this unifying molecular mechanism may aid in developing targeted therapies for CADASIL.

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