Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis

DA Figlewicz, A Krizus, MG Martinoli… - Human molecular …, 1994 - academic.oup.com
DA Figlewicz, A Krizus, MG Martinoli, V Meininger, M Dib, GA Rouleau, JP Julien
Human molecular genetics, 1994academic.oup.com
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder primarily affecting motor
neurons. The etiology of the majority of cases remains unknown. Recent findings from
several laboratories suggest a role for neurofilaments in the development of motor neuron
disorders. The C-terminal region of the human neurofilament heavy subunit (NEFH) contains
a unique functional domain consisting of 43 repeat motifs of the amino acids Lys-Ser-Pro
(KSP). This C-terminal region of NEFH forms the sidearm projections which cross-link the …
Abstract
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder primarily affecting motor neurons. The etiology of the majority of cases remains unknown. Recent findings from several laboratories suggest a role for neurofilaments in the development of motor neuron disorders. The C-terminal region of the human neurofilament heavy subunit (NEFH) contains a unique functional domain consisting of 43 repeat motifs of the amino acids Lys-Ser-Pro (KSP). This C-terminal region of NEFH forms the sidearm projections which cross-link the neurofilaments. Previously, we have demonstrated polymorphism in the C-terminal region of the human NEFH: an allelic variant of a slightly larger molecular size, containing an additional KSP phosphorylation motif. Novel mutations in this region were found in five ALS patients. We propose that changes in the KSP-repeat domain may affect the cross-linking properties of the heavy neurofilament subunit and perhaps contribute to the development of neurofilamentous swellings in motor neurons, a hallmark of ALS.
Oxford University Press