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By Friðjónsson, Jón

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Probands are identified by arrows. Blue diamonds denote ALS, orange FTD, and green both ALS and FTD in the same individual (adapted from Renton Neuron 72: 257 © 2011 Reprinted by permission from Elsevier) in sarcoma (FUS) were discovered to be present in a substantial fraction of the intracellular inclusions observed in not only ALS but also in frontotemporal lobar degeneration (FTLD). Mutations in these two proteins could directly account for another 10 % of the instances of FALS cases and some of the nonfamilial, or sporadic, cases, too.

The main tenet of the hypothesis is that the deposit of Aβ peptidein extracellular plaques arising from an imbalance between Aβ production and clearance leads to Alzheimer’s disease. This hypothesis had broad support from numerous findings in other major neurodegenerative diseases. However, there were also problems with this picture arising principally from the absence of correlations between these deposits and cognitive decline. Those observations were accompanied by a growing number of studies pointing to the possible involvement of the small, soluble oligomeric species of the same misfolded protein as the main culprits in the diseases.

Later in the same year, 1991, a pair of papers appeared reporting that Fragile X syndrome arises as a consequence of an unstable CGG repeat in the fragile X mental retardation 1 (FMR1) gene. In this case, the repeat expansion occurs in the nonprotein-coding 5ʹ UTR (untranslated region) of that gene. Other neurological disorders have been traced to unstable repeat expansions in nonprotein-coding regions, as well. That collection of illnesses includes myotonic (muscular) dystrophy and Friedrich’s ataxia among several others.

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A Course in Modern Icelandic by Friðjónsson, Jón


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