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Better alone than in bad company

Researchers identify new protein involved in amyloid aggregation

Oeiras, 19.10.2012

Toxic protein aggregates are a hallmark of many neurodegenerative diseases where specific proteins play the starring role. This is the case of amyotrophic lateral sclerosis (ALS), where progressive degeneration of motor neurons is associated to aggregation of the SOD1 protein. Now researchers from the Protein Folding Biochemistry and Stability Lab and co-workers uncover a potential new player in the protein aggregation process, which seems to take aggregation even further. Results are published this week in the online version of The Journal of Biological Chemistry.

Stimulated by the observation that S100A6 protein occurs at abnormally elevated levels in ALS patients, researchers investigated its ability to form amyloids, the designation given to the fibrous protein aggregates observed in this and other disorders. Indeed, S100A6 aggregated into amyloid in the test tube under physiological conditions, a process influenced by calcium, an activator of S100A6 and an important player in neuronal function. Further, amyloid precursors – typically responsible for disease-related toxicity – decreased the viability of nervous cells in culture by up to 40%. Researchers were further convinced of the possible contribution of S100A6 protein to ALS after observing in vitro how it speeded the aggregation of the ALS disease indicator, SOD1.

Original Article

Journal of Biological Chemistry (2012) doi: 10.1074/jbc.M112.396416

S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation

Hugo M. Botelho1, Sónia S. Leal1, Isabel Cardoso2,3, Kiran Yanamandra4, Ludmilla A. Morozova-Roche4, Günter Fritz5, Cláudio M. Gomes1

1 Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal
2 Molecular Neurobiology Unit, Instituto de Biologia Molecular e Celular, Porto, Portugal
3 Escola Superior Tecnologia Saúde Porto, Instituto Politécnico do Porto, Vila Nova de Gaia, Portugal
4 Department of Medical Biochemistry and Biophysics, Umeå University, Sweden
5 Department of Neuropathology, University of Freiburg, Germany


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