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Common Cause For Folding Diseases?

  April, 8 2002 8:14
your information resource in human molecular genetics
Diseases as diverse as Alzheimer's, diabetes and Creutzfeldt–Jacob disease (CJD) may have a common molecular foundation: protein misfolding. So suggests this week's Nature (Vol. 416, No. 6880, 04 Apr 02), hinting that breaking up rogue protein gangs could be a way to attack such diseases.

Small clumps of misshapen protein can damage cells, researchers have found. This is true for proteins in general and for the proteins that accumulate in the brains of Alzheimer's patients.

Christopher Dobson of the University of Cambridge, UK, and colleagues persuaded normally harmless proteins, one from bacteria and the other from cattle, to take on a new shape. This made them toxic to cells in culture. The rogue proteins were most damaging in small groups, before they formed into large insoluble clusters.

Meanwhile, Dennis Selkoe, of Harvard Medical School and the Brigham and Women’s Hospital, Boston, and colleagues, have found that small clusters of amyloid beta molecules, the misfolded protein that accumulates in much bigger clumps in the brains of Alzheimer's patients, disrupt the synapses in rat brains.

Researchers have argued over whether amyloid beta is toxic, or whether it is a consequence, rather than a cause of Alzheimer's. Pinning a specific form of damage on the molecule in living animals could help settle this debate.

"These ideas highlight the importance of understanding the cellular mechanisms that combat these potentially lethal mistakes, and identifying the precise cellular targets of those aggregates that escape such surveillance," say R. John Ellis and Teresa J. T. Pinheiro of the University of Warwick, UK, in an accompanying News and Views article.


Christopher Dobson
tel +44 1223 763 070
e-mail cmd44@cam.ac.uk

Dennis Selkoe
tel +1 617 525 5200
e-mail dselkoe@rics.bwh.harvard.edu

R. John Ellis
tel +44 2476 523509,
e-mail jellis@bio.warwick.ac.uk

(C) Nature press release.

Message posted by: Trevor M. D'Souza

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