A finding by an international team of plant biologists could be important in research into Alzheimer's and other age-related diseases.The study is published this week in the prestigious journal Proceedings of the National Academy of Sciences, and presents new data on the degradation of short peptides (chains of amino acid molecules) in cells.
The work is significant because it throws more light on the role of proteases, or enzymes, in disease in plants and animals, including humans.
The scientists identified and characterised a novel OligoPeptidase (OOP) from thale cress, a model organism often studied by molecular biologists. OOP degrades small peptides that are produced following the import of proteins into mitochondria and chloroplasts. Import of proteins into these organelles is essential for cellular function and the small peptides must be destroyed because they become toxic to the cell.
"The characterisation of these pathways for peptide degradation in model species is essential for understanding the role of proteases in disease in plants and animals", said Professor Jim Whelan of UWA and La Trobe.
Presequence Protease (PreP), which was also first extensively characterised in plants, has ability to degrade the peptide beta-amyloid that forms insoluble fibres in the brain of Alzheimer's patients.
"We believe the OOP and PreP co-operate to completely break down harmful peptides that accumulate and adversely affect mitochondrial activities," said Elzbieta Glaser, Professor of Biochemistry at the University of Stockholm.
"It will be very interesting to study the human variant of OOP, and examine its role in the degradation of amyloid-beta peptide. It may be of importance for research in Alzheimer's disease and other age-related diseases."
Explore further: Amyloid formation: Designer proteins light the way forward
More information: www.pnas.org/content/early/2013/09/11/1307637110.full.pdf+html
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A finding by an international team of plant biologists could be important in research into Alzheimer's and other age-related diseases.The study is published this week in the prestigious journal Proceedings of the National Academy of Sciences, and presents new data on the degradation of short peptides (chains of amino acid molecules) in cells.
The work is significant because it throws more light on the role of proteases, or enzymes, in disease in plants and animals, including humans.
The scientists identified and characterised a novel OligoPeptidase (OOP) from thale cress, a model organism often studied by molecular biologists. OOP degrades small peptides that are produced following the import of proteins into mitochondria and chloroplasts. Import of proteins into these organelles is essential for cellular function and the small peptides must be destroyed because they become toxic to the cell.
"The characterisation of these pathways for peptide degradation in model species is essential for understanding the role of proteases in disease in plants and animals", said Professor Jim Whelan of UWA and La Trobe.
Presequence Protease (PreP), which was also first extensively characterised in plants, has ability to degrade the peptide beta-amyloid that forms insoluble fibres in the brain of Alzheimer's patients.
"We believe the OOP and PreP co-operate to completely break down harmful peptides that accumulate and adversely affect mitochondrial activities," said Elzbieta Glaser, Professor of Biochemistry at the University of Stockholm.
"It will be very interesting to study the human variant of OOP, and examine its role in the degradation of amyloid-beta peptide. It may be of importance for research in Alzheimer's disease and other age-related diseases."
Explore further: Amyloid formation: Designer proteins light the way forward
More information: www.pnas.org/content/early/2013/09/11/1307637110.full.pdf+html
Medical Xpress on facebook
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Amyloid formation: Designer proteins light the way forward
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Insight into the mechanism of protein aggregation provides a model system that could lead to treatments for several associated diseases
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Feb 01, 2013
A research team in Israel has devised a novel approach to identifying the molecular basis for designing a drug that might one day decrease the risk diabetes patients face of developing Alzheimer's disease. The team will present ...
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Jan 12, 2012
More than half of all cases of dementia in the elderly can be attributed to Alzheimer's disease. Despite vast research efforts, an effective therapy has not been developed, and treatment consists of dealing with the symptoms. ...
Researchers find new piece in Alzheimer's puzzle
Feb 25, 2009
Yale researchers have filled in a missing gap on the molecular road map of Alzheimer's disease. In the Feb. 26 issue of the journal Nature, the Yale team reports that cellular prion proteins trigger the process by which ...
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In a landmark discovery, the final piece in the puzzle of understanding how the brain circuitry vital to normal fertility in humans and other mammals operates has been put together by researchers at New Zealand's University ...
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