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Amy Wyatt’s manuscript and artwork (pictured above) were recent... |
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Amy Wyatt, soon to receive her PhD, had her manuscript accepted (with... |
PhD student’s double success in overseas scientific journal
A soon-to-graduate PhD student under the supervision of Professor Mark Wilson in Biological Sciences had a manuscript accepted with no revisions requested by the prestigious USA-based scientific journal, The Journal of Biological Chemistry.
Amy Wyatt also submitted some artwork for consideration for the cover of the journal, which was also accepted for the recent edition.
The published journal article (284:21920-21927 [2009]) was titled “Structural characterisation of clusterin-client protein complexes” by Amy Wyatt, Dr Justin Yerbury, and Professor Mark Wilson.
Proteins are large biological molecules that perform many of the functions required to sustain life. For example, they give structure and strength to muscles, act as enzymes to allow us to digest food, and carry oxygen around in our bloodstream.
As a result of normal "wear and tear", soluble proteins eventually become "sticky" and join together with other worn proteins to form lumps (or aggregates) which fall out of solution.
These aggregates can accumulate in a variety of locations in the body and when they do, disease can result (e.g. the aggregation of a small protein in the brain is thought to underpin Alzheimer's disease).
Processes to inhibit protein aggregation inside cells in the body are well understood. However, as Amy’s manuscript highlighted, many protein aggregation diseases, including Alzheimer's disease, involve proteins found outside cells of the body.
“Remarkably, virtually nothing is known about the processes that operate to protect the body from diseases caused by protein aggregation outside cells,” Amy said.
Professor Wilson's laboratory is the first group in the world to describe how special proteins in blood (called "extracellular chaperones") act outside cells in the body to inhibit the inappropriate aggregation of proteins, to keep worn proteins soluble, and to help dispose of worn proteins without causing disease.
The recent publication in the Journal of Biological Chemistry describes a part of this story - specifically how it is that one of these extracellular chaperones (clusterin) holds worn proteins so that they remain soluble and do not form disease-causing lumps.