One step closer in finding treatment for amyloidosis

Oct 21, 2010
Image: Professor Mark Pepys

University College London scientists funded by the Medical Research Council (MRC) have devised a new approach to treatment of amyloidosis, according to new research published yesterday in Nature.

Systemic amyloidosis is a serious and usually fatal disease that can affect virtually any organ in the body. It is the cause of death in one per thousand of the population in developed countries.

Amyloid is composed of fibres that are deposited in the body’s tissues, damaging their structure and function. Diagnosis is often difficult and delayed so that, by the time the disease is recognised, most patients already have irreversible organ damage. The SAP protein from the blood accumulates in amyloid deposits and contributes to their formation and persistence.In work supported by the MRC spanning 30 years, Professor Mark Pepys FRS and his team from UCL discovered the role of SAP in amyloidosis and have been developing new treatments aimed at it. Initially they partnered with Roche to develop a small molecule drug, called CPHPC, which removes SAP from the blood but only partly clears it from amyloid deposits. This treatment stopped the accumulation of new amyloid but did not clear the existing deposits.

The latest development uses CPHPC to first remove SAP from that the blood so that antibodies to SAP can then be safely given to target the residual SAP in the amyloid deposits. In experimental models closely resembling human disease, this treatment swiftly eliminated all the amyloid. The next stage will be to test the treatment in patients and work towards clinical trials is now proceeding in collaboration with GlaxoSmithKline.

Professor Pepys, Director of the UCL Centre for Amyloidosis and Acute Phase Proteins, said: “Our findings open up the prospect of a successful treatment for patients with and we are looking forward to developing the drugs for testing in the first human studies.”

Explore further: Clipping proteins that package genes may limit abnormal cell growth in tumors

More information: The paper “Antibodies to human serum amyloid P component eliminate visceral amyloid deposits” was published yesterday in Nature.

Related Stories

Researcher determines link between foie gras and diseases

Jun 18, 2007

University of Tennessee Graduate School of Medicine professor and researcher Alan Solomon, M.D., director of the Human Immunology and Cancer/Alzheimer’s Disease and Amyloid-Related Disorders Research Program, led a team ...

New therapy targets for amyloid disease

Dec 04, 2009

A major discovery is challenging accepted thinking about amyloids - the fibrous protein deposits associated with diseases such as Alzheimer's and Parkinson's - and may open up a potential new area for therapeutics.

Give the foie gras a miss

Feb 10, 2009

Another reason not to eat pate de foie gras is discussed by Michael Greger of The Humane Society of the United States, Washington DC in a forthcoming issue of the International Journal of Food Safety, Nutrition and Public Health. ...

Recommended for you

Organovo has 3D-printed liver tissue for drug testing

Nov 20, 2014

(Medical Xpress)—The commercial release of 3D printed liver tissue was announced earlier this week. Organovo is the company behind the release. The product is intended for use for preclinical drug discovery ...

User comments : 1

Adjust slider to filter visible comments by rank

Display comments: newest first

Mangelamy
not rated yet Oct 21, 2010
For more information on amyloidosis see below.

AMYLOIDOSIS SUPPORT GROUPS
ASG wwwamyloidosissupport
Toll Free 866-404-7539
National Organization Member of NORD
amyloidosisonline - Over 885 have joined

"Don't Take Your Organs To Heaven, Heaven Knows We Need Them Here"

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.