New sensitive method for early detection of amyloidosis in humans

March 21, 2016

A team of scientists at Sweden's Linköping University has developed a molecular probe that can detect an array of different amyloid deposits in several human tissues. This new probe is extremely sensitive and was used at very low concentrations to correctly identify every positive amyloidosis sample when compared to the traditional clinical tests. The probe also picked up some amyloidosis signals that the traditional methods were unable to detect. This result means that the new probe could be used to detect amyloidosis before symptoms present, leading to faster and hence more effective treatment.

Amyloidosis is a general term for several different types of disease. Aggregates of form and deposit in different tissues which can affect the normal function. As the disease progresses and amyloid deposits grow, tissues become irreversibly damaged. Amyloid deposits can be found in many different organs leading to a wide range of possible symptoms and making diagnosis challenging.

To date, the primary mode of diagnosis for amyloidosis has been the Congo red stain. However, evidence from the Linköping team, presented in Amyloid Journal show that their new is much more sensitive, being able to detect small in samples that were previously determined to be amyloid-free.

"Given the sensitivity of the probe, we think this would make an excellent complement to traditional methods and could eventually be a replacement", says lead investigator Per Hammarström, professor at Linköping University.

According to the U.S. Office of Rare Diseases (ORD), a subsidiary of the National Institute of Health (NIH), amyloidosis is a rare disease, affecting less than 200,000 people in the U.S.. However, The Amyloidosis Foundation suspects that the figures are underreported and that amyloidosis is not that rare - just rarely diagnosed. A more sensitive diagnostic method would help to uncover the reality of the situation.

The Linköping team are optimistic about the use of the probe.

"It could also be used to identify new types of amyloids and presymptomatic patients who are at risk of developing the disease", says Hammarström and collaborator professor Peter Nilsson.

Research is continuing in this important field. In the future, the researchers hope to apply this to other diseases where amyloids are present and develop real-time, non-invasive diagnostic probes.

Explore further: Evidence for a remarkable structural diversity of amyloid fibrils in human and animal tissue

More information: Daniel Sjölander et al. Establishing the fluorescent amyloid ligand h-FTAA for studying human tissues with systemic and localized amyloid, Amyloid (2016). DOI: 10.3109/13506129.2016.1158159

Related Stories

Evidence for a remarkable structural diversity of amyloid fibrils in human and animal tissue

March 15, 2016
Formation of amyloid fibrils is a characteristic feature of neurogenerative diseases like Alzheimer's. As published in the journal Angewandte Chemie, German and American scientists have found evidence that these fibrils adopt ...

Amyloid imaging shows promise for detecting cardiac amyloidosis

February 4, 2013
While amyloid imaging may now be most associated with detecting plaques in the brain, it has the potential to change the way cardiac amyloidosis is diagnosed. According to first-of-its-kind research published in the February ...

Improving treatment for systemic amyloidosis

July 16, 2015
A potential new approach to treat systemic amyloidosis, invented at UCL and being developed by GlaxoSmithKline (GSK), marks the start of a successful and innovative academic-industry collaboration.

Amyloid scan of the heart predicts major cardiac events

June 8, 2015
Amyloid build-up is commonly talked about in relation to Alzheimer's disease, but amyloidosis can be found throughout the body. An excessive accumulation of these insoluble proteins could cause a heart attack or even death. ...

Amyloid formation may link Alzheimer disease and type 2 diabetes

February 17, 2015
The pathological process amyloidosis, in which misfolded proteins (amyloids) form insoluble fibril deposits, occurs in many diseases, including Alzheimer disease (AD) and type 2 diabetes mellitus (T2D). However, little is ...

Recommended for you

Alzheimer's Tau protein forms toxic complexes with cell membranes

November 22, 2017
The brains of patients with Alzheimer's disease contain characteristic tangles inside neurons. These tangles are formed when a protein called Tau aggregates into twisted fibrils. As a result, the neurons' transport systems ...

Researchers reveal new details on aged brain, Alzheimer's and dementia

November 21, 2017
In a comprehensive analysis of samples from 107 aged human brains, researchers at the Allen Institute for Brain Science, UW Medicine and Kaiser Permanente Washington Health Research Institute have discovered details that ...

Dementia study sheds light on how damage spreads through brain

November 20, 2017
Insights into how a key chemical disrupts brain cells in a common type of dementia have been revealed by scientists.

Researchers describe new biology of Alzheimer's disease

November 20, 2017
In a new study, researchers from Boston University School of Medicine (BUSM) describe a unique model for the biology of Alzheimer's disease (AD) which may lead to an entirely novel approach for treating the disease. The findings ...

Study shows video games could cut dementia risk in seniors

November 16, 2017
Could playing video games help keep the brain agile as we age?

New player in Alzheimer's disease pathogenesis identified

November 14, 2017
Scientists at Sanford Burnham Prebys Medical Discovery Institute (SBP) have shown that a protein called membralin is critical for keeping Alzheimer's disease pathology in check. The study, published in Nature Communications, ...

0 comments

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.