Trusted Resources: Education
Scientific literature and patient education texts
Hereditary Fibrinogen Aα-Chain Amyloidosis
source: University College London
year: N/A
summary/abstract:Amyloidosis is a rare disease caused by abnormal deposition and accumulation of proteins in the tissues of the body. Amyloid deposits are primarily made up of protein fibres known as amyloid fibrils. These amyloid fibrils are formed when normally soluble body proteins aggregate (clump together) and then remain in the tissues instead of being safely cleared away. About 30 different proteins are known to form amyloid deposits in humans.
These amyloid forming proteins are known as ‘precursor proteins’. Amyloid deposits cause disease by gradually accumulating within organs and thereby disrupting the structure and damaging the function of the affected tissues.
read moreRelated Content
-
How Can I Avoid Fluid Balance Problems?Many patients with AL amyloidosis should...
-
Alkylating Agents – ASG Webinar 2/13https://www.youtube.com/watch?v=4gUXPbOk...
-
Emerging Treatments for AmyloidosisAmyloidosis results from protein misfold...
-
Charlotte HaffnerCharlotte Haffner is the first Vanderbil...
-
Fred Hutchinson Cancer Research CenterFred Hutch is at the forefront of develo...
-
Cardiac Amyloidosis: Pathology, Nomenclature, and TypingAmyloidosis is an increasingly recognize...
-
ISA 2020 | AA Amyloidosis Managementhttps://www.youtube.com/watch?v=gENrlj8U...
To improve your experience on this site, we use cookies. This includes cookies essential for the basic functioning of our website, cookies for analytics purposes, and cookies enabling us to personalize site content. By clicking on 'Accept' or any content on this site, you agree that cookies can be placed. You may adjust your browser's cookie settings to suit your preferences.
More information
The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this.
To improve your experience on this site, we use cookies. This includes cookies essential for the basic functioning of our website, cookies for analytics purposes, and cookies enabling us to personalize site content. By clicking on 'Accept' or any content on this site, you agree that cookies can be placed. You may adjust your browser's cookie settings to suit your preferences.
More information
The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this.