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Amyloidosis is the accumulation of misfolded protein fibers in the body that can be associated with many chronic illnesses. Even though amyloidosis is common in chronic kidney disease (CKD) patients receiving chronic regular dialysis, it has also been reported in a patient with chronic kidney failure but who never received dialysis.
Amyloid light-chain (AL) amyloidosis, also known as primary amyloidosis, is the most common form of systemic amyloidosis. [1] The disease is caused when a person's antibody -producing cells do not function properly and produce abnormal protein fibers made of components of antibodies called light chains .
To date, 37 human proteins have been found to form amyloid in pathology and be associated with well-defined diseases. [2] The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by TTR). [3]
[19] [20] The vast majority of proteins that have been found to form amyloid deposits are secreted proteins, so the misfolding and formation of amyloid occurs outside cells, in the extracellular space. [19] Of the 37 proteins so far identified as being vulnerable to amyloid formation, only four are cytosolic. [19]
The most common presentation of AA amyloidosis is renal in nature, including proteinuria, nephrotic syndrome and progressive development of chronic kidney disease leading to end stage kidney disease (ESKD) and need for renal replacement therapy (e.g. dialysis or kidney transplantation). [3]
Familial renal amyloidosis is a form of amyloidosis primarily presenting in the kidney. [1] It is associated most commonly with congenital mutations in the fibrinogen alpha chain and classified as a dysfibrinogenemia (see Hereditary Fibrinogen Aα-Chain Amyloidosis). [2] [3] and, less commonly, with congenital mutations in apolipoprotein A1 [4 ...
Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor [5] and has been implicated as a regulator of synapse formation, [6] neural plasticity, [7] antimicrobial activity, [8] and iron export. [9]
LECT2 Amyloidosis (ALECT2) is a form of amyloidosis caused by the LECT2 protein. It was found to be the third most common (~3% of total) cause of amyloidosis in a set of more than 4,000 individuals studied at the Mayo Clinic; the first and second most common forms the disorder were AL amyloidosis and AA amyloidosis, respectively.