Premium
Antibodies gone bad – the molecular mechanism of light chain amyloidosis
Author(s) -
Absmeier Ramona M.,
Rottenaicher Georg J.,
Svilenov Hristo L.,
Kazman Pamina,
Buchner Johannes
Publication year - 2023
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.16390
Subject(s) - immunoglobulin light chain , amyloidosis , fibril , antibody , amyloid fibril , disease , al amyloidosis , mechanism (biology) , medicine , mutation , amyloid (mycology) , secretion , chemistry , pathology , immunology , biochemistry , gene , amyloid β , philosophy , epistemology
Light chain amyloidosis (AL) is a systemic disease in which abnormally proliferating plasma cells secrete large amounts of mutated antibody light chains (LCs) that eventually form fibrils. The fibrils are deposited in various organs, most often in the heart and kidney, and impair their function. The prognosis for patients diagnosed with AL is generally poor. The disease is set apart from other amyloidoses by the huge number of patient‐specific mutations in the disease‐causing and fibril‐forming protein. The molecular mechanisms that drive the aggregation of mutated LCs into fibrils have been enigmatic, which hindered the development of efficient diagnostics and therapies. In this review, we summarize our current knowledge on AL amyloidosis and discuss open issues.