Light chain (AL), serum amyloid A (AA), transthyretin (ATTR), leukocyte cell derived chemotaxin 2 (ALECT2), and fibrinogen Aa (AFib) amyloidosis are some of the most common types of protein-deposition disorders involving the kidney. Each amyloidogenic protein differs in its origin and little is known about the exact mechanisms that govern renal tropism and tissue injury for each amyloid subtype. While amyloidogenic precursor protein is different in each subtype of amyloidosis, its aggregation into fibrils depositing in target organs and leading to disruption of tissue architecture and progressive organ failure is a common denominator. Each amyloidogenic protein is characterized by a unique pattern of deposition in the renal parenchyma with variability in expected clinical outcomes. In this review, we focus on describing the distinct pathophysiologic mechanisms at the level of the kidneys of AL, AA, ATTR, ALECT2, and AFib amyloidosis.
Hu et al. (2026) studied this question.