AFib E85.2

Hereditary fibrinogen Aα-chain amyloidosis (Aα-chain amyloidosis) is a form of autosomal dominant systemic amyloidosis caused by mutations in the fibrinogen Aα-chain gene (FGA).

Predominantly Caucasian patients. Rarely Asians.

Amyloidoses are a rare and heterogeneous group of diseases characterized by the deposition of abnormally folded proteins in tissues, ultimately leading to organ damage. The deposits are mainly extracellular and can be identified by their affinity for Congo red and their yellow-green birefringence under polarized light. The current classification of amyloid in medical practice is based on the type of amyloid protein. To date, 36 proteins have been identified as amyloidogenic in humans. In clinical practice, it is critical to distinguish between treatable and nontreatable amyloidoses. In addition, amyloidoses with a genetic component must be distinguished from sporadic types and systemic amyloidoses from localized forms.

Determination of amyloid protein type is essential before specific therapy can be initiated.Early diagnosis of hereditary amyloidosis remains a major challenge and requires the involvement of many clinical and laboratory specialties.

Clinically, the most prominent manifestation in patients with Aα-chain amyloidosis is progressive nephropathy caused by excessive amyloid deposition in the glomeruli. Petechiae of the skin are found regularly.

Chemotherapy, renal transplantation (Ceglarz K et al. 2023).

1. Ceglarz K et al (2023) Difficulties in the Diagnosis of Fibrinogen Aα-Chain Amyloidosis-Literature Review and Case Report of a Patient After Kidney Transplantation. Transplant Proc 55: 644-648.
2. Mousson C et al (2006) Successful hepatorenal transplantation in hereditary amyloidosis caused by a frame-shift mutation in fibrinogen Aalpha-chain gene. Am J Transplant 6:632-635.
3. Picken MM (2020) The pathology of amyloidosis in classification: A review. Acta Haematol 143:322-334.
4. Yazaki M et al (2018) Hereditary fibrinogen Aα-chain amyloidosis in Asia: Clinical and Molecular Characteristics. Int J Mol Sci 19:320.