What is the pathophysiology of Amyloid A (AA) amyloidosis?

Medical Advisory BoardAll articles are reviewed for accuracy by our Medical Advisory Board
Article Review Status
Submitted
Under Review
Approved

Last updated: March 2, 2025 • View editorial policy

From the Guidelines

AA amyloidosis is a systemic disorder characterized by the extracellular deposition of amyloid A protein in various tissues and organs, triggered by persistent inflammation that leads to excessive production of serum amyloid A (SAA). The pathophysiology of AA amyloidosis begins with chronic inflammation, which stimulates the liver to synthesize SAA, an acute phase reactant, in response to pro-inflammatory cytokines like IL-1, IL-6, and TNF-α 1. During chronic inflammation, SAA levels can increase significantly, leading to abnormal processing of this protein and the formation of amyloid A fragments that are resistant to degradation. These fragments misfold into β-pleated sheet structures and aggregate to form amyloid fibrils that deposit in tissues, with proteoglycans and serum amyloid P component stabilizing these deposits and making them resistant to proteolysis. Key points about the pathophysiology of AA amyloidosis include:

  • Persistent inflammation triggers excessive SAA production
  • SAA is synthesized primarily by the liver in response to pro-inflammatory cytokines
  • Chronic elevation of SAA leads to the formation of amyloid A fragments and fibrils
  • Amyloid deposits can interfere with normal tissue architecture and function, leading to organ dysfunction
  • The kidneys, liver, spleen, adrenal glands, and gastrointestinal tract are commonly affected organs. As noted in the study by Bozkurt et al 1, anti-inflammatory therapies, such as anti-tumor necrosis factor used for the treatment of rheumatoid arthritis, have been shown to suppress serum amyloid A production, highlighting the importance of treating the underlying inflammatory condition to prevent progression of amyloidosis.

From the Research

Pathophysiology of Amyloid A (AA) Amyloidosis

The pathophysiology of Amyloid A (AA) amyloidosis involves the extracellular deposition of insoluble amyloid fibrils composed of amyloid A (AA) protein, an amino (N)-terminal fragment of serum amyloid A (SAA) 2, 3. This deposition disrupts tissue structure and compromises organ function, with the kidney being the most commonly affected organ 2, 3, 4.

Key Events in the Pathogenetic Cascade

  • The deposition of AA amyloid is preceded by a longstanding overproduction of SAA, which is induced by chronic inflammation 2, 5.
  • The time before amyloid deposition is determined by the circulating SAA concentration, with high levels of SAA expression inducing amyloidosis after a short delay 2.
  • Post-translational modifications (PTM) of AA protein, including carbamylation, acetylation, and oxidation, may play a role in fibrillogenesis 3.
  • The amyloid deposits can regress with restoration of normal SAA production, but reinduction of SAA overproduction can lead to rapid glomerular amyloid deposition and renal failure 2.

Organ Involvement

  • Renal involvement is the most common manifestation of AA amyloidosis, with almost all patients showing some degree of renal involvement 4.
  • Other organs, such as the heart, can also be affected, although this is less common 2.
  • The extent of organ involvement can vary widely between patients, and the disease can be systemic in nature 4.

Underlying Diseases and Inflammatory Markers

  • AA amyloidosis is typically associated with chronic inflammatory conditions, such as rheumatoid arthritis or Crohn's disease 4.
  • However, some patients may have idiopathic AA amyloidosis, with no known underlying inflammatory disease 4.
  • Inflammatory markers, such as interleukin-6, can be elevated in patients with AA amyloidosis, and may represent a therapeutic target 4.

References

Research

Pathogenetic mechanisms of amyloid A amyloidosis.

Proceedings of the National Academy of Sciences of the United States of America, 2013

Research

Post-translational modification of amyloid a protein in patients with AA amyloidosis.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2022

Research

AA amyloidosis: Mount Sinai experience, 1997-2012.

The Mount Sinai journal of medicine, New York, 2012

Research

Treatment strategies for amyloid A amyloidosis.

Expert opinion on pharmacotherapy, 2008

Professional Medical Disclaimer

This information is intended for healthcare professionals. Any medical decision-making should rely on clinical judgment and independently verified information. The content provided herein does not replace professional discretion and should be considered supplementary to established clinical guidelines. Healthcare providers should verify all information against primary literature and current practice standards before application in patient care. Dr.Oracle assumes no liability for clinical decisions based on this content.