Amyloidosis

Types of amyloidosis

Amyloidosis is not one disease but a family of distinct disorders, each defined by the type of protein that misfolds and the organs it affects. Understanding each type is the first step toward accurate diagnosis and targeted treatment.

Medical illustration · protein fibril diagram

01

The wide diversity of amyloidosis

More than 40 human precursor proteins are known to form amyloid deposits. Amyloidosis is classified according to the protein forming the fibrils. The most common systemic forms, AL, ATTR, and AA, each involve different precursor proteins, affect different organ systems, and require fundamentally different treatment strategies.

Because symptoms often mimic those of more common diseases, correct typing is essential and requires specialist testing. Early, accurate typing is the foundation of effective care.

AL amyloidosis · plasma cell pathology · microscopy

02 · Systemic

AL amyloidosis

AL (light chain) amyloidosis is caused by an abnormal proliferation of plasma cells in the bone marrow that produce misfolded immunoglobulin light chains. These fragments deposit as amyloid fibrils, principally in the heart and kidneys, but potentially in any organ.

It is the most common form of systemic amyloidosis in developed countries. Treatment targets the underlying plasma cell disorder, typically with chemotherapy protocols similar to those used in multiple myeloma.

03 · Systemic

ATTR amyloidosis

ATTR (transthyretin) amyloidosis occurs when the liver-produced transthyretin protein becomes unstable and misfolds. It primarily affects the heart and peripheral nervous system and exists in two distinct forms with different causes and treatment pathways.

Wild-type ATTR

Occurs spontaneously with age, and is not inherited. Most commonly presents as cardiomyopathy in older men. Increasingly recognised thanks to improved cardiac imaging.

Hereditary ATTR

Caused by a genetic mutation in the TTR gene. Inherited in an autosomal dominant pattern. Onset and organ involvement vary by specific mutation; neuropathy is a hallmark feature.

ATTR amyloidosis · cardiac imaging · echocardiogram
AA amyloidosis · chronic inflammation · tissue biopsy

04 · Systemic

AA amyloidosis

AA amyloidosis arises as a secondary complication of persistent systemic inflammation. The culprit protein, serum amyloid A (SAA), is an acute-phase reactant produced by the liver in response to chronic inflammatory states such as rheumatoid arthritis, inflammatory bowel disease, or chronic infections.

The kidneys are the primary target, leading to proteinuria and progressive renal failure. Treatment aims to control the underlying inflammatory or infectious disease and suppress production of serum amyloid A (SAA).

05

Rarer hereditary types

Beyond ATTR, a number of other gene mutations cause rarer hereditary forms of systemic amyloidosis. Each is defined by its precursor protein and carries its own pattern of organ involvement. Genetic testing is essential for diagnosis and has implications for family members.

AAPOA1

Apolipoprotein A-I mutation. Affects kidneys, liver, and peripheral nerves. Autosomal dominant inheritance.

AGEL

Gelsolin mutation. Principally causes cranial neuropathy and corneal lattice dystrophy. Most prevalent in Finland.

ALYS

Lysozyme mutation. Primarily renal involvement with hepatic deposits. British cases historically documented.

AFib

Fibrinogen A-alpha chain mutation. Exclusively renal disease; one of the more common hereditary forms in Western Europe.

Genetic counselling · rare hereditary amyloidosis
Localized amyloidosis · bronchial deposit · endoscopy

06 · Localized

Localized amyloidosis

Unlike systemic forms, localized amyloidosis is confined to a single organ or tissue, most commonly the airways, skin, bladder, or orbit. The amyloid is produced locally by resident plasma cells and does not spread systemically.

Prognosis is generally more favourable than systemic disease, as vital organ function is rarely compromised. Management depends on the site of involvement and the extent of local tissue damage.

07

Compare types

A quick-reference overview of the principal amyloidosis types — protein, primary organs affected, treatment approach, and where to find out more.

TypeProteinPrimary organsTreatment approachLearn more
ALImmunoglobulin light chainsHeart, kidneys, liver, nerves, soft tissuesPlasma cell-directed chemotherapy; stem cell transplant in eligible patientsAL amyloidosis →
ATTR — Wild-typeTransthyretin (wild-type)Heart (cardiomyopathy)TTR stabilisation and supportive cardiac care; approved indications and availability vary between countries.wtATTR amyloidosis →
ATTR — HereditaryTransthyretin (mutant)Peripheral nerves, heart (mutation-dependent)TTR silencers (siRNA, ASO); stabilisers; liver transplant (select mutations)hATTR amyloidosis →
AASerum amyloid A (SAA)Kidneys, liver, spleenControl of underlying inflammatory disease; anti-IL-1 agentsAA amyloidosis →
Rarer hereditaryApoA-I, Gelsolin, Lysozyme, Fibrinogen…Type-dependent (kidneys, nerves, liver)Supportive; organ transplant in selected casesRare hereditary amyloidosis →

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Read next

AL amyloidosis

The most common systemic form in Western countries, caused by misfolded immunoglobulin light chains.

TTR amyloidosis

Wild-type and hereditary forms of transthyretin amyloidosis, and how they differ from one another.

Rare hereditary amyloidosis

The rarer inherited forms, the proteins involved, and the organs they typically affect.