Fibril protein
Precursor protein
Systemic and/or localized
Acquired or hereditary
Target organs
AL
Immunoglobulin light chain
S, L
A, He
All organs except CNS (Local AL amyloidosis may occur)
AH
Immunoglobulin heavy chain
S, L
A
All organs except CNS (Local AH amyloidosis may occur)
AA
(Apo) Serum amyloid A
S
A
All organs except CNS
ATTR
Transthyretin, wild type
S
A
Heart mainly in males, Ligaments, Tenosynovium
Transthyretin, variants
S
H
PNS, ANS, heart, eye, leptomeninges
Aβ2M
β2-Microglobulin, wild type
L
A
Musculoskeletal system
β2-Microglobulin, variant
S
H
ANS
AApoAI
Apolipoprotein A I, variants
S
H
Heart, liver, kidney, PNS, testis, larynx (C terminal variants), skin (C terminal variants)
AApoAII
Apolipoprotein A II, variants
S
H
Kidney
AApoAIV
Apolipoprotein A IV, wild type
S
A
Kidney medulla and systemic
AGel
Gelsolin, variants
S
H
PNS, cornea
ALys
Lysozyme, variants
S
H
Kidney
ALECT2
Leukocyte chemotactic factor-2
S
A
Kidney, primarily
AFib
Fibrinogen α, variants
S
H
Kidney, primarily
ACys
Cystatin C, variants
S
H
PNS, skin
ABri
ABriPP, variants
S
H
CNS
ADanb
ADanPP, variants
L
H
CNS
Aβ
Aβ protein precursor, wild type
L
A
CNS
Aβ protein precursor, variant
L
H
CNS
APrP
Prion protein, wild type
L
A
CJD, Fatal insomnia
Prion protein variants
L
H
CJD, GSS syndrome, Fatal insomnia
ACal
(Pro)calcitonin
L
A
C-cell thyroid tumors
AIAPP
Islet amyloid polypeptidec
L
A
Islets of langerhans, Insulinomas
AANF
Atrial natriuretic factor
L
A
Cardiac atria
APro
Prolactin
L
A
Pituitary prolactinomas, aging pituitary
AIns
Insulin
L
A
Iatrogenic, local injection
ASpcd
Lung surfactant protein
L
A
Lung
AGal7
Galectin 7
L
A
Skin
ACor
Corneodesmosin
L
A
Cornified epithelia, Hair follicles
AMed
Lactadherin
L
A
Senile aortic, Media
AKer
Kerato-epithelin
L
A
Cornea, hereditary
ALac
Lactoferrin
L
A
Cornea
AOAAP
Odontogenic ameloblast-associated protein
L
A
Odontogenic tumors
ASem1
Semenogelin 1
L
A
Vesicula seminalis
AEnf
Enfurvitide
L
A
Iatrogenic, local injection
Diagnosis of Amyloidosis
The introduction of the cotton dye Congo red was a great step forward in the identification of amyloid [32]. The dye was synthesized in 1883 for the textile industry, and there is evidence that its name has a firm connection with a political conference, held in Berlin in 1884–1885, where the colonial powers discussed Central Africa; thus, the name has nothing to do with the origin of the dye [33]. Congo red was introduced as an intravenous test for systemic amyloidosis in patients, since deposits in the tissues bound the dye, and enhanced plasma clearance was taken as a sign of disease [34]. A quite substantial amount of Congo red was injected, often more than 10 ml of a 1 % aqueous solution of the dye [35]. Although unreliable and potentially dangerous, this test seems to have continued in use until the 1970s [36, 37]. This can seem surprising to us now, when some laboratories hesitate to utilize Congo red in histopathology due to its potential to be carcinogenic [38]. As early as 1884, the dye was tested as a histological stain [39], but it was not until 1927 that its properties as an amyloid stain were described [26]. At that time, a very important property of amyloid stained with Congo red was identified: namely, the enhanced birefringence of amyloid in tissue sections viewed under polarized light [26]. In fact, this technique is still used in diagnostic work throughout the world. Diagnostic biopsies from organs showing symptoms had been used for some time (for examples and references, see [40]), but it was not until 1960 that the well-known rectal biopsy was introduced as a diagnostic tool for systemic amyloidosis [41]. This was a most important advance, since before 1950, only 7 % of patients were diagnosed before death [42]. The technique most commonly used today, biopsy from subcutaneous fat tissue, was developed a decade later in the 1970s [43]. Since then, biopsy techniques have been further expanded to include determination of the biochemical nature of an amyloid deposit; today, this is considered to be a necessary step in the clinical handling of patients with systemic amyloidosis. Although a biopsy with microscopic demonstration of amyloid is still the only way to obtain a diagnosis, a method for visualizing amyloid in vivo based on the ubiquitously present serum amyloid P (SAP) component has been successfully developed [44].