Aspects of the History and Nomenclature of Amyloid and Amyloidosis


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 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


From Sipe et al. [12]

aProteins are listed, when possible, according to relationship. Thus, apolipoproteins are grouped together, as are polypeptide hormones

bADan is the product of the same gene as ABri

cAlso called amylin

dNot proven by amino acid sequence analysis

eBenson et al. [46]





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].

Only gold members can continue reading. Log In or Register to continue

Stay updated, free articles. Join our Telegram channel

May 14, 2017 | Posted by in PATHOLOGY & LABORATORY MEDICINE | Comments Off on Aspects of the History and Nomenclature of Amyloid and Amyloidosis

Full access? Get Clinical Tree

Get Clinical Tree app for offline access