Zusammenfassung
Ziel
In unserer Studie reevaluierten wir die Histopathologie und Herkunft von Amyloid in Leberbiopsien.
Material und Methoden
Alle Leberbiopsien stammten aus einer Serie von 588 Fällen mit histologisch gesicherter Amyloidose, die zwischen 02/2006 und 01/2009 an das Amyloidregister der Charité eingesendet worden waren. Die Leberbiopsien waren formalinfixiert und in Paraffin eingebettet worden. Die Paraffinschnitte (3–5 μm) wurden mit HE und Kongorot gefärbt. Das Amyloid wurde immunhistochemisch klassifiziert mittels Antikörpern gegen die Amyloid-P-Komponente, AA-Amyloid, Apolipoprotein Al, Fibrinogen, Lysozym, λ- und κ-Leichtketten sowie Transthyretin.
Ergebnisse
Amyloid war enthalten in 46 Leberbiopsien (29 Männer, 17 Frauen; durchschnittliches Alter 60 Jahre, Umfang 34–87 Jahre). In 42 Fällen gelang eine immunhistochemische Klassifikation. Eine AL-Amyloidose lag in 40 (87%) Fällen vor, weiter differenziert wurde in AL-Amyloid vom λ- (26 Fälle, 57%) und vom κ-Leichtketten-Subtyp (14 Fälle, 30%). ATTR- und AA-Amyloidose wurden bei je einem Patienten (2%) nachgewiesen, bei 4 Patienten (9%) konnte das Amyloid nicht klassifiziert werden.
Fazit
Die hepatische Amyloidose ist am häufigsten eine AL-Amyloidose vom λ- and κ-Leichtketten-Subtyp und geht einher mit einer erheblichen Parenchymatrophie.
Abstract
Introduction
We reassessed the histopathology and origin of amyloid in liver biopsies.
Materials and Methods
All liver biopsies were retrieved from a series of 588 cases with histologically confirmed amyloidosis submitted between February 2006 and January 2009 to the Amyloid Registry of the Charité University Hospital. Liver biopsies had been fixed in formalin and embedded in paraffin. 3-5 μm thick paraffin sections were stained with hematoxylin and eosin and Congo red. Amyloid was classified immunohistochemically, using antibodies directed against amyloid P-component, AA amyloid, apolipoprotein AI, fibrinogen, lysozyme, λ- and κ-light chain, and transthyretin.
Results
Amyloid was found in 46 liver biopsies (29 men, 17 women; mean age 60 years, range 34-87 years). Immunohistochemical classification succeeded in 42 cases. AL amyloidosis was present in 40 (87%) cases and was further categorized into AL amyloid of λ-light chain origin in 26 (57%) cases, and κ-light chain origin in 14 (30%) cases. ATTR and AA amyloidosis were found in a single patient each (2%). In 4 (9%) cases, amyloid remained unclassified.
Conclusions
Hepatic amyloidosis is most commonly AL amyloid of λ- and κ-light chain origin and is often associated with marked parenchymal atrophy.
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Danksagung
Unser Projekt wurde teilfinanziert mit Mitteln der Europäischen Union (EU FP6 EURAMY) und des Deutschen Akademischen Austauschdienstes (DAAD). Wir möchten allen Pathologen danken, die uns amyloidhaltige Leberbiopsien zur immunhistochemischen Klassifizierung geschickt haben.
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Gioeva, Z., Kieninger, B. & Röcken, C. Amyloidose in Leberbiopsien. Pathologe 30, 240–245 (2009). https://doi.org/10.1007/s00292-009-1133-4
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DOI: https://doi.org/10.1007/s00292-009-1133-4