Visceral organ involvement and extracellular matrix changes in beta 2-microglobulin amyloidosis--a comparative study with systemic AA and AL amyloidosis

• Published in: Virchows Archiv : an international journal of pathology Vol. 430; no. 6; pp. 479 - 487
• Main Authors: Ohashi, K, Takagawa, R, Hara, M
• Format: Journal Article
• Language: English
• Published: Germany 01-06-1997
• Subjects: Adult; Aged; Aged, 80 and over; Amyloid - analysis; Amyloid beta-Protein Precursor - analysis; Amyloidosis - classification; Amyloidosis - metabolism; Amyloidosis - pathology; beta 2-Microglobulin - analysis; Cardiomyopathies - metabolism; Cardiomyopathies - pathology; Chondroitin Sulfates - metabolism; Digestive System - chemistry; Extracellular Matrix - metabolism; Female; Gastrointestinal Diseases - metabolism; Gastrointestinal Diseases - pathology; Heparitin Sulfate - metabolism; Humans; Male; Middle Aged; Myocardium - chemistry; Renal Dialysis
• ISSN: 0945-6317; 1432-2307
• DOI: 10.1007/s004280050058

Patterns of amyloid distribution and extracellular matrix changes in the heart and gastrointestinal tract were compared among beta 2-microglobulin (B2M), AA (secondary), and AL (primary and multiple myeloma-associated) amyloidosis cases. B2M amyloid was found to be mainly distributed in the small arterioles, venules, endocardium and muscularis propria of these organs, the deposits characteristically forming subendothelial nodular lesions in the vessels. A marked increase of chondroitin sulfate (CS) was consistently detected in B2M amyloid. Heparan sulfate (HS) also showed an increase in amyloid deposits, but with less reactivity than CS in the small arterioles or venules. Basement membrane structures stained positively for laminin and collagen type IV were replaced by negative amyloid deposits. In the AL cases, the muscularis propria of the gastrointestinal tract was involved in amyloid deposits, as seen for the B2M type, but the vascular amyloid deposits were localized in the media and adventitia of larger vessels. Immunoreactivity for HS was more intense than that for CS, and no increase in laminin or collagen type IV was observed. In the AA cases, amyloid deposits were distributed in the capillaries, small arterioles, interstitium of the myocardium and mucosa. Immunoreactivity for laminin and collagen type IV was marked, and more intense than that for HS and CS. Although the existence of a direct relationship between increase in extracellular matrix material and amyloidogenesis remains to be proven, the observed variation in extracellular matrix changes in the background of each type of amyloidosis may indicate different binding sites of the amyloid precursor proteins, resulting in the specific histological features and distribution.