PMID: 9547005Apr 18, 1998Paper

An ultrastructural study of the colocalization of biglycan and decorin with AA amyloid fibrils in human renal glomeruli

Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis
J MossD Woodrow

Abstract

An investigation was undertaken on paraformaldehyde-fixed, Lowicryl resin-embedded renal biopsies from patients with AA amyloidosis to study the association of two small chondroitin sulphate/dermatan sulphate proteoglycans, decorin and biglycan, with amyloid fibrils using an ultrastructural immunogold technique. Biglycan was present in glomerular endothelial cells in both normal kidney and in amyloidosis, but little biglycan or decorin was present in the normal mesangial matrix. By contrast, conspicuous amounts of both biglycan and decorin were seen to be associated with amyloid fibrils in the glomerular matrix in cases of renal AA amyloidosis. The results further emphasise the close association between amyloid and extracellular matrix components which are now considered to be an integral part of the amyloid fibrils.

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Citations

Dec 1, 2004·Kidney International·Rashad Barsoum
Sep 1, 2013·Journal of Advanced Research·Rashad S BarsoumTamer El-Baz
Oct 26, 2018·Journal of Cell Communication and Signaling·Wei ZouYi Gong
Nov 13, 2004·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Mónica Mendes SousaMaria João Saraiva
Dec 9, 2004·Scandinavian Journal of Immunology·T N WienG Husby
Dec 17, 2021·Frontiers in Medicine·Barbara J BallermannBörje Haraldsson

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