Identification of glycosaminoglycans in human renal and splenic secondary AA amyloid fibril preparations.
The evidence that glycosaminoglycans (GAGs) are specifically associated with amyloid, is strong. In the present study we looked for GAGs in water extracts of amyloid fibrils from kidney and spleen laden with AA amyloid secondary to ankylosing spondylitis. Significant amounts of high molecular weight GAGs were isolated from the fibril preparations of both organs using ion-exchange chromatography and gel filtration procedures. The polysaccharides present in purified human renal and splenic amyloid fibril material were characterized as follows: a) Sulphated GAGs of high molecular weight were found in both renal and splenic amyloid fibril extracts, but not in extracts from corresponding normal tissues. b) All of the renal amyloid-associated high molecular weight GAGs were chondroitin sulphate/dermatan sulphate, whereas splenic amyloid-associated high molecular weight GAGs had a chondroitin sulphate/dermatan sulphate:heparan sulphate ratio of approximately 2:1. c) The findings gave no evidence that GAGs coisolated with AA amyloid fibrils were parts of intact proteoglycan molecules with several GAG chains.
Stenstad
T
T
Department of Rheumatology, University of Tromsø, Norway.
Magnus
J H
JH
Kolset
S O
SO
Husby
G
G
D000328:Adult; D000682:Amyloid / Q000378:metabolism; D006025:Glycosaminoglycans / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007668:Kidney / Q000378:metabolism*; D008297:Male; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D000685:Serum Amyloid A Protein / Q000302:isolation & purification / Q000378:metabolism*; D013154:Spleen / Q000378:metabolism*; D013167:Spondylitis, Ankylosing / Q000378:metabolism
D000682:Amyloid; D006025:Glycosaminoglycans; D011134:Polysaccharides; D000685:Serum Amyloid A Protein