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Glycosaminoglycans in Extracts of Cardiac Amyloid Fibrils from Familial Amyloid Cardiomyopathy of Danish Origin Related to Variant Transthyretin Met 111
Author(s) -
MAGNUS J. H.,
STENSTAD T.,
KOLSET S. O.,
HUSBY G.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb01521.x
Subject(s) - transthyretin , fibril , amyloid (mycology) , glycosaminoglycan , chemistry , biochemistry , amyloidosis , heparan sulfate , chondroitin sulfate , amyloid fibril , biology , pathology , amyloid β , endocrinology , medicine , disease , inorganic chemistry
We have previously demonstrated an association between secondary AA type amyloid fibrils and glycosaminoglycans (GAGs) in human liver. The present study was aimed ill investigating whether a similar association could be demonstrated in isolated cardiac amyloid fibrils from a unique Danish family with amyloid cardiomyopathy related to variant transthyretin (TTR) with a single amino acid substitution of a methionin for leucine at position 111 (TTR Met 111). Using gel nitration and ion exchange chromatography. significant amounts of GAGs were detected in close association with purified myocardial amyloid fibrils, whereas only truce amounts of polysaecharides were present in the corresponding normal preparation. The GAGs were identified as 50% chondroitin sulfate, 33% heparin/heparan sulfate, and 17% hyaluronan. With the methods used the amyloid associated GAGs appeared as high molecular weight free polysaccharidc chains, and not as part of intact proteoglycans (PGs) in the fibril extracts. We conclude that the association between purified amyloid fibrils and GAC is may be a general feature of amyloid deposits. Also, we suggest that the proportion of different GAGs in the amyloid deposits may depend both on the organ or tissues affected and the type of protein making up the fibrils.