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Biomedical subjects

J H Magnus

Publications and source records attributed to J H Magnus.

41 records · Page 3Linked to original sources
PubMed1991

High molecular weight glycosaminoglycans in AA type amyloid fibril extracts from human liver.

Glycosaminoglycans have previously been identified in extracts of AA type hepatic amyloid fibril from a patient with amyloidosis associated with juvenile rheumatoid arthritis. The macromolecular properties of these polysaccharides are described here in more detail. By gel filtration and ion exchange chromatography glycosaminoglycans in the form of high molecular weight free chains were shown to coisolate with water extracted amyloid fibrils. About 60% of these were characterised as galactosamines (chondroitin sulphate/dermatan sulphate), whereas the remaining 40% consisted of N-sulphated glucosamines (heparin/heparan sulphate). The amyloid associated glycosaminoglycans were not part of intact proteoglycans in the fibril extracts.

Amyloidosis↗
PubMed1991

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.

Adult↗
PubMed1990

[Primary Sjögren's syndrome--more than a dry mouth and dry eyes].

Primary Sjögren's syndrome is an autoimmune disease mainly affecting exocrine glands. The cardinal symptoms are keratoconjunctivitis sicca and xerostomia, the sicca complex, in addition to extraglandular manifestations. The diverse clinical picture and the therapeutic aspect of the syndrome are discussed.

Autoimmune Diseases↗
PubMed1989

Presence of glycosaminoglycans in purified AA type amyloid fibrils associated with juvenile rheumatoid arthritis.

Previous studies have strongly suggested an association between glycosaminoglycans and tissue deposits of amyloid. The present study was aimed at studying this association in purified preparations of hepatic amyloid fibrils obtained from human AA type secondary amyloidosis. Glycosaminoglycans were isolated by gradient ion exchange chromatography of purified amyloid fibrils treated with pronase. Degradation with specific enzymes identified the glycosaminoglycans as chondroitin sulphate, dermatan sulphate, and heparin/heparan sulphate. The total amount of glycosaminoglycans specifically coisolated with the amyloid fibrils was 15 micrograms/mg fibril weight. The presence of glycosaminoglycans in amyloid may play a part in the incorporation of structurally diverse protein precursors into amyloid fibrils of identical ultrastructure.

Amyloidosis↗