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Title: A study of the sulphated acid mucopolysaccharides in twenty cases of human amyloidosis and in eighteen controls
Author: Bitter, T.
Awarding Body: University of London
Current Institution: Imperial College London
Date of Award: 1964
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Amyloidosis is diagnosed and defined by several morphological criteria, most of which can be attributed directly or indirectly to the presence of sulphated acid mucopolysaccharides. However neither uronic acid nor sulphate containing components have been found by several more recent biochemical investigators to be increased. In the spleens of twenty cases with all kinds of generalized amyloidosis and of eighteen normal individuals between the ages of fourteen and ninety-eight years, the acid mucopolysaccharides were extracted quantitatively and separated from neutral aminopolysaccharides. In each case the mixture of sulphated acid mucopolysaccharides was examines by electrophoresis on cellulose acetate and analysed for uronic acid, total hexosamine, glucosamine and galactossmine content and for resistance to testicular hyaluronidase. Existing analytical methods had to be modified because of the small amounts of acid mucopolysaccharides present in the spleens. All but one spleen with amyloid deposits contained increased amounts of sulphated acid mucopolysaccharides. This was almost entirely due to heparan sulphate whose proportion was characteristically increased in all spleens with amyloidosis, even in the organ where the total amount of mucopolysaccharides was normal. Increases in the total amounts of dermatan sulphate and chondroitin sulphates also occured in some of the organs although their relative proportion was always decreased. All but one case showed an electrophoretic slow moving component, which in two cases was isolated and consisted of a low sulphated heparan. In the most acute case of amyloidosis heparan sulphate was the acid mucopolysaccharide present in splenic material insoluble in 8 M urea. In the normal spleens the acid mucopolysaccharides decreased with age without a major change in composition. Whilst it seems unlikely that the protein component of the lesions will be the same in diseases as different as myeloma, macroglobulinaemia, familial lipoproteinaemia and chronic inflammation, it could be shown that in all kinds of generalized human amyloidosis the spleen contains abnormal amounts of heparan sulphate, which might explain most of the morphological characteristics and represent a particular chemical feature of the amyloid lesion.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available