Insulin-dependent casein-induced amyloidosis in experimental animals.
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Amyloid↗
Biomedical subjects
I Kedar
Publications and source records attributed to I Kedar.
Regression of amyloidosis secondary to granulomatous ileitis following surgical resection and colchicine administration.
A patient with nephrotic syndrome was found to have amyloidosis secondary to an otherwise asymptomatic Crohn's disease. Resection of a major portion of the affected bowel and long-term colchicine therapy were followed by a complete clinical remission of the nephrotic syndrome, most probably due to a significant resolution of amyloidosis. The combination of resection of affected bowel segments, together with long-term colchicine therapy may offer a better prognosis than either method alone.
Adult↗
Treatment of experimental murine amyloidosis with dimethyl sulfoxide.
Dimethyl sulfoxide was administered intravenously for 60 days to twenty mice with casein-induced amyloidosis. Partial or total disappearance of amyloid deposits occurred in all treated animals. The urine of these animals contained a substance from which amyloid fibrils could be synthesized. A control group of mice with casein-induced amyloidosis given saline injections showed massive amyloid deposition in the liver and in the spleen at the end of the experiment. Neither the urine of these mice nor the urine of normal control mice treated with dimethyl sulfoxide contained substances from which amyloid fibrils could be synthesized. It is our assumption that dimethyl sulfoxide treatment of mice with amyloidosis resulted in a break up of amyloid fibres into small subunits which were excreted in the urine.
Amyloid↗
In vitro synthesis of "amyloid"fibrils from insulin, calcitonin and parathormone.
Insulin, calcitonin and parathyroid hormone subjected to one of two procedures-acidification and heating or incubation with mouse kidney lysosomal extracts-assumed a nonbranching fibrillar structure, 7 to 10 nm in diameter. The preparations showed green birefringence after Congo red staining. The in vitro synthesis from different hormonal polypeptides of fibrils, fulfilling the criteria for the identification of amyloid, indicates that these criteria are related to conformational rather than to compositional properties, and suggests that these hormones may provide the subunit of the amyloid formed in the corresponding endocrine organs.
Amyloid↗