chondroitin and Amyloidosis

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.

Topics: Amyloidosis; Arthritis, Juvenile; Child; Chondroitin; Glycosaminoglycans; Heparitin Sulfate; Humans; Male; Serum Amyloid A Protein

Two groups of mice (A/J/Han) were treated with casein for 3 weeks. They then received chondroitin sulfate for 1 week, the one group subcutaneously and the other intraperitoneally. Intraperitoneally, chondroitin sulfate produces a more pronounced amyloidosis than subcutaneously. It also causes a marked amyloidosis of the draining lymph nodes of the abdomen. These alterations probably result from an unspecific amyloidogenic effect of chondroitin sulfate, which becomes stronger as local concentration increases.

Topics: Abdomen; Amyloidosis; Animals; Caseins; Chondroitin; Injections, Intraperitoneal; Injections, Subcutaneous; Lymphatic Diseases; Mice; Mice, Inbred Strains; Time Factors

Topics: Amyloidosis; Bence Jones Protein; Binding Sites; Cellulose; Centrifugation, Density Gradient; Cetylpyridinium; Chondroitin; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis; Glycosaminoglycans; Guanidines; Humans; Hyaluronoglucosaminidase; Liver; Organoids; Protein Binding; Spectrophotometry, Ultraviolet; Spleen; Sulfatases

Topics: Amyloidosis; Animals; Caseins; Chondroitin; Female; Hyaluronic Acid; Iontophoresis; Kidney; Kidney Diseases; Liver; Liver Diseases; Lymph Nodes; Lymphatic Diseases; Mice; Spleen; Splenic Diseases; Sulfates

Topics: Amyloidosis; Animals; Chondroitin; Female; Heparin; Hyalin; Hyaluronoglucosaminidase; Kidney Glomerulus; Liver; Lymph Nodes; Mice; Mitosis; Mononuclear Phagocyte System; RNA; Spleen

Topics: Amyloid; Amyloidosis; Chondroitin; Coloring Agents; Humans; Molecular Weight; Solutions; Spectrophotometry; Staining and Labeling

Topics: Amyloid; Amyloidosis; Animals; Blood Protein Disorders; Caseins; Chondroitin; Fluoresceins; Kidney; Liver; Mice; Organ Size; Protein Binding; Serum Albumin; Spleen; Staining and Labeling

Topics: Amyloidosis; Animals; Chondroitin; Ducks; Glycosaminoglycans; Hexosamines; Liver; Models, Biological; Poultry Diseases; Uronic Acids

Topics: Amyloidosis; Aorta; Chondroitin; Electrophoresis; Glycosaminoglycans; Histocytochemistry; Humans; Hyaluronic Acid; Liver; Microscopy, Electron; Neuraminic Acids; Spleen; Uronic Acids

Topics: Amyloid; Amyloidosis; Chondroitin; Chromatography, Paper; Electrophoresis; Fluorescent Dyes; Heparin; Humans; Hyaluronic Acid; Hydrogen-Ion Concentration; Liver; Microscopy, Fluorescence; Spleen; Staining and Labeling

Topics: Amyloidosis; Chondroitin; Sulfuric Acids