Proteoglycans in haemodialysis-related amyloidosis
| Autor: | M. Yanagishita, Mitsuru Hara, S. Tachibana, Yosuke Ogura, Ryuko Kawai, Kenichi Ohashi |
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| Rok vydání: | 1995 |
| Předmět: |
Adult
Male Pathology medicine.medical_specialty Amyloid Pathology and Forensic Medicine Glycosaminoglycan chemistry.chemical_compound Renal Dialysis medicine Humans Chondroitin sulfate Molecular Biology Aged Aged 80 and over biology Amyloidosis Cell Biology General Medicine Heparan sulfate Middle Aged medicine.disease Immunohistochemistry Extracellular Matrix carbohydrates (lipids) Intervertebral disk medicine.anatomical_structure chemistry Proteoglycan Connective Tissue biology.protein Female Proteoglycans Synovial membrane |
| Zdroj: | Virchows Archiv. 427 |
| ISSN: | 1432-2307 0945-6317 |
| DOI: | 10.1007/bf00203737 |
| Popis: | Changes in extracellular matrices of articular tissue, intervertebral discs and systemic organs in patients with haemodialysis-related amyloidosis were investigated by immunohistochemical and biochemical examination of proteoglycans. Increased staining for chondroitin sulfate (CS) was detected in the amyloid deposits of all patients, ranging from early to advanced stages. Degenerative tissue changes around early-stage amyloid deposits in the intervertebral discs also showed positive staining for CS. Heparan sulfate (HS) was detected in amyloid deposits, especially in the synovial membrane. Biochemical analysis of connective tissues containing amyloid supported the immunohistochemical studies; CS was the major glycosaminoglycan species in these tissues, accounting for 55-81% of the total glycosaminoglycans. Although previous studies have stressed the importance of HS in amyloidogenesis, the present study showed that CS, which increased significantly in articular tissues associated with mechanical stress, also has a close relationship with amyloidogenesis. |
| Databáze: | OpenAIRE |
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