| [ Summary ] |
Many substances are co-deposited in the Beta2-microglobulin (Beta2-m) amyloidosis, and they play an important role for amyloid fibril formation. Proteoglycans are large complex molecules composed of core protein and glycosaminoglycans. Beta2-m amyloid deposits first appear in the cervical intervertebral discs, which are well known to be most susceptible to mechanical stress. A close relationship between changes of microenvironment caused by such stress and amyloid deposition is highly suggested. In Beta2-m amyloidosis, the increase of chondroitin sulfate proteoglycans is a constant finding. It is also confirmed in the visceral organ deposition and early stage deposition. Beta2-m has an affinity for proteoglycans, such as heparin. The affinity is related to interactions between negative charges of sulfate groups of proteoglycans and positive charges of basic amino acids of beta2-m. Further studies about interactions between proteoglycans and beta2-m lead to new therapy for amyloidosis. |