Amyloidosis : Pathogenesis of Amyloidosis
Amyloidosis results from abnormal folding of proteins which are deposited as fibrils in extracellular tissues and disrupt normal function.The proteins that form amyloid are either normal proteins that have an inherent tendency to fold improperly ,associate and form fibrils and do so when produced in increased amounts or mutant proteins that are prone to misfolding and subsequent aggregation. Normally misfolded proteins are degraded intracellularly in proteosomes or extracellularly by macrophage. In amyloidosis these mechanisms fail. In long standing inflammation there is an elevated level of SAA but elevated level of SAA by itself is not sufficient for deposition o amyloid.There are two explanations for this. May be there is a defect in macrophage enzymes or some genetic alteration of the amyloid molecule itself. In familial polyneuropathy there is no overproduction but the amyloid molecule is mutated and mutated protein are prone to misfolding and aggregation.
-
Category
No comments found