Human brain amyloidoses.

Abstract

Several diseases aVecting the central nervous system near future. (CNS) of humans result from the formation This review summarizes the salient clinical and of a substance, named amyloid. Amyloid currently pathological features of the brain amyloidoses with identifies aggregates of an insoluble protein which special emphasis on the data obtained by our group. (i) generally occupy the extracellular space, (ii) are Some of the mechanisms involved in the pathogenesis birefringent under polarized light, (iii) react with the of AD and prion disease are also briefly discussed. Congo red histological stain, (iv) have a s-pleated sheet secondary structure, (v) are fibrillary with an extensive antiparallel b-sheet strands quaternary structure, and (vi) are associated with other proteins pre- Brain amyloidomas sumed to be chaperones [1]. At least five biochemically distinct amyloids are known to aVect the human CNS Amyloid may deposit in the brain in the form of ( Table 1). The amyloidoses due to the aggregation of relatively large aggregates acting like space-occupying the amyloid b peptide (Ab), which include Alzheimer’s lesions, called amyloidomas [6‐16 ]. Twelve cases have disease (AD), Down’s syndrome (DS) and the been reported to date ( Table 2). The mean age at hereditary cerebral haemorrhage with amyloidosis presentation is 54 years (range 28‐76 years). The (HCHWA)-Dutch type, and the amyloidoses due to common clinical presentation is characterized by cogaggregation of the prion protein (PrP), which include nitive decline, seizures and signs of increased intracra+/ ++ + + ++ ++ +/ ’+ +/ ++ +/+ / ’’ ’ ’ +/ ++ + ++ +/++ + +/ ++ +/’ ++ + +/ ++ /+ ++/++ ++ ++ +/ ’+ + + +/++ +++/’