Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains.
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SourceNeuropathology and Applied Neurobiology, 32, 2, (2006), pp. 119-30
Article / Letter to editor
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Neuropathology and Applied Neurobiology
SubjectBio-Molecular Chemistry; DCN 1: Perception and Action; DCN 2: Functional Neurogenomics; DCN 3: Neuroinformatics; NCEBP 11: Alzheimer Centre; NCMLS 3: Growth and differentiation; NCMLS 3: Tissue engineering and pathology; NCMLS 7: Chemical and physical biology; ONCOL 3: Translational research; UMCN 3.2 Cognitive Neurosciences; UMCN 3.2: Cognitive neurosciences; UMCN 5.1: Genetic defects of metabolism
The small heat shock protein family (sHsp) comprises molecular chaperones able to interact with incorrectly folded proteins. Alzheimer's disease (AD) is characterized by pathological lesions such as senile plaques (SPs), cerebral amyloid angiopathy (CAA) and neurofibrillary tangles (NFTs), predominantly consisting of the incorrectly folded proteins amyloid-beta (Abeta) and tau respectively. The aim of this study was to investigate the association of the chaperones Hsp20, HspB2, alphaB-crystallin and Hsp27 with the pathological lesions of AD brains. For this purpose, a panel of well-characterized antibodies directed against these sHsps was used in immunohistochemistry and immunoblotting. We observed extracellular expression of Hsp20, Hsp27 and HspB2 in classic SPs, and Hsp20 expression in diffuse SPs. In addition, extracellular expression of HspB2 was observed in CAA. Both Hsp27 and alphaB-crystallin were also observed in astrocytes associated with both SPs and CAA. Furthermore, none of the sHsps were observed in NFTs in AD brains. We conclude that specific sHsp species may be involved in the pathogenesis of either SPs or CAA in AD.
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