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Apolipoprotein J (clusterin) and Alzheimer's disease
Author(s) -
Calero Miguel,
Rostagno Agueda,
Matsubara Etsuro,
Zlokovic Berislav,
Frangione Blas,
Ghiso Jorge
Publication year - 2000
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/1097-0029(20000815)50:4<305::aid-jemt10>3.0.co;2-l
Subject(s) - clusterin , amyloid (mycology) , microbiology and biotechnology , inflammation , oxidative stress , alzheimer's disease , apolipoprotein e , complement system , protein aggregation , chemistry , biology , neuroscience , disease , immunology , biochemistry , pathology , medicine , apoptosis , antibody
Apolipoprotein J (clusterin) is a ubiquitous multifunctional glycoprotein capable of interacting with a broad spectrum of molecules. In pathological conditions, it is an amyloid associated protein, co‐localizing with fibrillar deposits in systemic and localized amyloid disorders. In Alzheimer's disease, the most frequent form of amyloidosis in humans and the major cause of dementia in the elderly, apoJ is present in amyloid plaques and cerebrovascular deposits but is rarely seen in NFT‐containing neurons. ApoJ expression is up‐regulated in a wide variety of insults and may represent a defense response against local damage to neurons. Four different mechanisms of action could be postulated to explain the role of apoJ as a neuroprotectant during cellular stress: (1) function as an anti‐apoptotic signal, (2) protection against oxidative stress, (3) inhibition of the membrane attack complex of complement proteins locally activated as a result of inflammation, and (4) binding to hydrophobic regions of partially unfolded, stressed proteins, and therefore avoiding aggregation in a chaperone‐like manner. This review focuses on the association of apoJ in biological fluids with Alzheimer's soluble Aβ. This interaction prevents Aβ aggregation and fibrillization and modulates its blood‐brain barrier transport at the cerebrovascular endothelium. Microsc. Res. Tech. 50:305–315, 2000. © 2000 Wiley‐Liss, Inc.