Interactions of laminin with the amyloid ß peptide: Implications for Alzheimer's disease
Braz. j. med. biol. res
;
34(5): 597-601, May 2001. ilus
Article
in English
| LILACS
| ID: lil-285873
RESUMO
Extensive neuronal cell loss is observed in Alzheimer's disease. Laminin immunoreactivity colocalizes with senile plaques, the characteristic extracellular histopathological lesions of Alzheimer brain, which consist of the amyloid ß (Aß) peptide polymerized into amyloid fibrils. These lesions have neurotoxic effects and have been proposed to be a main cause of neurodegeneration. In order to understand the pathological significance of the interaction between laminin and amyloid, we investigated the effect of laminin on amyloid structure and toxicity. We found that laminin interacts with the Aß1-40 peptide, blocking fibril formation and even inducing depolymerization of preformed fibrils. Protofilaments known to be intermediate species of Aß fibril formation were also detected as intermediate species of laminin-induced Aß fibril depolymerization. Moreover, laminin-amyloid interactions inhibited the toxic effects on rat primary hippocampal neurons. As a whole, our results indicate a putative anti-amyloidogenic role of laminin which may be of biological and therapeutic interest for controlling amyloidosis, such as those observed in cerebral angiopathy and Alzheimer's disease
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Laminin
/
Amyloid beta-Protein Precursor
/
Extracellular Matrix
/
Alzheimer Disease
Limits:
Animals
/
Humans
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
2001
Type:
Article
/
Congress and conference
/
Project document
Affiliation country:
Chile
Institution/Affiliation country:
Pontificia Universidad Católica de Chile/CL
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