Title |
Interactions of laminin with the amyloid ß peptide: Implications for Alzheimer's disease
|
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Published in |
Brazilian Journal of Medical and Biological Research, May 2001
|
DOI | 10.1590/s0100-879x2001000500006 |
Pubmed ID | |
Authors |
C. Morgan, N.C. Inestrosa |
Abstract |
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 beta (A(beta)) 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 A(beta)1-40 peptide, blocking fibril formation and even inducing depolymerization of preformed fibrils. Protofilaments known to be intermediate species of A(beta) fibril formation were also detected as intermediate species of laminin-induced A(beta) 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. |
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Geographical breakdown
Country | Count | As % |
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Spain | 1 | 2% |
Unknown | 46 | 94% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 8 | 16% |
Researcher | 6 | 12% |
Student > Postgraduate | 6 | 12% |
Professor | 5 | 10% |
Other | 4 | 8% |
Other | 12 | 24% |
Unknown | 8 | 16% |
Readers by discipline | Count | As % |
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Medicine and Dentistry | 8 | 16% |
Neuroscience | 6 | 12% |
Engineering | 4 | 8% |
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Other | 4 | 8% |
Unknown | 10 | 20% |