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Serpins Inhibit the Toxicity of Amyloid Peptides
Author(s) -
Schubert David
Publication year - 1997
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.1997.tb01425.x
Subject(s) - serpin , serine proteinase inhibitors , serine protease , amyloid (mycology) , toxicity , biochemistry , serine , protease inhibitor (pharmacology) , chemistry , p3 peptide , biology , amyloid precursor protein , protease , enzyme , alzheimer's disease , immunology , medicine , disease , pathology , gene , inorganic chemistry , organic chemistry , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
The amyloid plaque in Alzheimer's disease (AD) contains numerous proteins, some of which may be relevant to the pathogenesis of the disease. The serine protease inhibitor α 1 ‐antichymotrypsin is specifically localized in AD plaques. It is shown here that α 1 ‐antichymotrypsin and several other serine protease inhibitors (serpins) inhibit the toxicity of amyloid peptides on primary cortical nerve cell cultures as well as a clonal cell line. This inhibition of toxicity is not mediated via the serpin enzyme complex receptor, the transferrin receptor, or by interference with the polymerization of amyloid fibrils. Since a variety of synthetic serine protease inhibitors mimic the effects of serpins on amyloid toxicity, it is likely that the antiprotease activities of serpins are responsible for their biological effects.