An aminopeptidase from Streptomyces sp. KK565 degrades beta amyloid monomers, oligomers and fibrils

초록

The accumulation of beta amyloid (A beta) has been a primary target for Alzheimer disease therapeutic strategies. Previously, we discovered an activity from Streptomyces sp. KK565 growth media that inhibits A beta aggregation. The active component was an aminopeptidase and named Streptomyces sp. KK565 aminopeptidase (SKAP). SKAP cleaved N-terminal amino-acids of A beta(1-42) monomer, inhibited formation of fibrils and protected A beta(1-42)-induced neurotoxicity. Over-expression of a human homolog of SKAP, glutamate carboxypeptidase II (hGCPII) in A beta-oversynthesizing cells dramatically reduced the A beta levels. These findings suggest a possible role of M28 family peptidases in preventing A beta deposits in mammalian brain. Structured summary: MINT-7992796: SKAP (uniprotkb:Q306T3) physically interacts (MI:0915) with Abeta (uniprotkb:P05067) by protease assay (MI: 0435) MINT-7992752, MINT-7992778: SKAP (uniprotkb: Q306T3) binds (MI: 0407) to Abeta (uniprotkb: P05067) by protease assay (MI: 0435) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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