An aminopeptidase from Streptomyces sp. KK565 degrades beta amyloid monomers, oligomers and fibrils |
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Authors: | Chulbae Yoo Sangmee Ahn Jo |
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Institution: | Division of Brain Diseases, Center for Biomedical Sciences, National Institute of Health, Korea Center for Disease Control and Prevention, 194 Tongillo, Eunpyeong-gu, Seoul 122-701, Republic of Korea |
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Abstract: | The accumulation of beta amyloid (Aβ) has been a primary target for Alzheimer disease therapeutic strategies. Previously, we discovered an activity from Streptomyces sp. KK565 growth media that inhibits Aβ aggregation. The active component was an aminopeptidase and named Streptomyces sp. KK565 aminopeptidase (SKAP). SKAP cleaved N-terminal amino-acids of Aβ1-42 monomer, inhibited formation of fibrils and protected Aβ1-42-induced neurotoxicity. Over-expression of a human homolog of SKAP, glutamate carboxypeptidase II (hGCPII) in Aβ-oversynthesizing cells dramatically reduced the Aβ levels. These findings suggest a possible role of M28 family peptidases in preventing Aβ deposits in mammalian brain.Structured summaryMINT-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) |
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Keywords: | Aβ beta amyloid SKAP Streptomyces sp KK565 aminopeptidase GCPII glutamate carboxypeptidase II |
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