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Mol. Cells 2005; 20(1): 83-89

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

HtrA2 Interacts with Aβ Peptide but Does Not Directly Alter Its Production or Degradation

Meng-Lu Liu, Ming-Jie Liu, Jin-Man Kim, Hyeon-Jin Kim, Jeong-Hak Kim, Seong-Tshool Hong

Abstract

HtrA2/Omi is a mammalian mitochondrial serine protease homologous to the E. coli HtrA/DegP gene products. Recently, HtrA2/Omi was found to have a dual role in mammalian cells, acting as an apoptosis-inducing protein and being involved in maintenance of mitochondrial homeostasis. By screening a human brain cDNA library with Ab peptide as bait in a yeast two-hybrid system, we identified HtrA2/Omi as a binding partner of Ab peptide. The interaction between Ab peptide and HtrA2/Omi was confirmed by an immunoblot binding assay. The possible involvement of HtrA2/Omi in Ab peptide metabolism was investigated. In vitro peptide cleavage assays showed that HtrA2/Omi did not directly promote the production of Ab peptide at the b/g-secretase level, or the degradation of Ab peptide. However, overexpression of HtrA2/Omi in K269 cells decreased the production of Ab40 and Ab42 by up to 30%. These results rule out the involvement of HtrA2/Omi in the etiology of Alzheimer’s disease. However, the fact that overexpression of HtrA2/Omi reduces the generation of Ab40 and Ab42 suggests that it may play some positive role in mammalian cells.

Keywords Ab Peptide; Alzheimer’s Disease; Apoptosis; HtrA2/Omi; Mitochondria Homeostasis; Secretase

Article

Research Article

Mol. Cells 2005; 20(1): 83-89

Published online August 31, 2005

Copyright © The Korean Society for Molecular and Cellular Biology.

HtrA2 Interacts with Aβ Peptide but Does Not Directly Alter Its Production or Degradation

Meng-Lu Liu, Ming-Jie Liu, Jin-Man Kim, Hyeon-Jin Kim, Jeong-Hak Kim, Seong-Tshool Hong

Abstract

HtrA2/Omi is a mammalian mitochondrial serine protease homologous to the E. coli HtrA/DegP gene products. Recently, HtrA2/Omi was found to have a dual role in mammalian cells, acting as an apoptosis-inducing protein and being involved in maintenance of mitochondrial homeostasis. By screening a human brain cDNA library with Ab peptide as bait in a yeast two-hybrid system, we identified HtrA2/Omi as a binding partner of Ab peptide. The interaction between Ab peptide and HtrA2/Omi was confirmed by an immunoblot binding assay. The possible involvement of HtrA2/Omi in Ab peptide metabolism was investigated. In vitro peptide cleavage assays showed that HtrA2/Omi did not directly promote the production of Ab peptide at the b/g-secretase level, or the degradation of Ab peptide. However, overexpression of HtrA2/Omi in K269 cells decreased the production of Ab40 and Ab42 by up to 30%. These results rule out the involvement of HtrA2/Omi in the etiology of Alzheimer’s disease. However, the fact that overexpression of HtrA2/Omi reduces the generation of Ab40 and Ab42 suggests that it may play some positive role in mammalian cells.

Keywords: Ab Peptide, Alzheimer’s Disease, Apoptosis, HtrA2/Omi, Mitochondria Homeostasis, Secretase

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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