TOP

Research Article

Split Viewer

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
Nov 30, 2023 Vol.46 No.11, pp. 655~725
COVER PICTURE
Kim et al. (pp. 710-724) demonstrated that a pathogen-derived Ralstonia pseudosolanacearum type III effector RipL delays flowering time and enhances susceptibility to bacterial infection in Arabidopsis thaliana. Shown is the RipL-expressing Arabidopsis plant, which displays general dampening of the transcriptional program during pathogen infection, grown in long-day conditions.

Share this article on

  • line

Molecules and Cells

eISSN 0219-1032
qr-code Download