ArticleThe Journal of biological chemistry2009
Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.
- Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015Pooled it
- Methods for Intracellular Peptidomic Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Quantitative Peptidomics: General Considerations.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Neurolysin Knockout Mice in a Diet-Induced Obesity Model.International journal of molecular sciences · 2023Article
- Toward Stability Enhancement of NTSPharmaceutics · 2023Article
- Probing the Conformational States of Thimet Oligopeptidase in Solution.International journal of molecular sciences · 2022Article
- Effect of FKBP12-Derived Intracellular Peptides on Rapamycin-Induced FKBP-FRB Interaction and Autophagy.Cells · 2022Article
- New Intracellular Peptide Derived from Hemoglobin Alpha Chain Induces Glucose Uptake and Reduces Blood Glycemia.Pharmaceutics · 2021Article
- Peptidome: Chaos or Inevitability.International journal of molecular sciences · 2021Review
- Optimizing the Profile of [International journal of molecular sciences · 2020Article
- Thimet Oligopeptidase Biochemical and Biological Significances: Past, Present, and Future Directions.Biomolecules · 2020Review
- Key-Protease Inhibition Regimens Promote Tumor Targeting of Neurotensin Radioligands.Pharmaceutics · 2020Article
- The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity.Biomolecules · 2020Article
- Thimet Oligopeptidase (EC 3.4.24.15) Key Functions Suggested by Knockout Mice Phenotype Characterization.Biomolecules · 2019Article
- Effect of Protein Denaturation and Enzyme Inhibitors on Proteasomal-Mediated Production of Peptides in Human Embryonic Kidney Cells.Biomolecules · 2019Article
- Intracellular Peptides in Cell Biology and Pharmacology.Biomolecules · 2019Review
- Redox modulation of thimet oligopeptidase activity by hydrogen peroxide.FEBS open bio · 2017Article
- Nuclear expression of renin-angiotensin system components in NRK-52E renal epithelial cells.Journal of the renin-angiotensin-aldosterone system : JRAAS · 2015Article
- Immunogenicity of necrotic cell death.Cellular and molecular life sciences : CMLS · 2015Review
- A novel intracellular peptide derived from g1/s cyclin d2 induces cell death.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Thimet oligopeptidase (EC 3.4.24.15; EP24.15) is an intracellular enzyme that has been proposed to metabolize peptides within cells, thereby affecting antigen presentation and G protein-coupled receptor signal transduction. However, only a small number of intracellular substrates of EP24.15 have been reported previously. Here we have identified over 100 peptides in human embryonic kidney 293 (HEK293) cells that are derived from intracellular proteins; many but not all of these peptides are substrates or products of EP24.15. First, cellular peptides were extracted from HEK293 cells and incubated in vitro with purified EP24.15. Then the peptides were labeled with isotopic tags and analyzed by mass spectrometry to obtain quantitative data on the extent of cleavage. A related series of experiments tested the effect of overexpression of EP24.15 on the cellular levels of peptides in HEK293 cells. Finally, synthetic peptides that corresponded to 10 of the cellular peptides were incubated with purified EP24.15 in vitro, and the cleavage was monitored by high pressure liquid chromatography and mass spectrometry. Many of the EP24.15 substrates identified by these approaches are 9-11 amino acids in length, supporting the proposal that EP24.15 can function in the degradation of peptides that could be used for antigen presentation. However, EP24.15 also converts some peptides into products that are 8-10 amino acids, thus contributing to the formation of peptides for antigen presentation. In addition, the intracellular peptides described here are potential candidates to regulate protein interactions within cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.