Mammalian carboxylesterase (CES) releases GPI-anchored proteins from the cell surface upon lipid raft fluidization
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Kaoru Orihashi
Abstract
Mammalian carboxylesterase (CES) is well known as a biotransformation enzyme for prodrugs and xenobiotics. Here, we purified CES as a GPI-anchored protein (GPI-AP)-releasing factor (GPIase) that releases such protein from the cell surface. All five isoforms of CES showed this activity to various degrees. When the serine residue of the catalytic triad for esterase was replaced by alanine, esterase activity was completely disrupted, while full GPIase activity remained, suggesting that these two activities are exhibited via different mechanisms. CES6, a new class of mammalian CES, exhibited the highest GPIase activity and released specific GPI-APs from the cell surface after lipid raft fluidization. The released product contained a GPI component, indicating that GPI-AP was released by cleavage in GPI. These results revealed for the first time that CES recognizes and catalyzes macromolecule GPI-AP as well as small molecules.
©2012 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- Genes and Nucleic Acids
- The effect of cancer procoagulant on expression of metastatic and angiogenic markers in breast cancer and embryonic stem cell lines
- Characterization of RNA damage under oxidative stress in Escherichia coli
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- Uncommon membrane distribution of Shiga toxin glycosphingolipid receptors in toxin-sensitive human glomerular microvascular endothelial cells
- Cell Biology and Signaling
- Nucleocytoplasmic shuttling of human inositol phosphate multikinase is influenced by CK2 phosphorylation
- Apolipoprotein A5 internalized by human adipocytes modulates cellular triglyceride content
- Mammalian carboxylesterase (CES) releases GPI-anchored proteins from the cell surface upon lipid raft fluidization
- Proteolysis
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- A fluorescence correlation spectroscopy-based enzyme assay for human Dicer
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