Functional analysis of carboxylesterase in human induced pluripotent stem cell-derived enterocytes
Human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug abs...
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Published in | Biochemical and biophysical research communications Vol. 486; no. 1; pp. 143 - 148 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
22.04.2017
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Abstract | Human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug absorption in the human small intestine. However, the expression patterns of CES2A1 and CES1A in Caco-2 cells differ from those in the human small intestine. There are also species-specific differences in CES expression patterns between human and experimental animals. Furthermore, it is difficult to obtain primary human intestinal epithelial cells. Therefore, there is currently no system that can precisely predict features of drug absorption, such as CES-mediated metabolism, in the human intestine. To develop a novel system to evaluate intestinal pharmacokinetics, we analyzed CES expression and function in human induced pluripotent stem (iPS) cell-derived enterocytes. CES2A1 mRNA and protein levels in human iPS cell-derived enterocytes were comparable to Caco-2 cells, whereas CES1A levels were lower in human iPS cell-derived enterocytes compared with Caco-2 cells. p-nitrophenyl acetate hydrolysis in human iPS cell-derived enterocytes was significantly inhibited by the CES2A1-specific inhibitor telmisartan. Hydrolysis levels of the CES2A1-specific substrate aspirin were similar in human iPS cell-derived enterocytes and Caco-2 cells, whereas hydrolysis of the CES1A-specific substrate monoethylglycylxylidine was observed in Caco-2 cells but not in human iPS cell-derived enterocytes. These findings demonstrated that the expression and activity of CES isozymes in human iPS cell-derived enterocytes are more similar to the human small intestine compared with Caco-2 cells.
•CES2A1 is expressed higher than CES1A in human iPS cell-derived enterocytes.•CES2A1 is primary mediator of CES substrates in the enterocytes.•CES expression and activity in the enterocytes is similar to human small intestine. |
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AbstractList | Human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug absorption in the human small intestine. However, the expression patterns of CES2A1 and CES1A in Caco-2 cells differ from those in the human small intestine. There are also species-specific differences in CES expression patterns between human and experimental animals. Furthermore, it is difficult to obtain primary human intestinal epithelial cells. Therefore, there is currently no system that can precisely predict features of drug absorption, such as CES-mediated metabolism, in the human intestine. To develop a novel system to evaluate intestinal pharmacokinetics, we analyzed CES expression and function in human induced pluripotent stem (iPS) cell-derived enterocytes. CES2A1 mRNA and protein levels in human iPS cell-derived enterocytes were comparable to Caco-2 cells, whereas CES1A levels were lower in human iPS cell-derived enterocytes compared with Caco-2 cells. p-nitrophenyl acetate hydrolysis in human iPS cell-derived enterocytes was significantly inhibited by the CES2A1-specific inhibitor telmisartan. Hydrolysis levels of the CES2A1-specific substrate aspirin were similar in human iPS cell-derived enterocytes and Caco-2 cells, whereas hydrolysis of the CES1A-specific substrate monoethylglycylxylidine was observed in Caco-2 cells but not in human iPS cell-derived enterocytes. These findings demonstrated that the expression and activity of CES isozymes in human iPS cell-derived enterocytes are more similar to the human small intestine compared with Caco-2 cells. Human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug absorption in the human small intestine. However, the expression patterns of CES2A1 and CES1A in Caco-2 cells differ from those in the human small intestine. There are also species-specific differences in CES expression patterns between human and experimental animals. Furthermore, it is difficult to obtain primary human intestinal epithelial cells. Therefore, there is currently no system that can precisely predict features of drug absorption, such as CES-mediated metabolism, in the human intestine. To develop a novel system to evaluate intestinal pharmacokinetics, we analyzed CES expression and function in human induced pluripotent stem (iPS) cell-derived enterocytes. CES2A1 mRNA and protein levels in human iPS cell-derived enterocytes were comparable to Caco-2 cells, whereas CES1A levels were lower in human iPS cell-derived enterocytes compared with Caco-2 cells. p-nitrophenyl acetate hydrolysis in human iPS cell-derived enterocytes was significantly inhibited by the CES2A1-specific inhibitor telmisartan. Hydrolysis levels of the CES2A1-specific substrate aspirin were similar in human iPS cell-derived enterocytes and Caco-2 cells, whereas hydrolysis of the CES1A-specific substrate monoethylglycylxylidine was observed in Caco-2 cells but not in human iPS cell-derived enterocytes. These findings demonstrated that the expression and activity of CES isozymes in human iPS cell-derived enterocytes are more similar to the human small intestine compared with Caco-2 cells. •CES2A1 is expressed higher than CES1A in human iPS cell-derived enterocytes.•CES2A1 is primary mediator of CES substrates in the enterocytes.•CES expression and activity in the enterocytes is similar to human small intestine. |
Author | Kabeya, Tomoki Matsumura, Wakana Hosokawa, Masakiyo Iwao, Takahiro Matsunaga, Tamihide |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28285137$$D View this record in MEDLINE/PubMed |
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Keywords | RT Metabolic activity SDS FGF S9 PAGE PNPA Carboxylesterase iPS MEGX Caco-2 cells CES BSA DMEM Enterocytes NEAA FBS Human induced pluripotent stem cells GAPDH HPLC PCR |
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SubjectTerms | Benzimidazoles - pharmacology Benzoates - pharmacology Blotting, Western Caco-2 Cells Caco-2 cells Carboxylesterase Carboxylesterase - antagonists & inhibitors Carboxylesterase - genetics Carboxylesterase - metabolism Cell Differentiation Cell Line Enterocytes Enterocytes - cytology Enterocytes - enzymology Enterocytes - metabolism Gene Expression Human induced pluripotent stem cells Humans Hydrolysis - drug effects Induced Pluripotent Stem Cells - cytology Induced Pluripotent Stem Cells - enzymology Induced Pluripotent Stem Cells - metabolism Intestine, Small - enzymology Intestine, Small - metabolism Isoenzymes - antagonists & inhibitors Isoenzymes - genetics Isoenzymes - metabolism Metabolic activity Nitrophenols - metabolism Reverse Transcriptase Polymerase Chain Reaction Substrate Specificity |
Title | Functional analysis of carboxylesterase in human induced pluripotent stem cell-derived enterocytes |
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