7 results on '"Ming-Yih Liu"'
Search Results
2. Sulfation of benzyl alcohol by the human cytosolic sulfotransferases (SULTs): a systematic analysis
- Author
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Katsuhisa Kurogi, Lingtian Zhang, Masahito Suiko, Ming-Cheh Liu, Alaina M. Schnapp, Yoichi Sakakibara, Frederick E. Williams, and Ming-Yih Liu
- Subjects
0301 basic medicine ,Kidney ,Human liver ,Chemistry ,organic chemicals ,Toxicology ,Small intestine ,03 medical and health sciences ,Cytosol ,chemistry.chemical_compound ,030104 developmental biology ,Sulfation ,medicine.anatomical_structure ,Biochemistry ,Caco-2 ,Benzyl alcohol ,In vivo ,medicine - Abstract
The aim of the present study was to identify human cytosolic sulfotransferases (SULTs) that are capable of sulfating benzyl alcohol and to examine whether benzyl alcohol sulfation may occur in cultured human cells as well as in human organ homogenates. A systematic analysis revealed that of the 13 known human SULTs, SULT1A1 SULT1A2, SULTA3, and SULT1B1 are capable of mediating the sulfation of benzyl alcohol. The kinetic parameters of SULT1A1 that showed the strongest benzyl alcohol-sulfating activity were determined. HepG2 human hepatoma cells were used to demonstrate the generation and release of sulfated benzyl alcohol under the metabolic settings. Moreover, the cytosol or S9 fractions of human liver, lung, kidney and small intestine were examined to verify the presence of benzyl alcohol sulfating activity in vivo. Copyright © 2015 John Wiley & Sons, Ltd.
- Published
- 2015
3. Sulfation of opioid drugs by human cytosolic sulfotransferases: Metabolic labeling study and enzymatic analysis
- Author
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Ming-Yih Liu, Yoichi Sakakibara, Masahito Suiko, Andriy Chepak, Katsuhisa Kurogi, Ming-Cheh Liu, and Michael T. Hanrahan
- Subjects
Narcotic Antagonists ,Pharmaceutical Science ,Nalorphine ,Pharmacology ,Kidney ,Sulfur Radioisotopes ,Article ,Naltrexone ,Cytosol ,Sulfation ,Intestine, Small ,medicine ,Humans ,Levorphanol ,Lung ,Sulfates ,Chemistry ,Hep G2 Cells ,Nalbuphine ,Analgesics, Opioid ,Liver ,Opioid ,Oxymorphone ,Morphine ,Sulfotransferases ,medicine.drug - Abstract
The current study was designed to examine the sulfation of eight opioid drugs, morphine, hydromorphone, oxymorphone, butorphanol, nalbuphine, levorphanol, nalorphine, and naltrexone, in HepG2 human hepatoma cells and human organ samples (lung, liver, kidney, and small intestine) and to identify the human SULT(s) responsible for their sulfation. Analysis of the spent media of HepG2 cells, metabolically labeled with [35S]sulfate in the presence of each of the eight opioid drugs, showed the generation and release of corresponding [35S]sulfated derivatives. Five of the eight opioid drugs, hydromorphone, oxymorphone, butorphanol, nalorphine, and naltrexone, appeared to be more strongly sulfated in HepG2 cells than were the other three, morphine, nalbuphine, and levorphanol. Differential sulfating activities toward the opioid drugs were detected in cytosol or S9 fractions of human lung, liver, small intestine, and kidney, with the highest activities being found for the liver sample. A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Collectively, the results obtained imply that sulfation may play a significant role in the metabolism of the tested opioid drugs in vivo.
- Published
- 2014
4. Human Cytosolic Sulfotransferase SULT1A3 Mediates the Sulfation of Dextrorphan
- Author
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Ming-Yih Liu, Masahito Suiko, Yoichi Sakakibara, Akihiro Yamamoto, Ming-Cheh Liu, Katsuhisa Kurogi, and Isaac T. Schiefer
- Subjects
0301 basic medicine ,Pharmacology ,Sulfotransferase ,Dextrorphan ,Chemistry ,Pharmaceutical Science ,General Medicine ,Dextromethorphan ,Hep G2 Cells ,Arylsulfotransferase ,03 medical and health sciences ,Cytosol ,030104 developmental biology ,Sulfation ,Biochemistry ,Caco-2 ,Cell culture ,medicine ,Humans ,Caco-2 Cells ,Excitatory Amino Acid Antagonists ,Active metabolite ,medicine.drug - Abstract
Dextrorphan, an active metabolite of the antitussive dextromethorphan, has been shown to be subjected to sulfation by several zebrafish cytosolic sulfotransferases (SULTs). We were interested in finding out which of the human SULT(s) is(are) capable of catalyzing the sulfation of dextrorphan, and to verify whether sulfation of dextrorphan may occur in cultured human cells and human organ cytosols. Data from the enzymatic assays showed that, of all thirteen known human SULTs, SULT1A3 displayed the strongest dextrorphan-sulfating activity. Cell culture experiments using HepG2 human hepatoma cells and Caco-2 human colon carcinoma cells incubated with [(35)S]sulfate together with varying concentrations of dextrorphan revealed indeed the production and release of [(35)S]sulfated dextrorphan in a concentration-dependent manner. Additionally, significant dextrorphan-sulfating activity was detected in human liver, small intestine and lung cytosols. Taken together, these results provided a biochemical basis for the sulfation of dextrorphan in humans.
- Published
- 2016
5. Sulfation of benzyl alcohol by the human cytosolic sulfotransferases (SULTs): a systematic analysis
- Author
-
Lingtian, Zhang, Katsuhisa, Kurogi, Ming-Yih, Liu, Alaina M, Schnapp, Frederick E, Williams, Yoichi, Sakakibara, Masahito, Suiko, and Ming-Cheh, Liu
- Subjects
Sulfates ,organic chemicals ,Hep G2 Cells ,Kidney ,Arylsulfotransferase ,Article ,Cytosol ,Liver ,Intestine, Small ,Humans ,heterocyclic compounds ,Caco-2 Cells ,Lung ,Benzyl Alcohol - Abstract
The aim of the present study was to identify human cytosolic sulfotransferases (SULTs) that are capable of sulfating benzyl alcohol and to examine whether benzyl alcohol sulfation may occur in cultured human cells as well as in human organ homogenates. A systematic analysis revealed that of the 13 known human SULTs, SULT1A1 SULT1A2, SULTA3, and SULT1B1 are capable of mediating the sulfation of benzyl alcohol. The kinetic parameters of SULT1A1 that showed the strongest benzyl alcohol-sulfating activity were determined. HepG2 human hepatoma cells were used to demonstrate the generation and release of sulfated benzyl alcohol under the metabolic settings. Moreover, the cytosol or S9 fractions of human liver, lung, kidney and small intestine were examined to verify the presence of benzyl alcohol sulfating activity in vivo. Copyright © 2015 John WileySons, Ltd.
- Published
- 2015
6. Sulphation of acetaminophen by the human cytosolic sulfotransferases: a systematic analysis
- Author
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Akihiro Yamamoto, Ming-Yih Liu, Katsuhisa Kurogi, Ming-Cheh Liu, Yoichi Sakakibara, Yuichi Saeki, and Masahito Suiko
- Subjects
Sulfotransferase ,Kidney ,Biochemistry ,digestive system ,Sulfation ,Cytosol ,In vivo ,medicine ,Humans ,Molecular Biology ,Lung ,Acetaminophen ,chemistry.chemical_classification ,organic chemicals ,digestive, oral, and skin physiology ,Regular Papers ,General Medicine ,Metabolism ,Hep G2 Cells ,Analgesics, Non-Narcotic ,Hydrogen-Ion Concentration ,Arylsulfotransferase ,digestive system diseases ,Intestines ,stomatognathic diseases ,Kinetics ,Enzyme ,medicine.anatomical_structure ,chemistry ,Liver ,Biocatalysis ,Caco-2 Cells ,Sulfotransferases ,medicine.drug - Abstract
Sulphation is known to be critically involved in the metabolism of acetaminophen in vivo. This study aimed to systematically identify the major human cytosolic sulfotransferase (SULT) enzyme(s) responsible for the sulphation of acetaminophen. A systematic analysis showed that three of the twelve human SULTs, SULT1A1, SULT1A3 and SULT1C4, displayed the strongest sulphating activity towards acetaminophen. The pH dependence of the sulphation of acetaminophen by each of these three SULTs was examined. Kinetic parameters of these three SULTs in catalysing acetaminophen sulphation were determined. Moreover, sulphation of acetaminophen was shown to occur in HepG2 human hepatoma cells and Caco-2 human intestinal epithelial cells under the metabolic setting. Of the four human organ samples tested, liver and intestine cytosols displayed considerably higher acetaminophen-sulphating activity than those of lung and kidney. Collectively, these results provided useful information concerning the biochemical basis underlying the metabolism of acetaminophen in vivo previously reported.
- Published
- 2015
7. Sulfation of opioid drugs by human cytosolic sulfotransferases: Metabolic labeling study and enzymatic analysis.
- Author
-
Katsuhisa Kurogi, Chepak, Andriy, Hanrahan, Michael T., Ming-Yih Liu, Yoichi Sakakibara, Masahito Suiko, and Ming-Cheh Liu
- Subjects
- *
SULFATION , *OPIOIDS , *SULFOTRANSFERASES , *ENZYMATIC analysis , *MORPHINE , *DRUG therapy , *BUTORPHANOL - Abstract
The current study was designed to examine the sulfation of eight opioid drugs, morphine, hydromorphone, oxymorphone, butorphanol, nalbuphine, levorphanol, nalorphine, and naltrexone, in HepG2 human hepatoma cells and human organ samples (lung, liver, kidney, and small intestine) and to identify the human SULT(s) responsible for their sulfation. Analysis of the spent media of HepG2 cells, metabolically labeled with [35S]sulfate in the presence of each of the eight opioid drugs, showed the generation and release of corresponding [35S]sulfated derivatives. Five of the eight opioid drugs, hydromorphone, oxymorphone, butorphanol, nalorphine, and naltrexone, appeared to be more strongly sulfated in HepG2 cells than were the other three, morphine, nalbuphine, and levorphanol. Differential sulfating activities toward the opioid drugs were detected in cytosol or S9 fractions of human lung, liver, small intestine, and kidney, with the highest activities being found for the liver sample. A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Collectively, the results obtained imply that sulfation may play a significant role in the metabolism of the tested opioid drugs in vivo. [ABSTRACT FROM AUTHOR]
- Published
- 2014
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