Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis
The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as m...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism - Amsterdam : Elsevier, 1170(1993), 3, Seite 258-264 |
| Übergeordnetes Werk: |
volume:1170 ; year:1993 ; number:3 ; pages:258-264 |
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NLEJ18585950X |
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| 245 | 1 | 0 | |a Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis |
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| 520 | |a The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. | ||
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(DE-627)NLEJ18585950X (DE-599)GBVNLZ18585950X DE-627 ger DE-627 rakwb eng Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsoukatos, D.C. oth Tselepis, A.D. oth Lekka, M.E. oth in Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Amsterdam : Elsevier 1170(1993), 3, Seite 258-264 (DE-627)NLEJ185856497 (DE-600)2209461-1 0005-2760 nnns volume:1170 year:1993 number:3 pages:258-264 http://linkinghub.elsevier.com/retrieve/pii/0005-2760(93)90008-W GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1170 1993 3 258-264 |
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(DE-627)NLEJ18585950X (DE-599)GBVNLZ18585950X DE-627 ger DE-627 rakwb eng Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsoukatos, D.C. oth Tselepis, A.D. oth Lekka, M.E. oth in Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Amsterdam : Elsevier 1170(1993), 3, Seite 258-264 (DE-627)NLEJ185856497 (DE-600)2209461-1 0005-2760 nnns volume:1170 year:1993 number:3 pages:258-264 http://linkinghub.elsevier.com/retrieve/pii/0005-2760(93)90008-W GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1170 1993 3 258-264 |
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(DE-627)NLEJ18585950X (DE-599)GBVNLZ18585950X DE-627 ger DE-627 rakwb eng Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsoukatos, D.C. oth Tselepis, A.D. oth Lekka, M.E. oth in Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Amsterdam : Elsevier 1170(1993), 3, Seite 258-264 (DE-627)NLEJ185856497 (DE-600)2209461-1 0005-2760 nnns volume:1170 year:1993 number:3 pages:258-264 http://linkinghub.elsevier.com/retrieve/pii/0005-2760(93)90008-W GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1170 1993 3 258-264 |
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(DE-627)NLEJ18585950X (DE-599)GBVNLZ18585950X DE-627 ger DE-627 rakwb eng Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsoukatos, D.C. oth Tselepis, A.D. oth Lekka, M.E. oth in Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Amsterdam : Elsevier 1170(1993), 3, Seite 258-264 (DE-627)NLEJ185856497 (DE-600)2209461-1 0005-2760 nnns volume:1170 year:1993 number:3 pages:258-264 http://linkinghub.elsevier.com/retrieve/pii/0005-2760(93)90008-W GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1170 1993 3 258-264 |
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(DE-627)NLEJ18585950X (DE-599)GBVNLZ18585950X DE-627 ger DE-627 rakwb eng Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsoukatos, D.C. oth Tselepis, A.D. oth Lekka, M.E. oth in Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Amsterdam : Elsevier 1170(1993), 3, Seite 258-264 (DE-627)NLEJ185856497 (DE-600)2209461-1 0005-2760 nnns volume:1170 year:1993 number:3 pages:258-264 http://linkinghub.elsevier.com/retrieve/pii/0005-2760(93)90008-W GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1170 1993 3 258-264 |
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Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis |
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Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis |
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studies on the subcellular distribution of 1-o-alkyl-2-acetyl-sn-glycero phosphocholine (paf) and on the enzymic activities involved in its biosynthesis within the ciliate tetrahymena pyriformis |
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Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis |
| abstract |
The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. |
| abstractGer |
The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. |
| abstract_unstemmed |
The ciliated protozoan Tetrahymena pyriformis contains platelet-activating factor (PAF) as a physiological minor lipid. Its subcellular localization was found as follows: 13.7% in the pellicles, 24.9% in mitochondria, 56.5% in microsomes and 7.1% in the cytosol. Succinate dehydrogenase was used as marker enzyme. PAF remains cell-associated unless bovine serum albumin is included in the extracellular medium. In this case 15% of total PAF, portion comparable to that found in the pellicles, is released. Investigation of the principal enzymic activities involved in PAF formation showed that PAF-acetyltransferase (2.3.1.67) is totally absent from the protozoan. This means that the 'remodelling' pathway occurring in pro-inflammatory cells does not contribute in PAF formation in our system. A dithiothreitol (DTT)-insensitive CDPcholine phosphocholinetransfcrase activity involved in PAF biosynthesis is shown for the first time to be responsible for PAF production in T. pyriformis. It uses exogenous alkyl-acetyl-glycerol as substrate and is saturated over substrate concentration 250 μM. It can also use endogenous lipids as substrate. It is distributed mainly in mitochondria and microsomes, much less is found in the pellicles and it is totally absent from the cytosol. Its insensitivity to DTT, its selectivity to alkyl-acetyl-G and its different distribution compared to the enzymic activity involved in PC formation (EC 2.7.8.2) suggest that a different enzyme, specific for PAF formation (EC 2.7.8.16) via the de novo pathway exists in the protozoan. |
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Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis |
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Tsoukatos, D.C. Tselepis, A.D. Lekka, M.E. |
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