The role of lipids in the activity of adenylate cyclase of rat liver plasma membranes |
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Authors: | A Réthy V Tomasi A Trevisani |
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Affiliation: | 1. Department of Biotechnological and Applied Clinical Sciences, University of L''Aquila, 67100 L''Aquila, Italy;2. Department of Physics, University of Trento, 38123 Trento, Italy;3. European Center for Brain Research/IRCCS Santa Lucia Foundation, 00143 Rome, Italy;4. Department of Medicine, Campus Bio-Medico University of Rome, 00128 Rome, Italy;5. Department of Bioscience and Technology for Agriculture, Food and Environment, Campus Universitario di Coste Sant''Agostino, University of Teramo, Italy;6. Department of Life, Health & Environmental Sciences, University of L''Aquila, 67100 L''Aquila, Italy;7. Department of Veterinary Medicine, University of Teramo, 64100 Teramo, Italy;8. Department of Chemistry, Sapienza University of Rome, Rome, Italy;9. Department of Translational Biomedicine and Neuroscience ‘DiBraiN’, University of Bari “Aldo Moro”, 70121 Bari, Italy;1. Jagiellonian University, Doctoral School of Exact and Natural Sciences, 11 Lojasiewicza Str., 30-348 Krakow, Poland;2. Jagiellonian University, Jagiellonian Centre for Experimental Therapeutics (JCET), 14 Bobrzynskiego Str., 30-348 Krakow, Poland;3. Jagiellonian University, Faculty of Chemistry, 2 Gronostajowa Str., 30-387 Krakow, Poland |
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Abstract: | The effect of mild lipid extraction and phospholipases on isolated rat liver plasma membrane was investigated. Extraction of membrane at 4 ° with a shaked mixture of petrol ether-n-butanol resulted in a dramatic reduction of the concentration of phosphatidylethanolamine (−97%) and phosphatidylserine (−99%), whereas phosphatidylinositol was reduced to about 30% of the initial value. Simultaneously the activity of adenylate cyclase as well as that of Mg2+-ATPase was strongly reduced −83 and −85%, respectively); another membrane enzyme, 5′-nucleotidase was slightly stimulated.The activity of solvent-treated adenylate cyclase was partially restored by addition of total membrane phospholipids or phosphatidylinositol, while phosphatidylserine was ineffective.Both phospholipase A and C reduced adenylate cyclase activity. However the effect of phospholipase C was prevented by serum albumin, while that of phospholipase A was not. This suggests that the effect of the latter enzyme may be related to alterations of phospholipids and (or) of membrane structure. |
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