Biochemical and pharmacological characterization of cyclic nucleotide phosphodiesterase in airway epithelium |
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Authors: | Eric Rousseau Jacky Gagnon Claire Lugnier |
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Institution: | (1) Department of Physiology and Biophysics, Faculty of Medicine, University of Sherbrooke, J1H 5N4 Sherbrooke, Quebec, Canada;(2) Laboratoire de pharmacologie cellulaire et moléculaire, CNRS URA 600, Université Louis Pasteur, B.P. 24, 67 401 Strasbourg, Illkirch, France |
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Abstract: | According to their respective elution order, specificity for cAMP and cGMP, their sensitivity to calmodulin, and their modulation by cGMP and rolipram, four cyclic nucleotide phosphodiesterases (PDE) were separated from the cytosol: PDE I (calmodulin-sensitive), PDE II (stimulated by cGMP, PDE IV (cGMP specific-PDE and inhibited by rolipram) and PDE V (cGMP specific). PDE IV (Km=1.4 M) was competitively inhibited rolipram (Ki=1.2 M) whereas PDE V (Km=0.83 M) was competitively inhibited by zaprinast in the molar range (Ki=0.12 M). Moreover the microsomal fraction contained three PDE isoforms: PDE II, PDE III (inhibited by cGMP or indolidan) and PDE IV. These results show that cAMP degradation in cytosolic and membrane fractions is modulated by cGMP and selectively inhibited by rolipram and, in addition, by indolidan in membrane fractions. (Mol Cell Biochem140: 171–175, 1994) |
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Keywords: | PDE-inhibitors bovine localization |
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