TAILIEUCHUNG - Báo cáo khoa học: Interaction of caspase-3 with the cyclic GMP binding cyclic GMP specific phosphodiesterase (PDE5a1)

Here, we show that recombinant bovine PDE5A1 is pro-teolysedby recombinant caspase-3 inin vitroand transfected Cos-7 cells. In addition, the treatment of PDE5A1-trans-fectedCos-7andPC12cellswithstaurosporine, anapoptotic agent that activates endogenous caspase-3, also induced proteolysis and inactivation of PDE5A1. These findings suggest that there is specificity in the interaction between caspase-3 and PDE5A1 that requires application of an apoptotic stimulus. | Eur. J. Biochem. 270 962-970 2003 FEBS 2003 doi Interaction of caspase-3 with the cyclic GMP binding cyclic GMP specific phosphodiesterase PDE5a1 Mhairi J. Frame1 Rothwelle Tate1 David R. Adams2 Keith M. Morgan3 M. D. Houslay4 Peter Vandenabeele5 and Nigel J. Pyne1 1 Department of Physiology and Pharmacology Strathclyde Institute for Biomedical Sciences University of Strathclyde Glasgow Scotland department of Chemistry Heriot-Watt University Riccarton Edinburgh Scotland 3School of Textiles Heriot-Watt University Scottish Borders Campus Galashiels Scotland 4Molecular Pharmacology Group Division of Biochemistry Molecular Biology Institute of Biological and Life Sciences University of Glasgow Scotland 5Department of Molecular Biology Institute of Biotechnology Flanders Interuniversity University of Ghent Belgium Here we show that recombinant bovine PDE5A1 is pro-teolysed by recombinant caspase-3 in in vitro and transfected Cos-7 cells. In addition the treatment of PDE5A1-trans-fected Cos-7 and PC12 cells with staurosporine an apoptotic agent that activates endogenous caspase-3 also induced proteolysis and inactivation of PDE5A1. These findings suggest that there is specificity in the interaction between caspase-3 and PDE5A1 that requires application of an apoptotic stimulus. The potential proteolysis of the 778 DQGD 781 site in PdE5A1 by caspase-3 might affect cGMP s hydrolyzing activity as this is within the boundary of the active site. We therefore created a truncated D781 mutant corresponding exactly to the potential cleavage product. This mutant was expressed equally well compared with the wild-type enzyme in transfected Cos-7 cells and was inactive. Inactivity of the truncated mutant was not due to potential misfolding of the enzyme as it eluted from gel filtration chromatography in the same fraction as the wild-type enzyme. Homology model comparison with the catalytic domain of PDE4B2 was used to probe a functional role for the .

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