Description
Humana Press Phosphodiesterase Methods And Protocols by Claire Lugnier
Adenosine 3,5 -cyclic monophosphate (cAMP) and guanosine 3 ,5 -cyclic monophosphate are ubiquitous nucleotides that have been described as the first and second messengers. In concert with intracellular calcium and IP3, they play a major role in the control of intracellular signaling, which orchestrates normal and pathophysiological responses. Downstream from the cyclic nucleotide synthesis by adenylyl and guanylyl cyclases, the multigenic family of cyclic nucleotide phosphodiesterases (PDEs), by specifically hydrolyzing cyclic nucleotides, controls cAMP and cGMP levels to maintain a basal state. Their critical role in intracellular sign- ing has recently designated them as new therapeutical targets. Several leading pharmaceutical companies are searching and developing new therapeutic agents that would potently and selectively inhibit PDE isozymes, notably PDE4 and PDE5. Nevertheless, the precise mechanism and the contribution of the various PDE isozymes in modulating intracellular signaling remain to be established.The aim of Phosphodiesterase Methods and Protocols is to provide a palette of a variety of conceptual and technical approaches designed to solve qu- tions concerning the role of PDEs, and ultimately of their different variants, in physiological functions as well as their implications in several pathologies.show more Study of Cyclic Adenosine Monophosphate Microdomains in CellsMarco Mongillo, Anna Terrin, Sandrine Evellin, Valentina Lissandron, and Manuela ZaccoloHigh-Resolution Measurements of Cyclic Adenosine Monophosphate Signals in 3D MicrodomainsJeffrey W. Karpen and Thomas C. RichCygnets: In Vivo Characterization of Novel cGMP Indicators and In Vivo Imaging of Intracellular cGMPAkira Honda, Carolyn L. Sawyer, Sharon M. Cawley, and Wolfgang R. G. DostmannHigh-Throughput Screening of Phosphodiesterase Activity in Living CellsThomas C. Rich and Jeffrey W. KarpenAssessment of Phosphodiesterase Isozyme Contribution in Cell and Tissue ExtractsTherese Keravis, Rima Thaseldar-Roumie, and Claire LugnierLocalization of the Cyclic Guanosine 39,59-Monophosphate- Hydrolyzing Phosphodiesterase Type 9 in Rat Brain by Nonradioactive In Situ HybridizationWilma C. G. van Staveren and Marjanne Markerink-van IttersumDetermination of Ca2+/Calmodulin-Stimulated Phosphodiesterase Activity in Intact CellsChen YanAdenovirus-Mediated Overexpression of Murine Cyclic Nucleotide Phosphodiesterase 3BFaiyaz Ahmad, Linda Harndahl, Yan Tang, Lena Stenson Holst, and Vincent C. ManganielloIdentification of Promoter Elements in the 5'-Flanking Region of Murine Cyclic Nucleotide Phosphodiesterase 3B GeneHanguan Liu, Jing Rong Tang, Eva Degerman, and Vincent C. ManganielloPurification of PDE6 Isozymes From Mammalian RetinaDana C. Pentia, Suzanne Hosier, Rachel A. Collupy, Beverly A. Valeriani, and Rick H. CoteCyclic Guanosine 59-Monophosphate Binding to Regulatory GAF Domains of Photoreceptor PhosphodiesteraseRick H. CoteRenaturation of the Catalytic Domain of PDE4A Expressed in Escherichia coli as Inclusion BodiesWito Richter, Thomas Hermsdorf, and Dietrich DettmerDetermining the SubunitStructure of Phosphodiesterases Using Gel Filtration and Sucrose Density Gradient CentrifugationWito RichterCrystallization of Cyclic Nucleotide PhosphodiesterasesHengming Ke, Qing Huai, and Robert X. XuGeneration of PDE4 Knockout Mice by Gene TargetingS.-L. Catherine Jin, Anne M. Latour, and Marco ContiImmunoprecipitation of PDE2 Phosphorylated and Inactivated by an Associated Protein KinaseJ. Kelley BentleyInvestigation of Extracellular Signal-Regulated Kinase 2 Mitogen-Activated Protein Kinase Phosphorylation and Regulation of Activity of PDE4 Cyclic Adenosine Monophosphate-Specific PhosphodiesterasesElaine V. Hill, Miles D. Houslay, and George S. BaillieRadiolabeled Ligand Binding to the Catalytic or Allosteric Sites of PDE5 and PDE11James L. Weeks II, Mitsi A. Blount, Alfreda Beasley, Roya Zoraghi, Melissa K. Thomas, Konjeti Raja Sekhar, Jackie D. Corbin, and Sharron H. FrancisAnalysis of Dimerization Determinants of the PDE6 Catalytic SubunitsKhakim G. Muradov, Kimberly K. Boyd, and Nikolai O. ArtemyevInteraction Between Catalytic and Inhibitory Subunits of PDE6Nikolai O. ArtemyevPurification, Reconstitution on Lipid Vesicles, and Assays of PDE6 and Its Activator G Protein, TransducinTheodore G. Wensel, Feng He, and Justine A. MalinskiIndex