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Main description:
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.
Contents:
Study of Cyclic Adenosine Monophosphate Microdomains in Cells
Marco Mongillo, Anna Terrin, Sandrine Evellin, Valentina Lissandron, and Manuela Zaccolo
High-Resolution Measurements of Cyclic Adenosine Monophosphate Signals in 3D Microdomains
Jeffrey W. Karpen and Thomas C. Rich
Cygnets: In Vivo Characterization of Novel cGMP Indicators and In Vivo Imaging of Intracellular cGMP
Akira Honda, Carolyn L. Sawyer, Sharon M. Cawley, and Wolfgang R. G. Dostmann
High-Throughput Screening of Phosphodiesterase Activity in Living Cells
Thomas C. Rich and Jeffrey W. Karpen
Assessment of Phosphodiesterase Isozyme Contribution in Cell and Tissue Extracts
Therese Keravis, Rima Thaseldar-Roumie, and Claire Lugnier
Localization of the Cyclic Guanosine 39,59-Monophosphate- Hydrolyzing Phosphodiesterase Type 9 in Rat Brain by Nonradioactive In Situ Hybridization
Wilma C. G. van Staveren and Marjanne Markerink-van Ittersum
Determination of Ca2+/Calmodulin-Stimulated Phosphodiesterase Activity in Intact Cells
Chen Yan
Adenovirus-Mediated Overexpression of Murine Cyclic Nucleotide Phosphodiesterase 3B
Faiyaz Ahmad, Linda Harndahl, Yan Tang, Lena Stenson Holst, and Vincent C. Manganiello
Identification of Promoter Elements in the 5'-Flanking Region of Murine Cyclic Nucleotide Phosphodiesterase 3B Gene
Hanguan Liu, Jing Rong Tang, Eva Degerman, and Vincent C. Manganiello
Purification of PDE6 Isozymes From Mammalian Retina
Dana C. Pentia, Suzanne Hosier, Rachel A. Collupy, Beverly A. Valeriani, and Rick H. Cote
Cyclic Guanosine 59-Monophosphate Binding to Regulatory GAF Domains of Photoreceptor Phosphodiesterase
Rick H. Cote
Renaturation of the Catalytic Domain of PDE4A Expressed in Escherichia coli as Inclusion Bodies
Wito Richter, Thomas Hermsdorf, and Dietrich Dettmer
Determining the SubunitStructure of Phosphodiesterases Using Gel Filtration and Sucrose Density Gradient Centrifugation
Wito Richter
Crystallization of Cyclic Nucleotide Phosphodiesterases
Hengming Ke, Qing Huai, and Robert X. Xu
Generation of PDE4 Knockout Mice by Gene Targeting
S.-L. Catherine Jin, Anne M. Latour, and Marco Conti
Immunoprecipitation of PDE2 Phosphorylated and Inactivated by an Associated Protein Kinase
J. Kelley Bentley
Investigation of Extracellular Signal-Regulated Kinase 2 Mitogen-Activated Protein Kinase Phosphorylation and Regulation of Activity of PDE4 Cyclic Adenosine Monophosphate-Specific Phosphodiesterases
Elaine V. Hill, Miles D. Houslay, and George S. Baillie
Radiolabeled Ligand Binding to the Catalytic or Allosteric Sites of PDE5 and PDE11
James L. Weeks II, Mitsi A. Blount, Alfreda Beasley, Roya Zoraghi, Melissa K. Thomas, Konjeti Raja Sekhar, Jackie D. Corbin, and Sharron H. Francis
Analysis of Dimerization Determinants of the PDE6 Catalytic Subunits
Khakim G. Muradov, Kimberly K. Boyd, and Nikolai O. Artemyev
Interaction Between Catalytic and Inhibitory Subunits of PDE6
Nikolai O. Artemyev
Purification, Reconstitution on Lipid Vesicles, and Assays of PDE6 and Its Activator G Protein, Transducin
Theodore G. Wensel, Feng He, and Justine A. Malinski
Index
PRODUCT DETAILS
Publisher: Springer (Humana Press Inc.)
Publication date: November, 2010
Pages: 336
Weight: 579g
Availability: Available
Subcategories: Biochemistry
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