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Cover Picture: 8‐pCPT‐2′‐O‐Me‐cAMP‐AM: An Improved Epac‐Selective cAMP Analogue (ChemBioChem 13/2008)
Author(s) -
Vliem Marjolein J.,
Ponsioen Bas,
Schwede Frank,
Pannekoek WillemJan,
Riedl Jurgen,
Kooistra Matthijs R. H.,
Jalink Kees,
Genieser HansGottfried,
Bos Johannes L.,
Rehmann Holger
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200890049
Subject(s) - chemistry , receptor , biophysics , membrane , hydrolysis , microbiology and biotechnology , biochemistry , biology
The cover picture shows the chemical structure of an acetoxymethyl ester of 8‐pCPT‐2′‐ O ‐Me‐cAMP (007‐AM). 007‐AM can pass cell membranes efficiently and is hydrolysed inside the cell by esterases to release the biologically active compound 8‐pCPT‐2′‐ O ‐Me‐cAMP (007). Due to its low membrane permeability 007 accumulates inside the cell, where it activates the cAMP receptor protein Epac. The inactive conformation of Epac is shown on the left, with the regulatory region in light blue and the catalytic region in dark blue. Binding of cAMP or 007 to Epac leads to a repositioning of the regulatory region, which allows the substrate protein Rap (yellow) to bind and become activated. Activated Rap causes several biological effects, such as the spreading of cells, shown here for A549‐B14 cells. For more information see the article by J. L. Bos, H. Rehmann et al. on p. 2052 ff. (Images of cells were kindly provided by Dr. Sarah Ross).