[11] Use of synergistic pairs of site-selective cAMP analogs in intact cells
References (44)
- et al.
J. Biol. Chem.
(1975) - et al.
J. Biol. Chem.
(1984) - et al.
Mol. Cell. Endocrinol.
(1984) - et al.
J. Biol. Chem.
(1983) - et al.
J. Biol. Chem.
(1980) - et al.
J. Biol. Chem.
(1978) - et al.
J. Biol. Chem.
(1975) - et al.
J. Biol. Chem.
(1975) Biochem. Biophys. Res. Commun.
(1978)- et al.
J. Biol. Chem.
(1980)
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Cheat.
Cited by (67)
Glucagon and insulin cooperatively stimulate fibroblast growth factor 21 gene transcription by increasing the expression of activating transcription factor 4
2017, Journal of Biological ChemistryCitation Excerpt :Increased intracellular cAMP levels, in turn, activate PKA and exchange protein directly activated by cAMP (EPAC), a guanine nucleotide exchange factor that activates the small GTPase Rap1 (24, 25). To assess the role of the cAMP/PKA pathway and the cAMP/EPAC pathway in mediating the stimulatory effect of glucagon plus insulin on FGF21 gene expression, we tested the ability of a membrane-permeable form of cAMP (i.e. dibutyryl cAMP), a PKA-selective agonist (i.e. N6-benzoyladenosine-3′,5′-cyclic monophosphate (6-Bnz-cAMP)) (26), and an EPAC-selective agonist (i.e. 8-(4-chlorophenylthio)-2′-O-methyladenosine-3′,5′-cyclic monophosphate (cpTOME)) (27) to mimic the glucagon induction of FGF21 mRNA abundance in the presence of insulin. In hepatocytes incubated in culture medium containing insulin, addition of dibutyryl cAMP or 6-Bnz-cAMP stimulated a 10- to 11-fold increase in FGF21 mRNA abundance (Fig. 6A).
Structural and evolutionary divergence of cyclic nucleotide binding domains in eukaryotic pathogens: Implications for drug design
2015, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :Synthetic library screening efforts have afforded the possibility for greatly improved targeting of CNB domains with reduced off-target effects [44–47]. Another successful targeting strategy involves combination treatments of cNMP analogs to synergistically and specifically target particular CNB domains [48,49]. Further bioinformatic and structure-based knowledge of pocket-specific features for the different CNB classes will be crucial for the future development of target-specific inhibitors.
Ganoderma atrum polysaccharide evokes antitumor activity via cAMP-PKA mediated apoptotic pathway and down-regulation of Ca<sup>2+</sup>/PKC signal pathway
2014, Food and Chemical ToxicologyCitation Excerpt :To further understand the molecular mechanism of antitumor function, we sought to examine the roles of secondary messengers, Ca2+ based, and cAMP-based signaling pathway in S180 cells apoptosis. Since cAMP and cGMP were the first secondary messengers discovered and are important for regulation of vital cell functions (e.g. proliferation, differentiation, cellular apoptosis and gene transcription) in essentially all organisms (Beebe et al., 1988). We focused our studies on the effect of cAMP and cGMP in S180 cells.
Transcriptional regulation of 5-aminolevulinate synthase by phenobarbital and cAMP-dependent protein kinase
1999, Archives of Biochemistry and BiophysicsThe role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3
1998, Journal of Biological ChemistryType I cAMP-dependent protein kinase delays apoptosis in human neutrophils at a site upstream of caspase-3
1998, Journal of Biological Chemistry