Sp-8-CPT-Cyclic AMPS (Sp-8-CPT-cAMPS) is a cell permeable cAMP analog that potently and selectively activates protein kinase A [1].
Protein kinase A, also known as cAMP-dependent protein kinase, is one of the most widely researched protein kinase. Protein kinase A phosphorylates proteins containing the motif Arginine-Arginine-X-Serine and activates or deactivates the proteins. Protein kinase A has been involved in regulation of glycogen, sugar, and lipid metabolism [2]. The effects of PKA activation vary with cell type. Protein kinase A has been implicated in muscular system, cardiovascular, and nervous system.
Sp-8-CPT-cAMPS is a structural combination of the lipophilic and non-hydrolyzable cAMP analogs 8-CPT-Cyclic AMP and Sp-Cyclic AMPS. Sp-8-CPT-cAMPS is used to investigate the effects of cAMP-dependent PKA signaling [1]. In guinea-pig trachealis, treatment with 10 μM Sp-8-CPT-cAMPS for 30 min reduced the spasmogenic response with the pEC50 value of 4.74 [3].
References:
[1] Dostmann W R, Taylor S S, Genieser H G, et al. Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3', 5'-cyclic phosphorothioates[J]. Journal of Biological Chemistry, 1990, 265(18): 10484-10491.
[2] Hanks S K, Quinn A M, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains[J]. Science, 1988, 241(4861): 42-52.
[3] Spicuzza L, Belvisi M G, Birrell M A, et al. Evidence that the anti‐spasmogenic effect of the β‐adrenoceptor agonist, isoprenaline, on guinea‐pig trachealis is not mediated by cyclic AMP‐dependent protein kinase[J]. British journal of pharmacology, 2001, 133(8): 1201-1212.