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The second messenger theory was first proposed by E. W. Sutherland in 1965. As a second messenger, cAMP is responsible for activation of the protein kinase A (PKA), exchange proteins directly activated by cAMP (Epac) and ion gated channel protein [7].
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7. 11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
cAMP generated as a consequence of AC activation can activate several effectors, the most well studied of which is cAMP-dependent protein kinase (PKA) (Pierce et al. 2002).
Diacylglycerol (DAG) activates the eight conventional and novel isozymes of protein kinase C (PKC) by binding to their C1 domains. The crystal structure of PKCII in a partially activated conformation showed how the C1B domain regulates activity by clamping a helix in the C-terminal AGC extension of the kinase domain.
All PKC enzymes are allosterically activated by phosphatidylserine, which binds to the C1 domain, but its affinity for membrane phospholipids is increased by the binding of DAG to the C1 domain and calcium‐binding to the C2 domain, depending on the class of PKCs.

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Protein kinase C (PKC) form a key family of enzymes involved in signalling pathways that specifically phosphorylates substrates at serine/threonine residues. Phosphorylation by PKC is important in regulating a variety of cellular events such as cell proliferation and the regulation of gene expression.
Protein kinase C (PKC) consists of a family of closely related enzymes highly concentrated in the CNS. These enzymes respond to the second messengers calcium (Ca2+) and diacylglycerol (DAG), to express their activities at membrane locations.
Binding of cAMP to the R subunits unleashes the active C subunits, thus allowing them to phosphorylate a variety of protein substrates, both cytosolic and nuclear [5, 6].

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