Answer-
According to the given
question-
- cAMP or 3' , 5' -
cyclic adenosine mono phosphate is work as secondary messenger and
helps in regulation of several physiological function .
- It translates the signal from the
extracellular stimulus into specific type of intracellular
response. But the level of cAMP is depend upon its generation and
breakdown or degradation.
- When an extracellular second
messenger such as hormones, drug, neurotransmitter, chemokines
binds with GPCR or G protein coupled receptor then adenyl cyclase
or AC catalyzes the conversion of ATP into cAMP.
- cAMP is broken down or degraded
with the help of phosphodiesterase into 5' - adenosine mono
phosphate or AMP and this leads to termination of cAMP signal.Beta
adrenergic receptor present in ventricular myocytes responsible for
activation of adenyl cyclase which generates by catalyzing ATP to
cAMP .
- now this cAMP activates PKA or
protein kinases which are cAMP dependent. PKA responsible for
phosphorylation of several proteins such as MyBP- C or myosin
binding protein C, toponin I ot TnI.
- Catecholamines also activates Beta
adrenergic receptor as well as cAMP / PKA signaling. So we can say
that the specificity of cAMP signals for hormones is depend upon
specific locations of several effectors of G protein coupled
receptors, adenyl cyalase and cAMP as well as regulators which
selectively activates different types of PKA and leads to
phosphorylation of particular target due to specific types of
stimulus.
- Phosphodiesterase which degrade
cAMP and control their level depend upon the phosphorylation by
PKA.
- e.g. When a Beta adrenergic
receptor agonists such as isoproterenol or PEG1 or prostaglandins
E1 showed different effect when there is same level of cAMP is
present for both the receptor agonists. stimulation of Beta
adrenergic receptor activated protein kinase A which activates
phosphorylase kinase , troponin I as well as glycogen phosphorylase
. while PEG1 increases level of cAMP and activates soluble protein
kinase A but not causes any change in substrate of protein kinase A
related to metabolism of glycogen..