Signals that  decrease Ca2+ sensitivity
• Well-established that cAMP and cGMP decreases Ca2+ sensitivity of
contraction in both intact and permeabilized smooth muscle.
• In vitro, PKA phosphorylates MLCK at two sites; site A decreases
affinity of MLCK for Ca2+/calmodulin complex.
• However, agents that elevate PKA have negligible effects on
phosphorylation of site A and Ca2+ activation of MLCK; suggests that
cAMP/PKA desensitizes smooth muscle by an alternate mechanism.
• Phosphorylation of MLCK by PKG has no effect on activity.
• Endogenous nitric oxide and related nitrovasodilators regulate blood
pressure by activation of soluble guanylate cyclase, elevation of cGMP,
activation of cGMP dependent kinase (cGKIaor PKG). cGMP-mediated
vascular smooth muscle cell relaxation is characterized by a reduction in
intracellular calcium concentration and activation of PP1M, which
reduces the sensitivity of the contractile apparatus to intracellular calcium.
• The mechanism by which cGMP increases PP1M activity and myosin
light chain dephosphorylation was elucidated in a series of experiments
published by Surks et al.