Biomedical Engineering Reference
In-Depth Information
Tabl e 8. 2. Calponin-binding proteins (Source: [ 710 ]). Addition of calponin to actin-tropomyosin
complex provokes formation of actin bundles.
Partner
Function
Actin
Modulation of actin-myosin-2 ATPase activity
α
-Actinin
Stabilization of the
α
-actinin-actin complex
Caldesmon
Myosin-2 binding regulation
Caltropin
Weakening of caldesmon-actin interaction
Calmodulin
Inhibition of actin binding
Myosin-2
Stimulation of myosin-2 ATPase activity
Tropomyosin
Actin stability and myosin-2 regulation
Tubulin
Microtubule binding
HSP90
Prevention of actin bundle formation
Decrease in calponin-induced polymerization of G actin
CamK2
Phosphorylated
ERK1/2
Scaffolding for ERK signaling
PKC
Phosphorylated
Interstitial flow upregulates matrix metalloproteinase expression in rat vascular
smooth myocytes, fibroblasts, and myofibroblasts via the FAK-ERK1/2-Jun path-
way [ 712 ]. At the surface glycocalyx of rat vascular smooth myocytes, heparan
sulfate proteoglycans sense interstitial flow and transduce this mechanical signal.
Subsequent phosphorylated (activated) of mechanosensitive focal adhesion kinase
enable ERK1/2 activation, interstitial collagenase (MMP13) expression, and smooth
myocyte motility.
8.3
Intrinsic Regulators of Smooth Myocyte Tone
8.3.1
Caldesmon and Calmodulin
Caldesmon may act on F actin by either phosphorylation by protein kinase-C and
Ca 2 + or formation of a caldesmon-calcium-calmodulin complex that is unable
to bind to actin. Moreover, caldesmon enhances the binding of ATP-bound heavy
meromyosin (HMM), as well as (but to a lesser extent) the subfragment S1-ATP
(like HMM-ATP in skeletal myocytes), to actin [ 713 ]. This effect is hindered by
Ca 2 + -calmodulin. Caldesmon also interacts with myosin in a process regulated by
casein kinase-2 [ 714 ].
 
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