scholarly journals A Review of Signal Transduction in Mechanisms of Smooth Muscle Contraction and Its Relevance for Specialized Physical Therapy

2013 ◽  
Vol 25 (1) ◽  
pp. 129-141 ◽  
Author(s):  
Ju-Hyun Kim ◽  
Lim-Kyu Lee ◽  
Won-Deok Lee ◽  
Jeong-Uk Lee ◽  
Mee-Young Kim ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Physical Therapy ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction

HSP27 in signal transduction and association with contractile proteins in smooth muscle cells

1999 ◽  
Vol 277 (2) ◽  
pp. G445-G454 ◽  
Author(s):  
Adenike I. Ibitayo ◽  
Jeanette Sladick ◽  
Sony Tuteja ◽  
Otto Louis-Jacques ◽  
Hirotaka Yamada ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Protein Kinase ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Contractile Proteins ◽  
Mitogen Activated Protein Kinase ◽  
Signal Transduction Cascade ◽  
Kinase C ◽  
Mitogen Activated Protein

Sustained smooth muscle contraction is mediated by protein kinase C (PKC) through a signal transduction cascade leading to contraction. Heat-shock protein 27 (HSP27) appears to be the link between these two major events, i.e., signal transduction and sustained smooth muscle contraction. We have investigated the involvement of HSP27 in signal transduction and HSP27 association with contractile proteins (e.g., actin, myosin, tropomyosin, and caldesmon) resulting in sustained smooth muscle contraction. We have carried out confocal microscopy to investigate the cellular reorganization and colocalization of proteins and immunoprecipitation of HSP27 with actin, myosin, tropomyosin, and caldesmon as detected by sequential immunoblotting. Our results indicate that 1) translocation of Raf-1 to the membrane when stimulated with ceramide is inhibited by vasoactive intestinal peptide (VIP), a relaxant neuropeptide; 2) PKC-α and mitogen-activated protein kinase translocate and colocalize on the membrane in response to ceramide, and PKC-α translocation is inhibited by VIP; 3) HSP27 colocalizes with actin when contraction occurs; and 4) HSP27 immunoprecipitates with actin and with the contractile proteins myosin, tropomyosin, and caldesmon. We propose a model in which HSP27 is involved in sustained smooth muscle contraction and modulates the interaction of actin, myosin, tropomyosin, and caldesmon.

Signal Transduction Pathways Mediating CCK-8S-Induced Gastric Antral Smooth Muscle Contraction

Digestion ◽  
2006 ◽  
Vol 73 (4) ◽  
pp. 249-258 ◽  
Author(s):  
Xin-Min Si ◽  
Lei Huang ◽  
Shelley Chireyath Paul ◽  
Ping An ◽  
He-Sheng Luo
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Signal Transduction Pathways

Interactions of oxidant stress and vascular reactivity

1991 ◽  
Vol 260 (4) ◽  
pp. L207-L211 ◽  
Author(s):  
G. H. Gurtner ◽  
T. Burke-Wolin
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Guanylate Cyclase ◽  
Physiological Response ◽  
Vascular Reactivity ◽  
Oxidant Stress ◽  
Smooth Muscle Contraction

Oxidants have complex effects on pulmonary vascular reactivity. They can stimulate production of vasoconstrictor arachidonate mediators and can also cause vasodilation through activation of guanylate cyclase. Oxidants can also inactivate vasomotor phenomenon by interfering with mechanisms of signal transduction or smooth muscle contraction. The final physiological response depends on the balance of these complex actions.

Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility

1991 ◽  
Vol 261 (2) ◽  
pp. L1-L14 ◽  
Author(s):  
P. de Lanerolle ◽  
R. J. Paul
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Protein Kinases ◽  
Airway Smooth Muscle ◽  
Smooth Muscles ◽  
Smooth Muscle Contraction ◽  
Energy Transduction ◽  
Signal Integration ◽  
Myosin Phosphorylation

Airway smooth muscles contract due to the activation of a highly sophisticated signal transduction mechanism. Signal transduction in muscle must include 1) a mechanism for converting chemical energy (i.e., ATP) into mechanical work (energy transduction) and 2) a mechanism for integrating the response to multiple stimuli (signal integration). In smooth and striated muscles, ATP hydrolysis due to the cyclic interaction of actin and myosin is the final site for both energy transduction and signal integration. There is growing consensus that this interaction in smooth muscles is regulated by the phosphorylation/dephosphorylation of the 20-kDa light chain of smooth muscle myosin. By phosphorylation/dephosphorylation we mean the enzyme-catalyzed transfer of the terminal phosphate of ATP to a serine or threonine residue on a protein, by a class of enzymes known as protein kinases, with the formation of a covalent phosphoester linkage and the enzyme-catalyzed removal of the phosphate group by phosphoprotein phosphatases. Smooth muscles contain many protein kinases and phosphatases, and the research emphasis on the regulation of smooth muscle contraction has focused on how these enzymes act individually and in concert to regulate the actin-myosin interaction. This review will describe the biochemical and physiological experiments that have been performed to understand the role of myosin phosphorylation/dephosphorylation in regulating smooth muscle contraction. Although data from studies on vascular and other smooth muscles will be summarized, this review will focus on studies performed on airway smooth muscle. More detailed reviews of studies on nonairway smooth muscles can be found in Refs. 47 and 79.

Ectopic expression of caveolin-1 restores physiological contractile response of aged colonic smooth muscle

2007 ◽  
Vol 293 (1) ◽  
pp. G240-G249 ◽  
Author(s):  
Sita Somara ◽  
Robert R. Gilmont ◽  
Jeffrery R. Martens ◽  
Khalil N. Bitar
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Contractile Response ◽  
Colonic Motility ◽  
Smooth Muscle Contraction ◽  
Membrane Microdomains ◽  
Aged Rats ◽  
Wild Type ◽  
Caveolin 1

Reduced colonic motility has been observed in aged rats with a parallel reduction in acetylcholine (ACh)-induced myosin light chain (MLC20) phosphorylation. MLC20 phosphorylation during smooth muscle contraction is maintained by a coordinated signal transduction cascade requiring both PKC-α and RhoA. Caveolae are membrane microdomains that permit rapid and efficient coordination of different signal transduction cascades leading to sustained smooth muscle contraction of the colon. Here, we show that normal physiological contraction can be reinstated in aged colonic smooth muscle cells (CSMCs) upon transfection with wild-type caveolin-1 through the activation of both the RhoA/Rho kinase and PKC pathways. Our data demonstrate that impaired contraction in aging is an outcome of altered membrane translocation of PKC-α and RhoA with a concomitant reduction in the association of these molecules with the caveolae-specific protein caveolin-1, resulting in a parallel decrease in the myosin phosphatase-targeting subunit (MYPT) and CPI-17 phosphorylation. Decreased MYPT and CPI-17 phosphorylation activates MLC phosphatase activity, resulting in MLC20 dephosphorylation, which may be responsible for decreased colonic motility in aged rats. Importantly, transfection of CSMCs from aged rats with wild-type yellow fluorescent protein-caveolin-1 cDNA restored translocation of RhoA and PKC-α and phosphorylation of MYPT, CPI-17, and MLC20, thereby restoring the contractile response to levels comparable with young adult rats. Thus, we propose that caveolin-1 gene transfer may represent a promising therapeutic treatment to correct the age-related decline in colonic smooth muscle motility.

PKC-mediated redistribution of mitogen-activated protein kinase during smooth muscle cell activation

1993 ◽  
Vol 265 (2) ◽  
pp. C406-C411 ◽  
Author(s):  
R. A. Khalil ◽  
K. G. Morgan
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Protein Kinase ◽  
Muscle Contraction ◽  
Map Kinase ◽  
Surface Membrane ◽  
Smooth Muscle Contraction ◽  
Cell Contraction ◽  
Signal Transduction Cascade ◽  
Mitogen Activated Protein

Protein kinase C (PKC) translocates from the cytosol to the surface membrane at the time it mediates agonist-induced contraction of ferret vascular smooth muscle cells (R. A. Khalil and K. G. Morgan. J. Physiol. Lond. 455: 585-599, 1992). However, no direct communication between membrane-associated PKC and the contractile filaments has been identified. Mitogen-activated protein (MAP) kinase is a substrate for PKC and is also capable of phosphorylating the actin-binding protein caldesmon at sites phosphorylated during smooth muscle contraction in vivo (L. P. Adam, C. J. Gapinski, and D. R. Hathaway. FEBS Lett. 302: 223-226, 1992). In the present study, the hypothesis that PKC and MAP kinase are involved in a signal-transduction cascade leading to smooth muscle contraction was tested. Immunofluorescence and digital-imaging microscopy were used to localize the epsilon-PKC isoform and MAP kinase during phenylephrine-induced Ca(2+)-independent activation of ferret aorta cells. We report that maintained phenylephrine-induced translocation of cytosolic PKC to the surface membrane is associated with transient redistribution of cytosolic MAP kinase to the surface membrane before cell contraction. Coincident with cell contraction, MAP kinase undergoes a second redistribution away from the plasmalemma and toward the vicinity of contractile filaments. Redistribution of MAP kinase is not stimulated by Ca2+ but is completely prevented by PKC inhibitors. The transient Ca(2+)-independent but PKC-dependent redistribution of MAP kinase points to MAP kinase as a missing link in the signal-transduction cascade between membrane-bound PKC and smooth muscle activation.

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