Smooth muscle and NMR review: An overview of smooth muscle metabolism

Nakayama, Shinsuke; Clark, Joseph F.

doi:10.1007/978-1-4615-0247-0_3

Cited by 17 publications

(22 citation statements)

References 74 publications

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“…All solutions contained 0.85 mM free Mg 2ϩ and 1.0 mM MgATP (8,40). Mg 2ϩ and MgATP concentrations were chosen based on those measured in the intact taenia cecum (20,33). To keep the MgATP supply sufficient, we chose concentrations of creatine phosphate (20 mM; Ref.…”

Section: Methodsmentioning

confidence: 99%

“…The results indicated a possibility that conformational change of smooth muscle myosin (SMM) by blebbistatin spatially interferes with actin-myosin interaction of smooth muscle cells. In the present study, we thus hypothesized that conformational change of SMM by blebbistatin would induce disruption of the arrangement and structure of contractile filaments and inhibition of the ATPase activity of SMM simultaneously, causing suppression of the smooth muscle contraction without affecting the phosphorylation level of MLC 20 . To test the hypothesis, we studied the effects of blebbistatin on the mechanical properties, phosphorylation level of MLC 20 , and structure of the contractile filaments of skinned (cell membrane permeabilized) taenia cecum from guinea pig, since myosin filament structure in intact and skinned taenia cecum was examined in detail and thought to be stable irrespective of MLC 20 phosphorylation (28,39).…”

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confidence: 99%

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Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig

Watanabe

Yumoto

Tanaka

et al. 2010

American Journal of Physiology-Cell Physiology

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To explore the precise mechanisms of the inhibitory effects of blebbistatin, a potent inhibitor of myosin II, on smooth muscle contraction, we studied the blebbistatin effects on the mechanical properties and the structure of contractile filaments of skinned (cell membrane permeabilized) preparations from guinea pig taenia cecum. Blebbistatin at 10 microM or higher suppressed Ca(2+)-induced tension development at any given Ca(2+) concentration but had little effects on the Ca(2+)-induced myosin light chain phosphorylation. Blebbistatin also suppressed the 10 and 2.75 mM Mg(2+)-induced, "myosin light chain phosphorylation-independent" tension development at more than 10 microM. Furthermore, blebbistatin induced conformational change of smooth muscle myosin (SMM) and disrupted arrangement of SMM and thin filaments, resulting in inhibition of actin-SMM interaction irrespective of activation with Ca(2+). In addition, blebbistatin partially inhibited Mg(2+)-ATPase activity of native actomyosin from guinea pig taenia cecum at around 10 microM. These results suggested that blebbistatin suppressed skinned smooth muscle contraction through disruption of structure of SMM by the agent.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig

Watanabe

Yumoto

Tanaka

et al. 2010

American Journal of Physiology-Cell Physiology

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“…For instance, immediate responses such as an increased requirement for energy to support homeostasis are met from phospho-L-arginine (PLA) stores in marine invertebrates (e.g. Bailey et al, 2003;Morley et al, 2009), or creatine phosphate in vertebrates (Nakayama and Clarke, 2003), and these stores could limit abilities to tolerate rapid environmental change. At the timescales of seconds to weeks or months, changes in gene expression can mediate overall organismal responses, such as those seen in heat shock responses in limpets through a tidal cycle (Clark et al, 2008b), or in seasonal hibernation in ground squirrels (Epperson et al, 2010).…”

Section: Scales Of Change and Scales Of Responsementioning

confidence: 99%

Organisms and responses to environmental change

Peck

2011

Marine Genomics

117

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“…A standard solution for skinned taenia cecum contained 0.85 mM Mg 2+ (2.1 mM Mg(methanesulfonate)2), 1 mM MgATP (1.35 mM total ATP Na2), 20 mM creatine phosphate Na2 (CrP), and 10 mM ethylene glycol-bis(2-aminoethyl) tetraacetic acid (EGTA). The values of Mg 2+ and MgATP concentrations were based on those of intact taenia cecum (Nakayama and Clark, 2003). Ca 2+ solutions contained 10 -4.35 M Ca 2+ (10 mM total Ca(methanesulfonate)2) and 1 µM bovine brain calmodulin (Wako Pure Chemicals, Osaka, Japan).…”

Section: All Experimental Procedures Conformed To the "Guidelines Formentioning

confidence: 99%

Differential effects of an expected actin-tropomyosin binding region of heat shock protein 20 on the relaxation in skinned carotid artery and taenia cecum from guinea pig

Yumoto

Watanabe²,

Konishi³

et al. 2009

J. Smooth Muscle Res.

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To explore the possible role of heat shock protein 20 (HSP20) -linked regulation of actin-myosin interaction in living vascular smooth muscle contraction, we studied the effects of HSP20p and TnIp, synthetic peptides originating from an actin tropomyosin binding region of human heat shock protein 20 [residues 110-121; GFVAREFHRRYR] and that of rabbit cardiac troponin I [residues 136-147; GKFKRPTLRRVR], respectively, on the active stress and phosphorylation level of myosin regulatory light chain (MLC20) during relaxation of skinned (cell membrane permeabilized) preparations from "tonic" carotid artery and "phasic" taenia cecum from guinea pig. Active stress of the skinned preparations, resulting from actin-myosin interaction, biphasically decayed following Ca 2+ removal (relaxation). Decay of MLC20 phosphorylation level by Ca 2+ removal was much faster than active stress in an exponential manner. In skinned carotid artery, HSP20p did neither affect relaxation time course nor MLC20 dephosphorylation, whereas, in skinned taenia cecum, the peptide slowed relaxation time course through inhibition of MLC20 dephosphorylation and slowing "latch"-bridge dissociation. On the other hand, TnIp accelerated relaxation time course without affecting MLC20 dephosphorylation in both skinned carotid artery and skinned taenia cecum. Our present results suggest that, HSP20p slows the relaxation processes through intracellular regulatory mechanisms such as Rho A/Rho-kinase mediated pathways, which are known to be dominant in "phasic" smooth muscles but to be recessive in "tonic" smooth muscles.

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Smooth muscle and NMR review: An overview of smooth muscle metabolism

Cited by 17 publications

References 74 publications

Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig

Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig

Organisms and responses to environmental change

Differential effects of an expected actin-tropomyosin binding region of heat shock protein 20 on the relaxation in skinned carotid artery and taenia cecum from guinea pig

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