Inhibition of the relative movement of actin and myosin by caldesmon and calponin.

Shirinsky, Vladimir P.; Biryukov, K. G.; Hettasch, Joann M.; Sellers, James R.

doi:10.1016/s0021-9258(19)49617-8

Cited by 168 publications

(32 citation statements)

References 41 publications

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“…As for ␣-SMA, the decline starts in the interventricular septum, extends first toward the left ventricular free wall and then to the right ventricular free wall, and only then to the trabeculae. manner (Shirinsky et al, 1992;Haeberle and Hemric, 1994). After ED14, the coexpression of ␣and ␤-MHC disappears and the expression of calponin and ␣-SMA begins to decline (Figs.…”

Section: The Transition Of the Embryonic Into The Definitive Myocardiummentioning

confidence: 95%

“…The temporary expression of the thinfilament protein ␣-smooth-muscle actin (␣-SMA) in the cardiomyocytes of the embryonic heart of rat and chicken (Sugi and Lough, 1992;Ruzicka and Schwartz, 1988;Woodcock-Mitchell et al, 1988;Sawtell and Lessard, 1989), therefore, prompted us to investigate whether the coexpression of ␣and ␤-myosin heavy chain (MHC) that is typical of the earliest phases of cardiomyocyte development is correlated with the expression of smooth-muscle proteins, and, if so, what this combination of phenotypic markers reveals about cardiomyocyte development. In this study, we investigated the spatiotemporal pattern of expression of ␣-SMA and the thin filament-binding proteins calponin and caldesmon (Shirinsky et al, 1992;Haeberle and Hemric, 1994;Gerthoffer and Pohl, 1994), and observed, indeed, a correlation in the expression of ␣-SMA and calponin, the troponin I/T-like molecule of smooth muscle, with the coexpression of both MHCs. Based on the electron microscopic data available in the literature, we argue that ␣-SMA expression is a very useful light microscope marker to follow the transition from the random arrangement of myofibrils in the embryonic heart to the highly ordered organization in the fetal heart; that is to say, to follow the myofibrillar maturation in the prenatal rat heart.…”

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confidence: 93%

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Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

Ya¹,

Markman²,

Wagenaar³

et al. 1997

Anat. Rec.

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The results indicate that alpha-SMA, calponin, and desmin are involved in the myofibrillar development in rat heart. The presence of spatiotemporal differences in the expression of these proteins reveals regional differences in the developmental timing of cardiomyocyte maturation. The maturation process extends from the compact myocardium in the IVS to the left and right ventricular free walls, whereas the atrioventricular junction, the ventricular trabeculae, and developing ventricular conduction system show a relatively slow maturation. Smooth-muscle proteins may contribute to the slow shortening speed that is characteristic of the embryonic myocardium.

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Section: The Transition Of the Embryonic Into The Definitive Myocardiummentioning

confidence: 95%

mentioning

confidence: 93%

Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

Ya¹,

Markman²,

Wagenaar³

et al. 1997

Anat. Rec.

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“…Calponin has been proposed to have a role in the cytoskeleton possibly via cross-linking actin and intermediate filaments (230,605). Calponin inhibits filament sliding in in vitro motility assay (70,248,308,589) and inhibits contraction in smooth muscle preparations (308,510), which shows that it also can influence the contractile system directly. Interestingly, calponin seems to mainly influence the V max (308,510).…”

Section: A Regulation Of Contractile Proteinsmentioning

confidence: 99%

Urinary Bladder Contraction and Relaxation: Physiology and Pathophysiology

Andersson

Arner

2004

Physiological Reviews

814

719

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The detrusor smooth muscle is the main muscle component of the urinary bladder wall. Its ability to contract over a large length interval and to relax determines the bladder function during filling and micturition. These processes are regulated by several external nervous and hormonal control systems, and the detrusor contains multiple receptors and signaling pathways. Functional changes of the detrusor can be found in several clinically important conditions, e.g., lower urinary tract symptoms (LUTS) and bladder outlet obstruction. The aim of this review is to summarize and synthesize basic information and recent advances in the understanding of the properties of the detrusor smooth muscle, its contractile system, cellular signaling, membrane properties, and cellular receptors. Alterations in these systems in pathological conditions of the bladder wall are described, and some areas for future research are suggested.

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“…Calponin is a 32-36-kDa actin-binding protein found first in smooth muscle (Takahashi et al, 1986) and select nonmuscle tissues (reviewed in Chalovich and Pfitzer, 1997). Calponin has properties that indicate it may regulate muscle contraction, including the ability to inhibit actomyosin ATPase activity (Winder and Walsh, 1990), force production in muscle fiber preparations (Itoh et al, 1994), and movement in the in vitro motility assay (Shirinsky et al, 1992;Haeberle, 1994). However, other observations suggest that calponin is a structural protein.…”

Section: Introductionmentioning

confidence: 99%

Calponin Interaction with α-Actinin-Actin: Evidence for a Structural Role for Calponin

Leinweber

Tang

Stafford

et al. 1999

Biophysical Journal

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The purpose of this study was to address the paradox of calponin localization with alpha-actinin and filamin, two proteins with tandem calponin homology (CH) domains, by determining the effect of these proteins on the binding of calponin to actin. The results show that actin can accommodate near-saturating concentrations of either calponin and alpha-actinin or calponin and filamin with little change or no change in ligand affinity. Little direct interaction occurred between alpha-actinin and calponin in the absence of actin, so this effect is not likely to explain the co-distribution of these proteins. Calponin, like alpha-actinin, induced elastic gel formation when added to actin. When alpha-actinin was added to newly formed calponin/actin gels, no change was seen in the mechanical properties of the gel compared to calponin and actin alone. However, when calponin was added to newly formed alpha-actinin/actin gels, the resulting gel was much stronger than the gels formed by either ligand alone. Furthermore, gels formed by the addition of calponin to alpha-actinin/actin exhibited a phenomenon known as strain hardening, a characteristic of mechanically resilient gels. These results add weight to the concept that one of the functions of calponin is to stabilize the actin cytoskeleton.

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Inhibition of the relative movement of actin and myosin by caldesmon and calponin.

Cited by 168 publications

References 41 publications

Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

Urinary Bladder Contraction and Relaxation: Physiology and Pathophysiology

Calponin Interaction with α-Actinin-Actin: Evidence for a Structural Role for Calponin

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