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Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase

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Summary

We investigated the influence of myosin P-LC phosphorylation catalysed by calcium/calmodulin-dependent myosin light chain kinase (MLCK) on the tension-pCa relation of chemically skinned human atrial fibres. MLCK-induced increased myosin P-LC phosphorylation sensitized human atrial skinned fibres for calcium by 0.11 pCa-units in patients with valvular heart disease, and by 0.05 to 0.07 pCa-units in patients with coronary heart disease. The MLCK effect could be antagonized by a light chain phosphatase. The protein phosphatase ocadaic acid (OA) had no influence on the tension-pCa relation of skinned human atrial fibres and had no potentiating effect together with MLCK. The MLCK preparation used in this study was from bovine ventricle and revealed a KM of 1.8×10−5 M and a Vmax of 822 nmol Pi/min/mg using purified bovine ventricular myosin-LCs as substrate.

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  1. I. Morano

    Present address: II. Physiologisches Institut, Universität Heidelberg, Im Neuenheimer Feld 326, 6900, Heidelberg, F.R.G.

Authors and Affiliations

  1. II. Physiologisches Institut, Universität Heidelberg, Im Neuenheimer Feld 326, 6900, Heidelberg, F.R.G.

    C. Bächle-Stolz & J. C. Rüegg

  2. Innere Medizin III, Heidelberg, F.R.G.

    A. Katus

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  1. I. Morano
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  2. C. Bächle-Stolz
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  3. A. Katus
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  4. J. C. Rüegg
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Morano, I., Bächle-Stolz, C., Katus, A. et al. Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase. Basic Res Cardiol 83, 350–359 (1988). https://doi.org/10.1007/BF02005820

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  • DOI: https://doi.org/10.1007/BF02005820

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