Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium
Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in...
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| Autor*in: |
Kopylova, Galina V. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Springer International Publishing, 1980, 42(2021), 2 vom: 03. Jan., Seite 343-353 |
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| Übergeordnetes Werk: |
volume:42 ; year:2021 ; number:2 ; day:03 ; month:01 ; pages:343-353 |
| Links: |
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| DOI / URN: |
10.1007/s10974-020-09593-4 |
|---|
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OLC2127017382 |
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| 520 | |a Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. | ||
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10.1007/s10974-020-09593-4 doi (DE-627)OLC2127017382 (DE-He213)s10974-020-09593-4-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin aut Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium 2021 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. Cardiac myosin Tropomyosin Tropomyosin phosphorylation In vitro motility assay Calcium regulation Matyushenko, Alexander M. aut Berg, Valentina Y. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Shchepkin, Daniil V. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 42(2021), 2 vom: 03. Jan., Seite 343-353 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:42 year:2021 number:2 day:03 month:01 pages:343-353 https://doi.org/10.1007/s10974-020-09593-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 AR 42 2021 2 03 01 343-353 |
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10.1007/s10974-020-09593-4 doi (DE-627)OLC2127017382 (DE-He213)s10974-020-09593-4-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin aut Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium 2021 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. Cardiac myosin Tropomyosin Tropomyosin phosphorylation In vitro motility assay Calcium regulation Matyushenko, Alexander M. aut Berg, Valentina Y. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Shchepkin, Daniil V. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 42(2021), 2 vom: 03. Jan., Seite 343-353 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:42 year:2021 number:2 day:03 month:01 pages:343-353 https://doi.org/10.1007/s10974-020-09593-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 AR 42 2021 2 03 01 343-353 |
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10.1007/s10974-020-09593-4 doi (DE-627)OLC2127017382 (DE-He213)s10974-020-09593-4-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin aut Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium 2021 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. Cardiac myosin Tropomyosin Tropomyosin phosphorylation In vitro motility assay Calcium regulation Matyushenko, Alexander M. aut Berg, Valentina Y. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Shchepkin, Daniil V. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 42(2021), 2 vom: 03. Jan., Seite 343-353 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:42 year:2021 number:2 day:03 month:01 pages:343-353 https://doi.org/10.1007/s10974-020-09593-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 AR 42 2021 2 03 01 343-353 |
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10.1007/s10974-020-09593-4 doi (DE-627)OLC2127017382 (DE-He213)s10974-020-09593-4-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin aut Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium 2021 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. Cardiac myosin Tropomyosin Tropomyosin phosphorylation In vitro motility assay Calcium regulation Matyushenko, Alexander M. aut Berg, Valentina Y. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Shchepkin, Daniil V. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 42(2021), 2 vom: 03. Jan., Seite 343-353 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:42 year:2021 number:2 day:03 month:01 pages:343-353 https://doi.org/10.1007/s10974-020-09593-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 AR 42 2021 2 03 01 343-353 |
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590 570 VZ 12 ssgn BIODIV DE-30 fid Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium Cardiac myosin Tropomyosin Tropomyosin phosphorylation In vitro motility assay Calcium regulation |
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Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium |
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Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium |
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Kopylova, Galina V. |
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Journal of muscle research and cell motility |
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Kopylova, Galina V. Matyushenko, Alexander M. Berg, Valentina Y. Levitsky, Dmitrii I. Bershitsky, Sergey Y. Shchepkin, Daniil V. |
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acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium |
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Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium |
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Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 |
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Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 |
| abstract_unstemmed |
Abstract Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylation decreases with age and also changes in heart pathologies. Myocardial pathologies, in particular ischemia, are usually accompanied by pH lowering in the cardiomyocyte cytosol. We studied the effects of acidosis on the structural and functional properties of the pseudo-phosphorylated form of Tpm1.1 with the S283D substitution. We found that in acidosis, the interaction of the N- and C-ends of the S283D Tpm molecules decreases, whereas that of WT Tpm does not change. The pH lowering increased thermostability of the complex of F-actin with S283D Tpm to a greater extent than with WT Tpm. Using an in vitro motility assay with NEM- modified myosin as a load, we assessed the effect of the Tpm pseudo-phosphorylation on the force of the actin-myosin interaction. In acidosis, the force generated by myosin in the interaction with thin filaments containing S283D Tpm was higher than with those containing WT Tpm. Also, the pseudo-phosphorylation increased the myosin ability to resist a load. We conclude that ischemia changes the effect of the phosphorylated Tpm on the contractile function of the myocardium. © The Author(s), under exclusive licence to Springer Nature Switzerland AG part of Springer Nature 2021 |
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Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium |
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