Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
Myosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the m...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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South African Heart Association
2017-04-01
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| Series: | SA Heart Journal |
| Subjects: | |
| Online Access: | https://www.journals.ac.za/index.php/SAHJ/article/view/1966 |
| _version_ | 1818932723111165952 |
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| author | Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook |
| author_facet | Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook |
| author_sort | Amsha Ramburan |
| collection | DOAJ |
| description | Myosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the most potent regulators of cardiac contractility. Phosphorylation of its N-terminus upon adrenergic stimulation, causes increased order in myosin heads as well as increased ATPase activity, Fmax and Ca2+-sensitivity of contraction, while its dephosphorylation upon cholinergic stimulation or during low flow ischaemia leads to changes in the sarcomeric thick filament that diminish interaction between myosin heads and actin. This dynamic flux in phosphorylation upon adrenergic stimulation is not only crucial to normal cardiac function and structure, but also vital for protection against ischaemic injury. Genetically-driven deficiency or inadequacy in cMyBPC leads to severe cardiac dysfunction and structural changes, including cardiac hypertrophy and dilation, and particularly attenuates the adaptive increase in left ventricular contractility that follows on β-adrenergic stimulation or pressure overload, resulting in decreased systolic function, and reduced cardiac output. |
| first_indexed | 2024-12-20T04:37:01Z |
| format | Article |
| id | doaj.art-d41b372101a849ac8d99c07d15e6327d |
| institution | Directory Open Access Journal |
| issn | 1996-6741 2071-4602 |
| language | English |
| last_indexed | 2024-12-20T04:37:01Z |
| publishDate | 2017-04-01 |
| publisher | South African Heart Association |
| record_format | Article |
| series | SA Heart Journal |
| spelling | doaj.art-d41b372101a849ac8d99c07d15e6327d2022-12-21T19:53:14ZengSouth African Heart AssociationSA Heart Journal1996-67412071-46022017-04-0171384710.24170/7-1-1966Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractilityAmsha Ramburan0Lundi Korkie1Johanna C. Moolman-Smook2University of StellenboschUniversity of StellenboschUniversity of StellenboschMyosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the most potent regulators of cardiac contractility. Phosphorylation of its N-terminus upon adrenergic stimulation, causes increased order in myosin heads as well as increased ATPase activity, Fmax and Ca2+-sensitivity of contraction, while its dephosphorylation upon cholinergic stimulation or during low flow ischaemia leads to changes in the sarcomeric thick filament that diminish interaction between myosin heads and actin. This dynamic flux in phosphorylation upon adrenergic stimulation is not only crucial to normal cardiac function and structure, but also vital for protection against ischaemic injury. Genetically-driven deficiency or inadequacy in cMyBPC leads to severe cardiac dysfunction and structural changes, including cardiac hypertrophy and dilation, and particularly attenuates the adaptive increase in left ventricular contractility that follows on β-adrenergic stimulation or pressure overload, resulting in decreased systolic function, and reduced cardiac output.https://www.journals.ac.za/index.php/SAHJ/article/view/1966myosin binding protein ccardiac contractility |
| spellingShingle | Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility SA Heart Journal myosin binding protein c cardiac contractility |
| title | Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility |
| title_full | Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility |
| title_fullStr | Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility |
| title_full_unstemmed | Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility |
| title_short | Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility |
| title_sort | cardiac myosin binding protein c adrenergic stimulation and cardiac contractility |
| topic | myosin binding protein c cardiac contractility |
| url | https://www.journals.ac.za/index.php/SAHJ/article/view/1966 |
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