NDLI: THE GREEN TEA POLYPHENOL (−)-EPIGALLOCATECHIN-3-GALLATE INHIBITS MAGNESIUM BINDING TO THE C-DOMAIN OF CARDIAC TROPONIN C

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Impaired contractile responses and altered expression and phosphorylation of Ca2+ sensitization proteins in gastric antrum smooth muscles from ob/ob mice

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THE GREEN TEA POLYPHENOL (−)-EPIGALLOCATECHIN-3-GALLATE INHIBITS MAGNESIUM BINDING TO THE C-DOMAIN OF CARDIAC TROPONIN C

Content Provider	PubMed Central
Author	Fuchs, Franklin Zenon, Grabarek
Abstract	Cardiac muscle contraction is activated via the single Ca2+-binding site (site II) in the N-domain of troponin C (cTnC). The two Ca2+/Mg2+ binding sites in the C-domain of cTnC (sites III and IV) have been considered to play a purely structural role in anchoring cTnC to the thin filament. However, several recent discoveries suggest a possible role of this domain in contractile regulation. The green tea polyphenol (−)-epigallocatechin 3-gallate (EGCg), which binds specifically to the C-domain of cTnC, reduces cardiac myofilament Ca2+ sensitivity along with maximum force and acto-myosin ATPase activity. We have determined the effect of EGCg on Ca2+ and Mg2+ binding to the C-domain of cTnC. In the absence of Mg2+ there was no significant effect of EGCg on the Ca2+-cTnC affinity. Surprisingly, in the presence of Mg2+ EGCg caused an increase in Ca2+ affinity for sites III and IV of cTnC. However, in the absence of Ca2+ the addition of EGCg caused a significant reduction in Mg2+-cTnC affinity. This reduction is presumably responsible for the increase in Ca2+-cTnC affinity produced by EGCg in the presence of Mg2+. We propose that the inhibitory effect of EGCg on myofilament Ca2+ activation may be related to an enhanced Ca2+-Mg2+exchange at sites III and IV of cTnC, which might reduce the myosin crossbridge dependent component of thin filament activation.
Related Links	http://dx.doi.org/10.1007/s10974-013-9338-9
Ending Page	113
Page Count	7
Starting Page	107
File Format	PDF
ISSN	15732657
e-ISSN	15732657
Journal	Journal of muscle research and cell motility
Issue Number	2
Volume Number	34
Language	English
Publisher Date	2013-05-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology Biochemistry

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The green tea polyphenol (−)-epigallocatechin-3-gallate inhibits magnesium binding to the C-domain of cardiac troponin C

Solution Structure of Human Cardiac Troponin C in Complex with the Green Tea Polyphenol, (−)-Epigallocatechin 3-Gallate*

Solution Structure of Human Cardiac Troponin C in Complex with the Green Tea Polyphenol, (−)-Epigallocatechin 3-Gallate

Solution Structure of Human Cardiac Troponin C in Complex with the Green Tea Polyphenol, (−)-Epigallocatechin 3-Gallate

Correction: A Computational Exploration of the Interactions of the Green Tea Polyphenol (–)-Epigallocatechin 3-Gallate with Cardiac Muscle Troponin C

A Computational Exploration of the Interactions of the Green Tea Polyphenol (–)-Epigallocatechin 3-Gallate with Cardiac Muscle Troponin C

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THE GREEN TEA POLYPHENOL (−)-EPIGALLOCATECHIN-3-GALLATE INHIBITS MAGNESIUM BINDING TO THE C-DOMAIN OF CARDIAC TROPONIN C

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