Related Experiment Video

Updated: Jun 5, 2026

Analysis of Cardiac Contractile Dysfunction and Ca2+ Transients in Rodent Myocytes
07:32

Analysis of Cardiac Contractile Dysfunction and Ca2+ Transients in Rodent Myocytes

Published on: May 25, 2022

Structure of trans-resveratrol in complex with the cardiac regulatory protein troponin C

Sandra E Pineda-Sanabria1, Ian M Robertson, Brian D Sykes

  • 1Department of Biochemistry, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada.

Biochemistry
|January 14, 2011
PubMed

Insights

Trans-resveratrol, found in wine, may protect the heart by binding to troponin C. This interaction could alter how troponin C and troponin I bind, potentially explaining its cardioprotective effects.

Area of Science:

  • Biochemistry
  • Cardiovascular Science
  • Pharmacology

Background:

  • Cardiovascular diseases pose a global health burden.
  • The
  • French paradox
  • suggests wine consumption, rich in trans-resveratrol, may offer cardioprotection.
  • The precise mechanism of trans-resveratrol's action on heart function remains unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of trans-resveratrol's cardioprotective effects.
  • To determine the binding interaction between trans-resveratrol and cardiac troponin C (cTnC).

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was employed.
  • The study determined the structure of trans-resveratrol free and bound to troponin C.

Main Results:

  • Trans-resveratrol binds to the hydrophobic pocket of the cTnC C-domain.
  • Binding induces a minor conformational change in trans-resveratrol.
  • The binding site overlaps with the troponin I (TnI) binding site on cTnC.

Conclusions:

  • Trans-resveratrol's interaction with cTnC suggests a potential mechanism for its inotropic effect.
  • Modulation of the cTnC-TnI interaction is implicated in trans-resveratrol's cardioprotective action.
  • This finding provides a structural basis for understanding wine's cardiovascular benefits.

More Related Videos

Analysis of Tubular Membrane Networks in Cardiac Myocytes from Atria and Ventricles10:30

Analysis of Tubular Membrane Networks in Cardiac Myocytes from Atria and Ventricles

Published on: October 15, 2014

Related Concept Videos

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Structure of Cardiac Muscles01:13

Structure of Cardiac Muscles

Cardiac muscle, or myocardium, is a specialized type of muscle found exclusively in the heart. Its unique structural and functional characteristics enable the heart to perform its vital role of pumping blood throughout the body continuously and rhythmically. The cardiac muscle cells, or cardiomyocytes, possess an endomysium and perimysium but do not have an epimysium.
Compared to skeletal muscles, cardiac muscle cells are small and mostly have a single nucleus. Additionally, they are usually...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...