Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
The Electron Transport Chain01:30

The Electron Transport Chain

The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Cellular Injury I: Introduction01:00

Cellular Injury I: Introduction

Cellular injury occurs when a cell cannot maintain homeostasis or adapt to stressors such as hypoxia, toxins, or trauma. Depending on severity and duration, injury may be reversible, allowing recovery, or irreversible, leading to cell death.General Mechanisms of Cell InjuryAlthough causes vary, most cellular injuries arise from a few key mechanisms that disrupt essential functions and often amplify one another. Cell survival depends on the extent and balance of these disturbances.ATP depletion...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
The Sarcomere01:08

The Sarcomere

A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each myosin...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Redox and proteolytic regulation of cardiomyocyte β<sub>1</sub>-adrenergic receptors - a novel paradigm for the regulation of catecholamine responsiveness in the heart.

Frontiers in immunology·2023
Same author

Beta<sub>1</sub>-Adrenergic Receptor Cleavage and Regulation by Elastase.

JACC. Basic to translational science·2023
Same author

Michael R. Rosen, MD (1938-2023).

Heart rhythm·2023
Same author

Lipid-independent activation of a muscle-specific PKCα splicing variant.

American journal of physiology. Heart and circulatory physiology·2022
Same author

G Protein-Coupled Receptors-Receptors With New Tricks Up Their Sleeves.

Journal of cardiovascular pharmacology·2022
Same author

Trypsin cleavage of the β<sub>1</sub>-adrenergic receptor.

American journal of physiology. Heart and circulatory physiology·2022
Same journal

SBK2 Links Cardiac Stress Signaling to Mitochondrial Proteostasis.

Circulation research·2026
Same journal

Myeloid Piezo1 as a Brake on Efferocytosis and Cardiac Repair in the Infarcted Heart.

Circulation research·2026
Same journal

Targeting Late Na<sup>+</sup> Current: Too Late or Better Late Than Never?

Circulation research·2026
Same journal

HFpEF-Any: Human Single-Nuclear Transcriptomics Challenging the Translational Validity of Current HFpEF Models.

Circulation research·2026
Same journal

Myovascular Niche: The Role of Endothelial Cells in Skeletal Muscle Health and Disease.

Circulation research·2026
Same journal

Meet the First Authors.

Circulation research·2026
See all related articles

Related Experiment Video

Updated: May 15, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Oxidative stress and sarcomeric proteins.

Susan F Steinberg1

  • 1Department of Pharmacology, College of Physicians and Surgeons, Columbia University, 630 W. 168 St, New York, NY 10032, USA. sfs1@columbia.edu

Circulation Research
|January 19, 2013
PubMed
Summary
This summary is machine-generated.

Oxidative stress impacts heart function by altering sarcomere proteins. Understanding reactive oxygen species (ROS) modifications is key to treating heart failure and other cardiac disorders.

More Related Videos

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Related Experiment Videos

Last Updated: May 15, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Area of Science:

  • Cardiology
  • Biochemistry
  • Molecular Biology

Background:

  • Oxidative stress is a common factor in cardiac disorders like ischemia/reperfusion, diabetes, and hypertension.
  • Reactive oxygen species (ROS) can be protective at low levels but damaging at high levels, affecting sarcomere structure and cardiac pump function.
  • The specific effects of ROS on cardiac contractility depend on the oxidant source, stress level, and post-translational modifications of sarcomere proteins.

Purpose of the Study:

  • To review the various ways reactive oxygen species (ROS) induce post-translational modifications in myofilament proteins.
  • To explore how these modifications influence cardiac contractility and contribute to heart failure pathogenesis.

Main Methods:

  • Literature review focusing on studies investigating ROS-induced changes in myofilament proteins.
  • Analysis of direct oxidative modifications, ROS-activated enzyme phosphorylation, and ROS-activated protease cleavage of myofilament proteins.

Main Results:

  • ROS can directly oxidize myofilament proteins, alter their phosphorylation state via signaling pathways, or lead to cleavage by proteases.
  • These modifications disrupt sarcomere structure and function, contributing to impaired cardiac contractility.
  • The precise outcome is contingent on the specific ROS, concentration, and targeted proteins.

Conclusions:

  • Redox-dependent post-translational modifications of myofilament proteins are critical regulators of cardiac contractility.
  • Targeting these ROS-induced modifications offers potential therapeutic strategies for heart failure and related cardiac conditions.