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

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...
Excitation-Contraction Coupling in Skeletal Muscles01:20

Excitation-Contraction Coupling in Skeletal Muscles

Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
When an action potential...
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
Cross-bridge Cycle01:26

Cross-bridge Cycle

As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
Microscopic Anatomy of Skeletal Muscles01:13

Microscopic Anatomy of Skeletal Muscles

Skeletal muscle cells, also called muscle fibers, are distinctly elongated, multi-nucleated, slender biological units. They are packed with specialized structures designed to facilitate their primary function, which is contraction.
The muscle sarcolemma is a plasma membrane enclosing each muscle cell that conducts electrical signals called action potentials. The sarcolemma extends into the cell to form T-tubules, ensuring the neural impulses are uniformly distributed across the entire muscle...
Overview of Skeletal Muscle01:15

Overview of Skeletal Muscle

Skeletal muscles are composed of a bundle of muscle fibers and are attached to bones through tendons. Each skeletal muscle fiber is a single muscle cell. The sarcolemma, the plasma membrane of a skeletal muscle cell, consists of a lipid bilayer and glycocalyx that supports muscle fibers. The sarcolemma extends into the muscle cells to form tubular structures called transverse or T-tubules. Each side of the T-tubules consists of a membrane-bound structure called the sarcoplasmic reticulum,...

You might also read

Related Articles

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

Sort by
Same author

Cellular accumulation of lipofuscin in the heart: implications in health and disease.

Histochemistry and cell biology·2026
Same author

Reviving formalin-fixed, paraffin embedded (FFPE) tissues for on-slide and multiscale correlative microscopy.

Scientific reports·2026
Same author

Biomolecular condensation of cMLCK enables myosin motor phosphorylation in the heart.

bioRxiv : the preprint server for biology·2026
Same author

Hearts may grow concentrically to balance ATP supply and demand and eccentrically to stabilize titin-based stress.

bioRxiv : the preprint server for biology·2026
Same author

A finite element computational framework coupling four-chamber heart mechanics with the systemic and pulmonary circulations.

Research square·2026
Same author

Spatial control of myosin regulatory light chain phosphorylation modulates cardiac thick filament mechanosensing.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Conformational changes upon pore blocker removal reveal conductive states of TMEM16A.

The Journal of general physiology·2026
Same journal

On the mechanism of hypomagnesemia with treatment-resistant seizures caused by variants of the Na+,K+-ATPase α1 subunit (ATP1A1).

The Journal of general physiology·2026
Same journal

Label-free real-time imaging of mitochondrial matrix volume changes and permeability transition in living cells.

The Journal of general physiology·2026
Same journal

Differential regulation of β1-dependent voltage shifts and kinetic modulation by an extracellular glutamate in NaV1.6 VSDIV.

The Journal of general physiology·2026
Same journal

Mechanistic insights into DCPIB inhibition of VRAC: Electrostatic control and binding plasticity.

The Journal of general physiology·2026
Same journal

An epilepsy-associated KV3.1 potassium channel variant acts via dominant-positive effect.

The Journal of general physiology·2026
See all related articles

Related Experiment Video

Updated: Jun 10, 2026

Sarcomere Shortening of Pluripotent Stem Cell-Derived Cardiomyocytes using Fluorescent-Tagged Sarcomere Proteins.
08:37

Sarcomere Shortening of Pluripotent Stem Cell-Derived Cardiomyocytes using Fluorescent-Tagged Sarcomere Proteins.

Published on: March 3, 2021

Distorting the sarcomere

Kenneth S Campbell1

  • 1Department of Physiology, University of Kentucky, Lexington, KY 40536, USA. k.s.campbell@uky.edu

The Journal of General Physiology
|July 28, 2010
PubMed
Summary

No abstract available in PubMed .

More Related Videos

Measurement of Maximum Isometric Force Generated by Permeabilized Skeletal Muscle Fibers
11:30

Measurement of Maximum Isometric Force Generated by Permeabilized Skeletal Muscle Fibers

Published on: June 16, 2015

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer
07:55

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer

Published on: May 7, 2020

Related Experiment Videos

Last Updated: Jun 10, 2026

Sarcomere Shortening of Pluripotent Stem Cell-Derived Cardiomyocytes using Fluorescent-Tagged Sarcomere Proteins.
08:37

Sarcomere Shortening of Pluripotent Stem Cell-Derived Cardiomyocytes using Fluorescent-Tagged Sarcomere Proteins.

Published on: March 3, 2021

Measurement of Maximum Isometric Force Generated by Permeabilized Skeletal Muscle Fibers
11:30

Measurement of Maximum Isometric Force Generated by Permeabilized Skeletal Muscle Fibers

Published on: June 16, 2015

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer
07:55

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer

Published on: May 7, 2020