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

Introduction to Actin01:26

Introduction to Actin

5.2K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
5.2K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.3K
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
5.3K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

13.5K
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...
13.5K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.0K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
3.0K
Actin Treadmilling01:18

Actin Treadmilling

8.1K
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
8.1K

You might also read

Related Articles

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

Sort by
Same author

In Vitro Orientation of Fibroblasts and Myoblasts on Aligned Collagen Film.

Development, growth & differentiation·2023
Same author

Troponin in Cultured Chicken Breast Muscle Cells: (troponin / muscle cell / chicken).

Development, growth & differentiation·2023
Same author

DIRECT ISOLATION OF NATIVE THIN FILAMENTS FROM EMBRYONIC MUSCLE CELLS.

Development, growth & differentiation·2023
Same author

Periodic Stretching of Cultured Myotubes Enhances Myofibril Assembly.

Zoological science·2022
Same author

Chimeric Mice with Deletion of <i>Cfl2</i> that Encodes Muscle-Type Cofilin (MCF or Cofilin-2) Results in Defects of Striated Muscles, Both Skeletal and Cardiac Muscles.

Zoological science·2019
Same author

Factors affecting the incidence and outcome of Trueperella pyogenes mastitis in cows.

The Journal of veterinary medical science·2017

Related Experiment Video

Updated: Jul 27, 2025

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart
10:56

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart

Published on: March 26, 2015

21.4K

PRESENCE OF THREE ACTIN TYPES IN SKELETAL MUSCLE OF CHICK EMBRYOS.

Noriko Shimizu1, Takashi Obinata1

  • 1Department of Biology, Chiba University, Yayoi-cho, Chiba 260 and Laboratory for Contractile Proteins, Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113.

Development, Growth & Differentiation
|June 7, 2023
PubMed
Summary

This study investigated actin types in developing chick skeletal muscle. While all three actin types (alpha, beta, gamma) were initially present, beta and gamma actins were found to disappear from myofibrils during muscle development.

More Related Videos

In Vivo Imaging of Muscle-tendon Morphogenesis in Drosophila Pupae
08:33

In Vivo Imaging of Muscle-tendon Morphogenesis in Drosophila Pupae

Published on: February 6, 2018

11.5K
DNA Transfection of Mammalian Skeletal Muscles using In Vivo Electroporation
15:56

DNA Transfection of Mammalian Skeletal Muscles using In Vivo Electroporation

Published on: October 19, 2009

17.9K

Related Experiment Videos

Last Updated: Jul 27, 2025

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart
10:56

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart

Published on: March 26, 2015

21.4K
In Vivo Imaging of Muscle-tendon Morphogenesis in Drosophila Pupae
08:33

In Vivo Imaging of Muscle-tendon Morphogenesis in Drosophila Pupae

Published on: February 6, 2018

11.5K
DNA Transfection of Mammalian Skeletal Muscles using In Vivo Electroporation
15:56

DNA Transfection of Mammalian Skeletal Muscles using In Vivo Electroporation

Published on: October 19, 2009

17.9K

Area of Science:

  • Muscle development
  • Cellular biology
  • Biochemistry

Background:

  • Actin is a crucial protein in muscle structure and function.
  • Different actin isoforms are expressed in various cell types and developmental stages.
  • Understanding actin dynamics is key to comprehending muscle differentiation.

Purpose of the Study:

  • To identify and quantify actin isoforms during chick skeletal muscle development.
  • To investigate the assembly and fate of different actin types within myofibrils.
  • To elucidate the differential distribution of actin isoforms in soluble and myofibril fractions.

Main Methods:

  • Electrophoretic separation of actin isoforms.
  • Quantitative analysis of actin bands using Coomassie Brilliant Blue R-250 staining and spectrophotometry.
  • Fractionation of soluble and myofibril components.

Main Results:

  • Alpha (α), beta (β), and gamma (γ) actins were detected in embryonic skeletal muscle.
  • β- and γ-actins were observed to decrease in myofibrils as muscle development progressed.
  • Actin isoform proportions differed between soluble (β>γ>α) and myofibril (α>β>γ) fractions.

Conclusions:

  • Chick skeletal muscle development involves dynamic changes in actin isoform composition.
  • The differential expression and localization of actin isoforms are critical for myofibril formation and maturation.
  • Specific actin types are preferentially incorporated into myofibrils during muscle differentiation.