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

Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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.
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
Introduction to Actin01:26

Introduction to Actin

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 different species.
Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

You might also read

Related Articles

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

Sort by
Same author

Tracheal aspirates of mechanically ventilated preterm infants possess cytopathic tau variants: a prospective exploratory study.

American journal of physiology. Lung cellular and molecular physiology·2026
Same author

PPM1B utilizes a trinuclear metal architecture for phosphatase activity.

bioRxiv : the preprint server for biology·2026
Same author

Lung endothelial cytopathic tau is sufficient to impair long-term potentiation during infection.

American journal of respiratory cell and molecular biology·2026
Same author

<i>Pseudomonas aeruginosa</i> exoenzyme Y activity inhibits exoenzyme S-induced caspase activation in pulmonary microvascular endothelial cells.

American journal of physiology. Lung cellular and molecular physiology·2026
Same author

MUC16-dependent Renal Vascular Adhesion of Candida Promotes Tissue Invasion and Predicts Clinical Outcome in Candidemia.

Research square·2026
Same author

Tau is necessary for Pseudomonas aeruginosa-induced blood-brain barrier dysfunction.

Communications biology·2026

Related Experiment Video

Updated: Jun 27, 2026

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
08:37

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Published on: November 18, 2011

The actin cytoskeleton in endothelial cell phenotypes.

Nutan Prasain1, Troy Stevens

  • 1Department of Molecular and Cellular Pharmacology, College of Medicine, University of South Alabama, Mobile, AL 36688, USA.

Microvascular Research
|November 26, 2008
PubMed
Summary

Endothelial cells line blood vessels and form a semi-permeable barrier between blood and tissue. Their function depends on internal structures that help maintain cell shape and adhesion. The actin cytoskeleton is one such structure, providing a dynamic scaffold that supports membrane proteins and responds to environmental signals. This review explores three key actin-based structures: spectrin cross-linking, the cortical actin rim, and stress fibers. Each plays a role in cell behavior, and their organization changes in response to signals. The authors synthesize findings to explain how actin structures contribute to different endothelial cell phenotypes. They emphasize the importance of understanding how actin responds to environmental cues for better vascular research.

Keywords:
actin structuresendothelial cell functioncytoskeletal dynamicscell signaling

Frequently Asked Questions

More Related Videos

Micropatterning and Assembly of 3D Microvessels
13:05

Micropatterning and Assembly of 3D Microvessels

Published on: September 9, 2016

Related Experiment Videos

Last Updated: Jun 27, 2026

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
08:37

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Published on: November 18, 2011

Micropatterning and Assembly of 3D Microvessels
13:05

Micropatterning and Assembly of 3D Microvessels

Published on: September 9, 2016

Area of Science:

  • Cell biology
  • Vascular physiology
  • Cytoskeletal dynamics

Background:

Endothelial cells form a semi-permeable layer between blood and tissue. Their function depends on cell-cell and cell-matrix interactions. These connections rely on internal cellular structures for stability. Prior research has shown that the actin cytoskeleton plays a central role in this process. However, the specific mechanisms remain unclear in some contexts. This gap motivated a deeper exploration of actin's role in endothelial behavior. No prior work had resolved how actin structures vary across cell states. Understanding these differences is crucial for advancing vascular research.

Purpose Of The Study:

This review aims to clarify how the actin cytoskeleton influences endothelial cell behavior. It focuses on three distinct actin structures and their roles. The study examines how these structures respond to cellular signals. The motivation stems from the need to understand endothelial cell adaptation. This includes how cells change shape and maintain integrity. The goal is to identify how actin organization affects cell function. The authors aim to synthesize findings from multiple studies. This approach helps explain how actin contributes to different cell phenotypes.

Main Methods:

The authors conducted a literature-based review of endothelial cell actin structures. They analyzed three main components: spectrin cross-linking, cortical actin, and stress fibers. Each structure was examined for its role in cell behavior. The study focused on how these structures respond to signaling pathways. The approach involved comparing findings from various experimental models. The authors synthesized evidence from in vitro and in vivo studies. They evaluated how actin organization changes under different conditions. The method emphasized a structured comparison of actin-related mechanisms.

Main Results:

The review highlights that actin cross-linking with spectrin supports membrane stability. The cortical actin rim contributes to cell shape and adhesion. Stress fibers are involved in contractility and cell movement. These structures respond to extracellular signals in distinct ways. The study found that actin organization varies with cell state. For example, stress fibers increase in response to mechanical stress. The review also notes that signaling pathways regulate actin dynamics. These findings suggest that actin structures are adaptable to cellular needs.

Conclusions:

The authors conclude that the actin cytoskeleton is essential for endothelial cell function. They propose that actin structures are regulated by environmental signals. The review suggests that changes in actin organization affect cell behavior. The findings support the idea that actin structures are dynamic and context-dependent. The authors emphasize the importance of understanding actin signaling. They note that further research is needed to clarify these mechanisms. The review does not claim that actin is the sole factor in cell behavior. It suggests that actin structures work in concert with other cellular components.

The actin cytoskeleton provides a dynamic scaffold that supports cell shape and membrane organization.

Stress fibers are involved in cell contractility and movement, especially under mechanical stress.

The cortical actin rim helps maintain cell shape and adhesion to neighboring cells and the extracellular matrix.

Spectrin cross-linking supports membrane stability and contributes to the integrity of the cell surface.

Actin structures adapt to signals such as mechanical stress and extracellular signaling molecules.

The authors suggest that actin organization is regulated by signaling pathways in response to environmental changes.