Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions

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...

Activation of Integrins

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.

Integrins

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...

Regulation of Angiogenesis and Blood Supply

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...

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...

You might also read

Related Articles

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

Sort by

Same author

Gut Microbiota Shapes the Effects of Saturated and Polyunsaturated Fatty Acids on Skin and Hair Follicle Homeostasis.

The Journal of investigative dermatology·2026

Same author

Product of arachidonic acid oxidation inhibits neutrophil migration by forming the inflammatory substrate for integrin αMβ2.

Journal of immunology (Baltimore, Md. : 1950)·2026

Same author

Sex-specific angiogenic responses in endothelial cells-role of the pluripotency factor OCT4.

Angiogenesis·2025

Same author

Structural Insights into Recognition and Translocation of Oxidized Phospholipid by CD36 Using Mass Spectrometry, Molecular Docking, Dynamics, and Metadynamics Simulations.

Journal of the American Chemical Society·2025

Same author

Kindlin-2 Deletion in Mural Cells Leads to Vascular Instability.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2025

Same author

Kindlin-3 phosphorylation is crucial for thrombosis and hemostasis <i>in vivo</i>.

Research and practice in thrombosis and haemostasis·2025

Search research articles

Related Experiment Video

Updated: May 23, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Integrin signaling in vascular function.

Nikolay L Malinin¹, Elzbieta Pluskota, Tatiana V Byzova

¹Department of Molecular Cardiology, Taussig Cancer Center, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.

Current Opinion in Hematology

|April 11, 2012

Summary

This summary is machine-generated.

Kindlins regulate integrin activation, impacting vascular permeability and angiogenesis. Targeting kindlin-dependent pathways requires paralog specificity to avoid adverse vascular effects.

More Related Videos

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Published on: February 11, 2022

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response

Published on: September 15, 2017

Related Experiment Videos

Last Updated: May 23, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Published on: February 11, 2022

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response

Published on: September 15, 2017

Area of Science:

Cell biology
Vascular biology
Molecular signaling

Background:

Integrins are crucial for cell adhesion and mechanotransduction in the vasculature.
Integrin inside-out signaling, mediated by proteins like kindlins, regulates vascular physiology.
Recent discoveries have significantly advanced the understanding of kindlin function in vascular systems.

Purpose of the Study:

To review recent advancements in the vasculature-specific function and regulation of integrins and associated proteins.
To summarize new findings on the role of kindlins in vascular biology and their mechanistic functions.
To highlight progress in understanding integrin inside-out activation.

Main Methods:

Review of recent literature and studies on integrin and kindlin function.
Analysis of data from tissue-specific knockout models for integrins and related genes.
Discussion of newly identified molecular interactions and binding properties of kindlins.

Main Results:

Kindlin-2 is a key modulator of angiogenesis and vascular permeability in heterozygous knockout models.
New findings reveal an additional lipid-binding site in kindlins and preferential binding to nonphosphorylated β-integrins.
Specific knockout models for integrin-associated proteins like integrin-linked kinase, focal adhesion kinase, and talin-1 have been developed.

Conclusions:

Integrins play specific signaling roles in angiogenesis beyond adhesion and mechanotransduction.
The integrin inside-out pathway is critical for vascular physiology, directly regulating endothelial permeability.
Targeting kindlin-dependent pathways for platelet aggregation inhibition must be paralog-specific to prevent negative impacts on vascular permeability.