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Related Concept Videos

Integrins01:10

Integrins

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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,...
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Activation of Integrins01:15

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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...
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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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...
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Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
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Related Experiment Video

Updated: Apr 15, 2026

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor
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Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor

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Cardiac integrins the ties that bind.

D G Simpson1, T A Reaves1, D T Shih1

  • 1Department of Developmental Biology and Anatomy, School of Medicine, University of South Carolina, Columbia, South Carolina USA.

Cardiovascular Pathology : the Official Journal of the Society for Cardiovascular Pathology
|April 9, 2015
PubMed
Summary
This summary is machine-generated.

Cardiac cell shape and myofibrillar organization are regulated by extracellular matrix interactions with integrin receptors. These interactions, along with angiotensin II, influence heart development and function.

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Area of Science:

  • Developmental Biology
  • Cell Biology
  • Cardiovascular Research

Background:

  • Heart development involves complex morphogenetic events.
  • Cardiac myocyte interactions with the extracellular matrix (ECM) are crucial for form and function.

Purpose of the Study:

  • To investigate how cardiac myocyte-environment interactions regulate cardiac form and function.
  • To elucidate the role of integrins and ECM in cardiac development and protein metabolism.

Main Methods:

  • In vitro studies using aligned cardiac myocyte cultures.
  • Experiments assessing the effects of suppressing α1 integrin and overexpressing α2 and α5 integrins.
  • Whole embryo culture system to study angiotensin II effects.

Main Results:

  • Cardiac cell shape is regulated by dynamic interactions between ECM and integrin receptors (e.g., α1β1).
  • ECM contains phenotypic information transduced by integrins into intracellular signals.
  • Suppression of α1 integrin and overexpression of α2/α5 integrins impact cardiac myocyte phenotype and protein metabolism.
  • Angiotensin II influences cardiac looping and myofibril proliferation during development.

Conclusions:

  • Integrin-mediated signaling pathways are critical for cardiac development and function.
  • The ECM acts as a reservoir of information influencing cardiac cell behavior.
  • Biochemical and mechanical signals converge on common intracellular pathways in the heart.