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Related Concept Videos

Integrins01:10

Integrins

5.5K
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

Activation of Integrins

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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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Adhesion01:14

Adhesion

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Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
Capillary action is a result of water’s adhesive tendencies. When a narrow...
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Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)01:20

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

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Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others.
The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...
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Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

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Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the involved orbitals. The...
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What is Behavior?00:54

What is Behavior?

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Behaviors are actions that an organism engages in—they can be related to finding food, reproducing, defending against threats, and many other possible actions. Behaviors include activities related to the environment around the animal—such as migration—as well as social interactions within a species or population. Many behaviors involve motor output—that is, muscle movements—while others involve less visible actions, such as learning.
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Related Experiment Video

Updated: Feb 6, 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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Coupling integrin dynamics to cellular adhesion behaviors.

Catherine G Galbraith1, Michael W Davidson2, James A Galbraith1

  • 1Oregon Center for Spatial Systems Biomedicine, Department of Biomedical Engineering, Oregon Health Science University, Portland, OR 97201, USA galbrcat@ohsu.edu galbrjam@ohsu.edu.

Biology Open
|August 17, 2018
PubMed
Summary
This summary is machine-generated.

Labeling integrins (cell adhesion molecules) with fluorescent proteins can alter their behavior and conformation. This study reveals how beta-subunit labeling impacts cell spreading and protrusion, affecting cellular function.

Keywords:
Cell adhesionIntegrinsSingle moleculeSuper-resolution microscopy

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Imaging

Background:

  • Visualizing cellular components with fluorescent proteins is crucial for understanding cell function.
  • Microscopy advances allow single-molecule resolution, but validating native behavior of labeled molecules is challenging.
  • Integrins mediate cell-extracellular matrix (ECM) interactions, linking ECM to the cytoskeleton.

Purpose of the Study:

  • To quantify the mobility and conformation of labeled integrins.
  • To investigate how labeling affects integrin behavior and cellular function.
  • To determine the coupling between molecular dynamics and cellular outputs.

Main Methods:

  • Utilized integrin alpha-beta heterodimers for labeling and analysis.
  • Employed microscopy techniques to observe integrin localization, mobility, and conformation.
  • Assessed cellular behaviors such as protrusive activity, adhesion size, and cell spreading.

Main Results:

  • Integrin mobility decreased when the beta subunit was labeled compared to the alpha subunit.
  • Beta-subunit labeling altered cellular behavior, reducing protrusion and increasing adhesion size and cell spreading.
  • Labeling the beta subunit induced conformational changes in integrins, extending the molecule and exposing an epitope.

Conclusions:

  • Fluorescent protein labeling can induce changes in integrin dynamics, conformation, and function.
  • These labeling-induced changes demonstrate a coupling between molecular behavior and cellular adhesion-dependent outputs.
  • The study highlights the importance of considering labeling artifacts in molecular visualization studies.