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Related Concept Videos

Integrins01:10

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,...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Activation of Integrins01:15

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.
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...
Selectins01:25

Selectins

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, which...

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Related Experiment Video

Updated: Jun 10, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

An engineered alpha1 integrin-binding collagenous sequence.

Neungseon Seo1, Brooke H Russell, Jose J Rivera

  • 1Center for Infectious and Inflammatory Diseases, Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|August 3, 2010
PubMed
Summary

Researchers modified bacterial collagen-like proteins (Scl2) with specific integrin-binding sequences. These engineered proteins selectively target α1β1 and α2β1 integrins, influencing cell attachment but not platelet aggregation.

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Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction

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Last Updated: Jun 10, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
07:12

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
12:38

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction

Published on: February 15, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomaterials Science

Background:

  • Collagen, an extracellular matrix protein, regulates cellular functions via integrin interactions (α1β1, α2β1, α10β1, α11β1).
  • Bacterial collagen-like proteins (Scl) offer a versatile scaffold for protein engineering.

Purpose of the Study:

  • To engineer Streptococcus pyogenes Scl2 protein by incorporating specific integrin-binding sequences.
  • To investigate the binding specificities of modified Scl2 proteins to human integrin α1β1 and α2β1.
  • To evaluate the functional consequences of these modifications on cell adhesion and platelet aggregation.

Main Methods:

  • Site-directed mutagenesis was used to introduce integrin-binding sequences (GLPGER, GFPGER, GFPGEN) into the Scl2 backbone.
  • Enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) were employed to assess protein-ligand interactions.
  • Cell adhesion assays using C2C12 cells, fibroblasts, endothelial cells, and smooth muscle cells were performed.

Main Results:

  • Modified Scl2 proteins (Scl2(GLPGER), Scl2(GFPGER), Scl2(GFPGEN)) maintained triple helix stability.
  • Scl2(GLPGER) and Scl2(GFPGER) bound to α1 and α2 I-domains metal-dependently, independent of hydroxyproline.
  • Scl2(GFPGEN) demonstrated selective binding to the α1 I-domain, while Scl2(GLPGER) and Scl2(GFPGER) bound to both α1 and α2 I-domains.
  • Modified Scl2 proteins mediated cell attachment for various cell types but did not aggregate platelets.

Conclusions:

  • Streptococcal collagen-like protein 2 (Scl2) serves as an effective scaffold for introducing mammalian integrin-binding motifs.
  • Engineered Scl2 variants can be designed to selectively target specific integrin subtypes (α1β1 and α2β1).
  • These findings open avenues for developing targeted biomaterials and therapeutic agents modulating cell-matrix interactions.