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

Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
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,...
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...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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.
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...

You might also read

Related Articles

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

Sort by
Same author

Emergence of functional prey depletion halo through penguin-krill behavioural dynamics.

Proceedings. Biological sciences·2026
Same author

GPR17+ Oligodendrocyte Lineage Cells Regulate the Critical Period of Brain Development Through Novel Chondroitin Sulfate-Rich Structures.

Glia·2026
Same author

A Novel Near-Infrared Fluorescence Vaginal Pipe (LunaPipe) for Navigation in Robot-Assisted Total Hysterectomy.

Journal of minimally invasive gynecology·2026
Same author

Tracking of Neuroinflammation Dynamics During Combined Anti-β-Amyloid Therapy (AAT) and Immunomodulation in a Preclinical Alzheimer's Disease Model.

International journal of molecular sciences·2026
Same author

Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network.

The Journal of biological chemistry·2026
Same author

Direct Selection of Functional De Novo Macrocycles for Activation of On-Cellulo Insulin Receptor.

Angewandte Chemie (International ed. in English)·2026

Related Experiment Video

Updated: Jun 12, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Laminin-121--recombinant expression and interactions with integrins.

Takako Sasaki1, Junichi Takagi, Camilla Giudici

  • 1Max-Planck-Institut für Biochemie, Martinsried, Germany. tsasaki@molmed.uni-erlangen.de

Matrix Biology : Journal of the International Society for Matrix Biology
|June 23, 2010
PubMed
Summary

Recombinant laminin-121 (laminin-3) exhibits high affinity for specific integrins, promoting neurite outgrowth. This suggests β2 laminins offer greater integrin binding than β1 laminins.

More Related Videos

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

Fabrication and Characterization of Layer-By-Layer Janus Base Nano-Matrix to Promote Cartilage Regeneration
08:55

Fabrication and Characterization of Layer-By-Layer Janus Base Nano-Matrix to Promote Cartilage Regeneration

Published on: July 6, 2022

Related Experiment Videos

Last Updated: Jun 12, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

Fabrication and Characterization of Layer-By-Layer Janus Base Nano-Matrix to Promote Cartilage Regeneration
08:55

Fabrication and Characterization of Layer-By-Layer Janus Base Nano-Matrix to Promote Cartilage Regeneration

Published on: July 6, 2022

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Laminins are crucial extracellular matrix glycoproteins involved in cell adhesion and differentiation.
  • Laminin-121, previously known as laminin-3, is a heterotrimer composed of α1, β2, and γ1 chains.

Purpose of the Study:

  • To recombinantly express and characterize laminin-121.
  • To compare the integrin binding affinities and biological functions of laminin-121 with other laminin isoforms.

Main Methods:

  • Triple transfection of human embryonic kidney (HEK) 293 cells to express mouse laminin α1, β2, and γ1 chains.
  • Purification of recombinant laminin-121 using Heparin-Sepharose and molecular sieve chromatography.
  • Analysis of protein folding by electron microscopy and circular dichroism (CD).
  • Assessment of integrin binding affinities and support of neurite outgrowth.

Main Results:

  • Recombinant laminin-121 was successfully expressed, purified, and shown to be correctly folded.
  • CD spectra indicated reduced stability of the coiled-coil structure in laminin-121 compared to laminin-111.
  • Laminin-121 demonstrated the highest affinity for α6β1 and α7β1 integrins.
  • Laminin-121 most effectively supported neurite outgrowth.

Conclusions:

  • The β2 laminin chain contributes to higher integrin binding affinity compared to the β1 chain.
  • Laminin-121 is a potent stimulator of neurite outgrowth due to its strong integrin interactions.