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...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
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...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

You might also read

Related Articles

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

Sort by
Same author

Glycocalyx and basal lamina in neurological disorders.

Matrix biology : journal of the International Society for Matrix Biology·2026
Same author

Dual AAV amelioration of Lama2-null muscular dystrophy and neuropathy.

bioRxiv : the preprint server for biology·2026
Same author

Glomerular basement membrane structural integrity dictates trans-tissue deposition of laminin in the kidney.

Cell reports·2026
Same author

Cryo-EM reveals molecular mechanisms underlying the inhibitory effect of netrin-4 on laminin matrix formation.

Nature communications·2025
Same author

Polymerizing laminins in development, health, and disease.

The Journal of biological chemistry·2024
Same author

Dual transgene amelioration of Lama2-null muscular dystrophy.

Matrix biology : journal of the International Society for Matrix Biology·2023
Same journal

Airway macrophage specific glycocalyx expression and remodeling following viral infection.

Matrix biology : journal of the International Society for Matrix Biology·2026
Same journal

Cartilage intermediate layer protein (CILP) in cardiac fibrosis: Protective or pathogenic?

Matrix biology : journal of the International Society for Matrix Biology·2026
Same journal

Oligodendrocyte integrin-β1 regulates blood-brain barrier and remyelination in hemorrhagic brain.

Matrix biology : journal of the International Society for Matrix Biology·2026
Same journal

Dynamic regulation of the tissue microenvironment by integrins and the extracellular matrix.

Matrix biology : journal of the International Society for Matrix Biology·2026
Same journal

Corrigendum to "Basement membrane components define the microenvironment of aggregated fibroblasts in the skin and support their aggregation in vitro" [Matrix Biology 146 (2026) 102008].

Matrix biology : journal of the International Society for Matrix Biology·2026
Same journal

The Cost of Convenient Truths: Artificial Intelligence in Matrix Biology.

Matrix biology : journal of the International Society for Matrix Biology·2026
See all related articles

Related Experiment Video

Updated: Jun 27, 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

Polymerizing laminins: Assembly, functions and disorders.

Peter D Yurchenco1

  • 1Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ, USA.

Matrix Biology : Journal of the International Society for Matrix Biology
|June 25, 2026
PubMed
Summary
This summary is machine-generated.

Laminin polymerization is crucial for basement membrane assembly. Restoring laminin polymerization via gene therapy shows promise for treating laminin-alpha2-deficient congenital muscular dystrophy.

Keywords:
basement membraneslaminin, collagen, nidogen, proteoglycan, structure, muscular, dystrophy

More Related Videos

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture
07:44

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture

Published on: March 3, 2023

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

Related Experiment Videos

Last Updated: Jun 27, 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

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture
07:44

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture

Published on: March 3, 2023

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

Area of Science:

  • Biochemistry and Molecular Biology
  • Cell Biology
  • Genetics and Disease Mechanisms

Background:

  • Laminins are key proteins initiating basement membrane assembly through cell adhesion and polymerization.
  • Laminin polymerization occurs via specific LN domain interactions, forming polymer nodes that are essential for matrix structure.
  • Mutations in the LAMA2 gene cause laminin-alpha2-deficient congenital muscular dystrophy, impacting muscle, nerve, and brain tissues.

Purpose of the Study:

  • To elucidate the molecular mechanisms of laminin polymerization and its role in basement membrane formation.
  • To investigate the structural basis of laminin polymerization defects in LAMA2-deficient muscular dystrophy.
  • To develop and evaluate gene therapy strategies for ameliorating laminin-alpha2-deficient muscular dystrophy.

Main Methods:

  • Utilized negative staining, mutagenesis, and cryo-electron microscopy to study laminin polymerization nodes.
  • Employed a dy2J/dy2J mouse model to test therapeutic strategies involving laminin-binding proteins with functional alpha1-LN domains.
  • Investigated a dy3K/dy3K mouse model, assessing the efficacy of expressing proteins that enable polymerization and dystroglycan binding via adeno-associated virus (AAV) delivery.

Main Results:

  • The laminin polymer node is a triskelion structure formed by specific 'toe-to-heel' LN domain interactions.
  • In-frame mutations in the alpha2-LN domain can prevent essential laminin polymerization, leading to dystrophy.
  • Gene therapy approaches using AAV to deliver genes encoding functional laminin-binding proteins demonstrated disease amelioration in mouse models.

Conclusions:

  • Laminin polymerization is a critical, structurally defined process for basement membrane integrity.
  • Defective laminin polymerization due to LAMA2 mutations underlies a subset of congenital muscular dystrophies.
  • Adeno-associated virus-mediated gene therapy holds significant therapeutic potential for treating laminin-alpha2-deficient muscular dystrophies.