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

2.6K
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...
2.6K
Basal Lamina are the Specialized Form of ECM01:03

Basal Lamina are the Specialized Form of ECM

3.2K
The basal lamina is a thin extracellular layer that lies underneath the cells and separates them from other tissues. The three layers of the basal lamina are lamina lucida, lamina densa and lamina reticularis. The basal lamina, a mixture of glycoproteins and collagen, provides an attachment site for the epithelium, separating it from underlying connective tissue. The framework of basal lamina has other essential proteins such as laminins mesh, perlecan, entactin, and type IV collagen.
Proteins...
3.2K
Anchoring Junctions01:03

Anchoring Junctions

4.3K
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
4.3K
Renewal of Skin Epidermal Stem Cells01:12

Renewal of Skin Epidermal Stem Cells

2.7K
The skin is divided into epidermis, dermis, and hypodermis, the skin's outermost, middle, and inner layers. The human epidermal layer regularly undergoes renewal, where old, dead cells are replaced by new cells. Epidermal stem cells or EpiSCs divide and differentiate to restore the lost cells. For the renewal process, some EpiSCs continuously self-renew. In contrast, few others differentiate into transit-amplifying cells, which later form prickle or spinous cells, followed by granular...
2.7K
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

2.4K
Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
2.4K
Role Of Notch Signalling In Intestinal Stem Cell Renewal01:12

Role Of Notch Signalling In Intestinal Stem Cell Renewal

2.2K
Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...
2.2K

You might also read

Related Articles

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

Sort by
Same author

Fibroblast depletion reveals mammalian epithelial resilience across neonatal and adult stages.

The Journal of cell biology·2026
Same author

Species-specific oxygen sensing governs the initiation of vertebrate limb regeneration.

Science (New York, N.Y.)·2026
Same author

Modeling aging in a culture dish: towards the development of more sophisticated in vitro models of human skin aging.

Ageing research reviews·2026
Same author

Restoring the tumour mechanophenotype of vocal fold cancer reverts its malignant properties.

Nature materials·2026
Same author

Engineered intestinal crypt geometry uncovers YAP1-dependent fetal-to-adult transition.

Cell stem cell·2026
Same author

Spectrin coordinates cell shape and signaling essential for epidermal differentiation.

The Journal of cell biology·2026

Related Experiment Video

Updated: Nov 6, 2025

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

1.2K

Laminin 332 Is Indispensable for Homeostatic Epidermal Differentiation Programs.

Raneem Tayem1, Catherin Niemann2, Monika Pesch1

  • 1Center for Biochemistry, Faculty of Medicine, University of Cologne, Cologne, Germany.

The Journal of Investigative Dermatology
|May 9, 2021
PubMed
Summary

Loss of laminin 332 (Lm332) causes skin blistering. Conditional Lm332 disruption in mice revealed its role in epidermal homeostasis, affecting keratinocyte fate and epidermal structure.

More Related Videos

Isolation and Culture of Primary Mouse Keratinocytes from Neonatal and Adult Mouse Skin
10:51

Isolation and Culture of Primary Mouse Keratinocytes from Neonatal and Adult Mouse Skin

Published on: July 14, 2017

32.1K
Generation of Genetically Modified Organotypic Skin Cultures Using Devitalized Human Dermis
09:16

Generation of Genetically Modified Organotypic Skin Cultures Using Devitalized Human Dermis

Published on: December 14, 2015

11.6K

Related Experiment Videos

Last Updated: Nov 6, 2025

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

1.2K
Isolation and Culture of Primary Mouse Keratinocytes from Neonatal and Adult Mouse Skin
10:51

Isolation and Culture of Primary Mouse Keratinocytes from Neonatal and Adult Mouse Skin

Published on: July 14, 2017

32.1K
Generation of Genetically Modified Organotypic Skin Cultures Using Devitalized Human Dermis
09:16

Generation of Genetically Modified Organotypic Skin Cultures Using Devitalized Human Dermis

Published on: December 14, 2015

11.6K

Area of Science:

  • Dermatology
  • Cell Biology
  • Molecular Biology

Background:

  • The skin epidermis relies on laminin 332 (Lm332) in the basement membrane for dermal attachment.
  • Lm332 deficiency causes severe blistering disorders like epidermolysis bullosa junctionalis.

Purpose of the Study:

  • To investigate the functions of Lm332 beyond keratinocyte adhesion.
  • To explore the consequences of Lm332 loss on epidermal homeostasis in adult mice.

Main Methods:

  • Conditional disruption of Lm332 expression in basal keratinocytes of adult mice.
  • Analysis of epidermal structure, RNA expression, and cytoskeletal organization.

Main Results:

  • Inducible Lm332 deletion was compatible with life due to hair follicle anchorage.
  • Loss of Lm332 led to epidermal thickening, exaggerated desquamation, and altered keratinocyte gene expression.
  • Changes included keratin and cornified envelope protein expression, cellular stress markers, cell shape, and actin cytoskeleton disorganization.

Conclusions:

  • Lm332 is crucial for maintaining epidermal homeostasis and proper keratinocyte progenitor cell adhesion.
  • Disruption of Lm332-mediated adhesion alters keratinocyte fate and disturbs epidermal integrity.
  • This study provides insights into Lm332's broader role in skin biology.