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

4.3K
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...
4.3K
Anchoring Junctions01:03

Anchoring Junctions

5.7K
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:...
5.7K
Tight Junctions01:29

Tight Junctions

9.0K
Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
9.0K
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

4.3K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
4.3K
Adherens Junctions01:24

Adherens Junctions

7.8K
Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
7.8K
Surface Membrane Barriers01:18

Surface Membrane Barriers

3.6K
The skin and mucous membranes serve as the primary line of defense against pathogens by providing both physical and chemical protection. These barriers are essential in preventing the entry and establishment of microbes, thereby maintaining the integrity of the host.
The outer layer of the skin, the epidermis, is a robust barrier comprising layers of closely packed keratinized cells. This dense arrangement prevents microbes from penetrating the body. The periodic shedding of epidermal cells...
3.6K

You might also read

Related Articles

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

Sort by
Same author

Heterogeneous structure and distinctive rheological behavior of loach skin mucin aqueous solution.

International journal of biological macromolecules·2026
Same author

Unlocking Electronic Spatiotemporal Confinement to Activate FeMn-Based Phosphates for High Energy Density and Ultra-Wide Temperature Na Storage.

Journal of the American Chemical Society·2026
Same author

Flourishing among undergraduate nursing students: Insights from a latent profile analysis.

Acta psychologica·2026
Same author

DR-MHEA-GCN: A Semisupervised Graph Framework with Dual-Residual Edge Attention for Chemical Bond Classification in 2D Nanomaterials.

The journal of physical chemistry letters·2026
Same author

Schottky-Orbital Coupling Drives Ion-Electron Transfer: Triggering Stable Fast-Charging in MnV-Based Phosphate Cathode.

Angewandte Chemie (International ed. in English)·2026
Same author

Sustainable Aqueous Zn-ion Batteries: Green Materials, Low-Carbon Manufacturing, and Circular Economy.

Angewandte Chemie (International ed. in English)·2026

Related Experiment Video

Updated: Apr 15, 2026

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
09:24

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

27.5K

Boundary lubrication by associative mucin.

Xiang Wang1, Miao Du1, Hongpeng Han1

  • 1MOE Key Laboratory of Macromolecular Synthesis and Functionalization, Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China.

Langmuir : the ACS Journal of Surfaces and Colloids
|April 7, 2015
PubMed
Summary

This study shows that associative mucin in mucus significantly reduces friction by forming gel structures. Intermolecular associations, not adsorbed layers, are key to this enhanced boundary lubrication.

More Related Videos

Macro-Rheology Characterization of Gill Raker Mucus in the Silver Carp, Hypophthalmichthys molitrix
09:13

Macro-Rheology Characterization of Gill Raker Mucus in the Silver Carp, Hypophthalmichthys molitrix

Published on: July 10, 2020

3.6K
Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
09:54

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

11.3K

Related Experiment Videos

Last Updated: Apr 15, 2026

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
09:24

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

27.5K
Macro-Rheology Characterization of Gill Raker Mucus in the Silver Carp, Hypophthalmichthys molitrix
09:13

Macro-Rheology Characterization of Gill Raker Mucus in the Silver Carp, Hypophthalmichthys molitrix

Published on: July 10, 2020

3.6K
Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
09:54

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

11.3K

Area of Science:

  • Tribology
  • Biomaterials Science
  • Biophysics

Background:

  • Mucus acts as a lubricant in organisms, relying on associative mucin for its gel structure.
  • Limited tribological research exists on associative mucin fluids.
  • Understanding mucin's lubrication mechanisms is crucial for biomaterial applications.

Purpose of the Study:

  • To investigate the tribological behavior of intact vertebrate mucin (loach skin mucin).
  • To explore the role of hydrophobic associations in mucin's lubricating properties.
  • To determine the relationship between mucin concentration, association, and boundary lubrication.

Main Methods:

  • Investigated loach skin mucin's friction on hydrophobic and hydrophilic polydimethylsiloxane (PDMS) substrates.
  • Varied mucin concentration and used sodium dodecyl sulfate (SDS) to disrupt associations.
  • Measured boundary friction coefficients (μ) under physiological conditions.

Main Results:

  • Loach skin mucin reduced boundary friction by up to 10-fold.
  • Lubrication on hydrophobic PDMS was stable, while it decreased on hydrophilic PDMS over time.
  • Lubricating ability correlated with mucin concentration (μ ∼ c(-0.7)) and was impaired by SDS, indicating the importance of intermucin associations.

Conclusions:

  • Intermolecular mucin association in bulk solution significantly enhances boundary lubrication.
  • Tightly adsorbed mucin layers play a minimal role in lubrication.
  • Associated mucin is a major contributor to the lubricating ability of biological mucus in vivo.