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

Structure of Cadherins01:25

Structure of Cadherins

4.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.6K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

6.0K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
6.0K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.1K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.1K
Catenins01:23

Catenins

3.0K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
3.0K
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

3.4K
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...
3.4K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

3.7K
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
3.7K

You might also read

Related Articles

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

Sort by
Same author

Transformer-based advertisement image layout generation and object fidelity optimization.

PloS one·2026
Same author

Post-cardiac surgery mortality in ICU patients with serum glucose-potassium ratio: A retrospective cohort analysis of the MIMIC-IV database.

Medicine·2026
Same author

Polystyrene nanoparticles and phosphorus sources jointly modulate antibiotic resistance gene enrichment in microalgae-bacteria systems.

Journal of hazardous materials·2026
Same author

Proposing an explanatory framework based on the fear-avoidance model: a mixed-methods analysis of kinesiophobia in patients after percutaneous coronary intervention in home-based cardiac rehabilitation.

Frontiers in cardiovascular medicine·2026
Same author

Identification of potential therapeutic targets for idiopathic pulmonary fibrosis: an integrated multiomics analysis.

Frontiers in immunology·2026
Same author

Correlation between nerve conduction velocity abnormality patterns and clinical severity grading in chemotherapy-induced peripheral neuropathy: a retrospective cohort study.

Frontiers in neurology·2026

Related Experiment Video

Updated: Jan 12, 2026

A Calcium Bioluminescence Assay for Functional Analysis of Mosquito Aedes aegypti and Tick Rhipicephalus microplus G Protein-coupled Receptors
10:46

A Calcium Bioluminescence Assay for Functional Analysis of Mosquito Aedes aegypti and Tick Rhipicephalus microplus G Protein-coupled Receptors

Published on: April 20, 2011

16.0K

Functional characterization of a calcium-dependent bacterial-binding C-type lectin from amphioxus.

Huiqing Huang1, Enjin Deng2, Dandan Xu1

  • 1Guangdong Food and Drug Vocational College, No. 321 Longdong North Road, Tianhe District, Guangzhou 510520, China.

International Immunopharmacology
|November 8, 2025
PubMed
Summary
This summary is machine-generated.

We identified AmphiCTL6, a novel C-type lectin (CTL) in amphioxus, acting as a broad-spectrum pattern recognition receptor (PRR). It binds diverse bacteria, highlighting its role in innate immunity and gut surveillance.

Keywords:
AgglutinationAmphioxusC-type lectinInnate immunityPattern recognition receptors

More Related Videos

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.9K
A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors
08:46

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

Published on: December 2, 2022

2.7K

Related Experiment Videos

Last Updated: Jan 12, 2026

A Calcium Bioluminescence Assay for Functional Analysis of Mosquito Aedes aegypti and Tick Rhipicephalus microplus G Protein-coupled Receptors
10:46

A Calcium Bioluminescence Assay for Functional Analysis of Mosquito Aedes aegypti and Tick Rhipicephalus microplus G Protein-coupled Receptors

Published on: April 20, 2011

16.0K
Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.9K
A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors
08:46

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

Published on: December 2, 2022

2.7K

Area of Science:

  • Innate immunity
  • Comparative immunology
  • Marine biology

Background:

  • C-type lectins (CTLs) are crucial pattern recognition receptors (PRRs) in innate immunity.
  • Amphioxus possesses a vast repertoire of CTL genes, yet few are functionally characterized.
  • Understanding CTL function in basal chordates like amphioxus provides insights into immune evolution.

Purpose of the Study:

  • To characterize a novel CTL, AmphiCTL6, from Branchiostoma japonicum (B. japonicum).
  • To investigate the immune functions and binding capabilities of AmphiCTL6.
  • To explore the role of AmphiCTL6 in the innate immune system of amphioxus.

Main Methods:

  • Gene prediction and genomic analysis identified AmphiCTL6.
  • In situ hybridization and single-cell RNA-seq determined AmphiCTL6 expression patterns.
  • Recombinant protein expression, carbohydrate-binding assays, bacterial agglutination, and domain-truncation analyses were performed.

Main Results:

  • AmphiCTL6 exhibits a unique structure with tandem EGF-like domains and a CTLD.
  • High expression was observed in the hepatic cecum, intestine, gills, and gonads, particularly in gut epithelial cells.
  • AmphiCTL6 demonstrated calcium-dependent binding and agglutination of diverse bacteria, with the CTLD mediating these interactions.

Conclusions:

  • AmphiCTL6 functions as a broad-spectrum pattern recognition receptor (PRR) in amphioxus.
  • This finding expands the known functional diversity of CTLs in basal chordates.
  • AmphiCTL6 plays a significant role in gut immune surveillance and innate immunity.