Related Experiment Video
Updated: Feb 8, 2026
09:04
Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells
Published on: May 22, 2014
21.4K
Cyclic Stretching Exacerbates Tendinitis by Enhancing NLRP3 Inflammasome Activity via F-Actin Depolymerization.
Qiufang Chen1, Jun Zhou2, Bingyu Zhang1
1Key Laboratory of Biorheological Science and Technology, College of Bioengineering, Ministry of Education, Chongqing University, Chongqing, 400044, China.
Inflammation
|June 29, 2018
Summary
The NLRP3 inflammasome contributes to tendinitis by promoting inflammation. Cyclic stretching activates this pathway, suggesting new therapeutic targets for tendon inflammation.
Area of Science:
- Molecular Biology
- Immunology
- Cell Biology
Background:
- Tendinopathy involves inflammation, impacting treatment outcomes.
- The NLRP3 inflammasome is implicated in various disease pathologies.
Purpose of the Study:
- To investigate NLRP3 inflammasome's role in tendinitis.
- To determine if cyclic stretching influences tendon inflammation via this pathway.
Main Methods:
- Examined the effect of hydrogen peroxide (H2O2) on inflammatory markers.
- Assessed NLRP3 inflammasome activation and IL-1β maturation in tenocytes.
- Investigated the impact of cyclic stretching on NLRP3 inflammasome activation.
- Analyzed the role of filamentous actin (F-actin) depolymerization.
Main Results:
- H2O2 enhanced IL-1β, TNF-α, and IL-6 expression and release.
- H2O2-induced IL-1β maturation required NLRP3 inflammasome activation.
- Cyclic stretching promoted H2O2-induced NLRP3 inflammasome activation in tenocytes.
- F-actin depolymerization was necessary for cyclic stretching-enhanced NLRP3 inflammasome activation.
Conclusions:
- NLRP3 inflammasome plays a key role in tendinitis pathogenesis.
- Cyclic stretching exacerbates inflammation by activating the NLRP3/IL-1β pathway.
- Findings support novel anti-inflammatory treatment strategies for tendinopathy.
Related Concept Videos
01:19Actin Filament Depolymerization
4.0K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
4.0K
01:18Actin Treadmilling
9.7K
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
9.7K
02:33Stereoisomerism of Cyclic Compounds
11.1K
In this lesson, we delve into the role of ring conformation and its stability, which determines the spatial arrangement and, consequently, the molecular symmetry and stereoisomerism of cyclic compounds. 1,2-Dimethylcyclohexane is used as a case study to evaluate the possible number of stereoisomers. Here, given the multiple (n = 2) chiral centers, there are 2n = 4 possible configurations that lack a plane of symmetry, as the ring skeleton exists in a non-planar chair conformation. In addition,...
11.1K
01:24IR Frequency Region: X–H Stretching
1.5K
In IR spectroscopy, signals produced by the X−H bonds (such as C−H, O−H, or N−H) can be observed in the frequency range of 2700–4000 cm–1. The C−H stretching vibration forms sharp bands in the region 2850–3000 cm–1. The presence of the O−H stretching vibration leads to the forming of an absorption band in the frequency range 3650–3200 cm−1. At the same time, N−H stretching can be confirmed by absorption bands in...
1.5K
01:26Introduction to Actin
6.6K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across...
6.6K
01:42Actin Polymerization
8.6K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
8.6K