Related Experiment Video
Updated: Jul 9, 2025
09:14
Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
16.2K
Leucine-Rich Repeat Containing 15-Mediated Cell Adhesion Is Essential for Integrin Signaling in TGF-β1-Induced PDL
Hyun-Jin Kim1, Dong-Jun Kim1, Seong-Min Kim1
1Department of Nanobiomedical Science and BK21 FOUR NBM Global Research Center for Regenerative Medicine, Dankook University, Cheonan, Korea.
Stem Cells (Dayton, Ohio)
|December 5, 2023
Summary
Leucine-rich repeat containing 15 (LRRC15) is crucial for human periodontal ligament cell (hPDLC) differentiation into fibroblasts. Inhibiting LRRC15 disrupts cell morphology and key signaling pathways involved in periodontal ligament regeneration.
Area of Science:
- Cell Biology
- Biochemistry
- Regenerative Medicine
Background:
- Human periodontal ligament cells (hPDLCs) possess stem cell properties and can differentiate into periodontal ligament (PDL) fibroblasts.
- Extracellular matrix and cell surface molecules are vital for cellular differentiation processes.
Purpose of the Study:
- To identify and characterize cell surface molecules involved in TGF-β1-induced PDL fibroblast differentiation.
- To investigate the role of leucine-rich repeat containing 15 (LRRC15) in PDL fibroblast differentiation and function.
Main Methods:
- Development of monoclonal antibodies against PDL fibroblast-specific cell surface molecules.
- Mass spectrometry to identify the antigen recognized by anti-PDL51 antibody as LRRC15.
- siRNA-mediated depletion and antibody blocking to inhibit LRRC15 function.
- Analysis of cell morphology, marker expression, and signaling pathways (integrin β1, focal adhesion kinase).
Main Results:
- The anti-PDL51 antibody specifically recognizes LRRC15, which is upregulated during TGF-β1-induced PDL fibroblast differentiation.
- Increased LRRC15 expression was observed at the cell surface and membrane during fibroblastic differentiation.
- LRRC15 inhibition led to downregulation of PDL fibroblastic markers, loss of cell elongation, and altered cell morphology.
- LRRC15 interacts with integrin β1, activating the focal adhesion kinase signaling pathway and regulating cell adhesion, proliferation, and migration.
Conclusions:
- LRRC15 is a key regulator of PDL fibroblast differentiation, morphology, and function.
- LRRC15 plays a critical role in activating integrin-mediated signaling pathways essential for PDL cell activities.
- Targeting LRRC15 may offer therapeutic potential for periodontal regeneration.
Keywords:
TGF-β1focal adhesion kinasehuman periodontal ligament cellsintegrin α11β1leucine-rich repeat containing 15periodontal ligament fibroblastsMore Related Videos
Related Concept Videos
01:17Intracellular Signaling Affects Focal Adhesions
2.7K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
2.7K
01:16TGF - β Signaling Pathway
7.4K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.4K
01:10Integrins
4.0K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.0K
01:15Activation of Integrins
3.5K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
3.5K
00:55Laminins are the Adhesive Proteins of Basal Lamina
2.2K
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...
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...
2.2K
01:31Mechanism of Lamellipodia Formation
2.6K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.6K