Phosphatases in cell–matrix adhesion and migration

Cell-cell adhesion is a key mechanism to control tissue integrity and migration. In head and neck squamous cell carcinoma (HNSCC), cell migration facilitates distant metastases and is correlated with poor prognosis. RAP1, a ras-like protein, has an important role in the progression of HNSCC. RAC1 is an integrin-linked, ras-like protein that promotes cell migration. Here we show that loss of cell-cell adhesion is correlated with inactivation of RAP1 confirmed by 2 different biochemical approaches. RAP1 activation is required for cell-matrix adhesion confirmed by adhesion to fibronectin-coated plates with cells that have biochemically activated RAP1. This effect is reversed when RAP1 is inactivated. In addition, RAP1GTP-mediated adhesion is only facilitated through α5β1 integrin complex and is not a function of either α5 or β1 integrin alone. Moreover, the inside-out signaling of RAP1 activation is coordinated with RAC1 activation. These findings show that RAP1 has a prominent role in cell-matrix adhesion via extracellular matrix molecule fibronectin-induced α5β1 integrin and supports a critical role for the RAP1/RAC1 signaling axis in HNSCC cell migration.

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A New Candidate Substrate for Cell-Matrix Adhesion Study: The Acellular Human Amniotic Matrix

Journal of Biomedicine and Biotechnology ◽

10.1155/2012/306083 ◽

2012 ◽

Vol 2012 ◽

pp. 1-10 ◽

Cited By ~ 7

Author(s):

Qianchen Guo ◽

Xuya Lu ◽

Yuan Xue ◽

Hong Zheng ◽

Xiaotao Zhao ◽

...

Keyword(s):

Tensile Force ◽

Three Dimensional ◽

Biomechanical Properties ◽

Simple Method ◽

Matrix Adhesion ◽

Cell Matrix ◽

And Migration ◽

Cell Matrix Adhesion

In vivoadhesions between cells and the extracellular matrix play a crucial role in cell differentiation, proliferation, and migration as well as tissue remodeling. Natural three-dimensional (3D) matrices, such as self-assembling matrices and Matrigel, have limitations in terms of their biomechanical properties. Here, we present a simple method to produce an acellular human amniotic matrix (AHAM) with preserved biomechanical properties and a favorable adhesion potential. On the stromal side of the AHAM, human foreskin fibroblasts (HFFs) attached and extended with bipolar spindle-shaped morphology proliferated to multilayer networks, invaded into the AHAM, and migrated in a straight line. Moreover,αV integrin, paxillin, and fibronectin were observed to colocalize after 24 h of HFF culture on the stromal side of the AHAM. Our results indicate that the AHAM may be an ideal candidate as a cell-matrix adhesion substrate to study cell adhesion and invasion as well as other functionsin vitrounder a tensile force that mimics thein vivoenvironment.

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Faculty Opinions recommendation of Cell-matrix adhesion controls Golgi organization and function through Arf1 activation in anchorage-dependent cells.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.733708071.793549021 ◽

2018 ◽

Author(s):

Martin A Schwartz

Keyword(s):

Matrix Adhesion ◽

Cell Matrix ◽

And Function ◽

Golgi Organization ◽

Cell Matrix Adhesion

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Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells

International Journal of Molecular Sciences ◽

10.3390/ijms22105144 ◽

2021 ◽

Vol 22 (10) ◽

pp. 5144

Author(s):

Antonín Sedlář ◽

Martina Trávníčková ◽

Pavla Bojarová ◽

Miluše Vlachová ◽

Kristýna Slámová ◽

...

Keyword(s):

Stem Cells ◽

Endothelial Cells ◽

Cell Adhesion ◽

Vascular Tissue ◽

Cell Functions ◽

Matrix Adhesion ◽

Cell Matrix ◽

Selective Ligand ◽

Galectin 3 ◽

Cell Matrix Adhesion

Galectin-3 (Gal-3) is a β-galactoside-binding protein that influences various cell functions, including cell adhesion. We focused on the role of Gal-3 as an extracellular ligand mediating cell-matrix adhesion. We used human adipose tissue-derived stem cells and human umbilical vein endothelial cells that are promising for vascular tissue engineering. We found that these cells naturally contained Gal-3 on their surface and inside the cells. Moreover, they were able to associate with exogenous Gal-3 added to the culture medium. This association was reduced with a β-galactoside LacdiNAc (GalNAcβ1,4GlcNAc), a selective ligand of Gal-3, which binds to the carbohydrate recognition domain (CRD) in the Gal-3 molecule. This ligand was also able to detach Gal-3 newly associated with cells but not Gal-3 naturally present on cells. In addition, Gal-3 preadsorbed on plastic surfaces acted as an adhesion ligand for both cell types, and the cell adhesion was resistant to blocking with LacdiNAc. This result suggests that the adhesion was mediated by a binding site different from the CRD. The blocking of integrin adhesion receptors on cells with specific antibodies revealed that the cell adhesion to the preadsorbed Gal-3 was mediated, at least partially, by β1 and αV integrins—namely α5β1, αVβ3, and αVβ1 integrins.

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