CD147-targeting siRNA inhibits cell-matrix adhesion of human malignant melanoma cells by phosphorylating focal adhesion kinase

2011 ◽  
Vol 39 (1) ◽  
pp. 63-67 ◽  
Author(s):  
Rie NISHIBABA ◽  
Yuko HIGASHI ◽  
Juan SU ◽  
Tatsuhiko FURUKAWA ◽  
Kazuhiro KAWAI ◽  
...  
Keyword(s):  
Malignant Melanoma ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Melanoma Cells ◽  
Human Malignant Melanoma ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion

scholarly journals Ezrin Interacts with Focal Adhesion Kinase and Induces Its Activation Independently of Cell-matrix Adhesion

2001 ◽  
Vol 276 (40) ◽  
pp. 37686-37691 ◽  
Author(s):  
Patrick Poullet ◽  
Alexis Gautreau ◽  
Gress Kadaré ◽  
Jean-Antoine Girault ◽  
Daniel Louvard ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion

scholarly journals Protein tyrosine phosphatase 1B, PTP1B, targets fak and paxillin in cell-matrix adhesions

2021 ◽  
Author(s):  
Ana E. González Wusener ◽  
Ángela González ◽  
María E. Perez Collado ◽  
Melina R. Maza ◽  
Ignacio J. General ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Bimolecular Fluorescence Complementation ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Adhesion Sites ◽  
Cell Matrix Adhesion

Protein tyrosine phosphatase 1B (PTP1B) is an established regulator of cell-matrix adhesion and motility. However, the nature of substrate targets at adhesion sites remains to be validated. Here we used Bimolecular Fluorescence Complementation (BiFC) assays in combination with a substrate trapping mutant of PTP1B to directly examine whether relevant phosphotyrosines on paxillin and FAK are substrates of the phosphatase in the context of cell-matrix adhesion sites. We find that formation of catalytic complexes at cell-matrix adhesions requires intact tyrosine residues Y31 and Y118 on paxillin and the localization of the focal adhesion kinase (FAK) at adhesion sites. In addition, we find that PTP1B specifically targets the Y925 on the focal adhesion target (FAT) domain of FAK at adhesion sites. Electrostatic analysis indicates that dephosphorylation of this residue promotes the closed conformation of the FAT 4-helix bundle, and its interaction with paxillin at adhesion sites.

scholarly journals The focal adhesion kinase (P125FAK) is constitutively active in human malignant melanoma

Oncogene ◽  
2002 ◽  
Vol 21 (25) ◽  
pp. 3969-3977 ◽  
Author(s):  
Orlie Kahana ◽  
Michael Micksche ◽  
Isaac P Witz ◽  
Ilana Yron
Keyword(s):  
Malignant Melanoma ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Human Malignant Melanoma ◽  
Constitutively Active

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

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.

scholarly journals Cell–matrix adhesion

2007 ◽  
Vol 213 (3) ◽  
pp. 565-573 ◽  
Author(s):  
Allison L. Berrier ◽  
Kenneth M. Yamada
Keyword(s):  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion

scholarly journals Toxicogenomics of A375 human malignant melanoma cells treated with arbutin

2006 ◽  
Vol 14 (1) ◽  
pp. 87-105 ◽  
Author(s):  
Sun-Long Cheng ◽  
Rosa Huang Liu ◽  
Jin-Nan Sheu ◽  
Shui-Tein Chen ◽  
Supachok Sinchaikul ◽  
...  
Keyword(s):  
Malignant Melanoma ◽  
Melanoma Cells ◽  
Human Malignant Melanoma
Sign in / Sign up

Export Citation Format

Share Document