Discoidin domain receptors (DDRs): Potential implications in periodontitis

2021 ◽  
Author(s):  
Rui Ma ◽  
Xudong Xie ◽  
Lei Zhao ◽  
Yafei Wu ◽  
Jun Wang
Keyword(s):  
Discoidin Domain Receptors

scholarly journals Tyrosine kinase discoidin domain receptors DDR1 and DDR2 are coordinately deregulated in triple-negative breast cancer

2015 ◽  
Vol 150 (1) ◽  
pp. 9-18 ◽  
Author(s):  
Kathy A. Toy ◽  
Rajeshwari R. Valiathan ◽  
Fernando Núñez ◽  
Kelley M. Kidwell ◽  
Maria E. Gonzalez ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Tyrosine Kinase ◽  
Triple Negative Breast Cancer ◽  
Triple Negative ◽  
Discoidin Domain Receptors

Discoidin Domain Receptors in Normal Mammary Development and Breast Cancer Progression

2016 ◽  
pp. 119-144
Author(s):  
Sandamali A. Ekanayaka ◽  
Celina G. Kleer ◽  
Aliccia Bollig-Fischer ◽  
Rodrigo Fernandez-Valdivia ◽  
Rafael Fridman
Keyword(s):  
Breast Cancer ◽  
Cancer Progression ◽  
Mammary Development ◽  
Breast Cancer Progression ◽  
Discoidin Domain Receptors

Discoidin Domain Receptors in Liver Fibrosis

2016 ◽  
pp. 293-313
Author(s):  
Elvira Olaso ◽  
Joana Marquez ◽  
Aitor Benedicto ◽  
Iker Badiola ◽  
Beatriz Arteta
Keyword(s):  
Liver Fibrosis ◽  
Discoidin Domain Receptors

Discoidin domain receptors (DDRs): Potential implications in atherosclerosis

2015 ◽  
Vol 751 ◽  
pp. 28-33 ◽  
Author(s):  
Gui-Xia Ju ◽  
Ying-Bin Hu ◽  
Mei-Rong Du ◽  
Jun-Lin Jiang
Keyword(s):  
Discoidin Domain Receptors

DDR1/E-cadherin complex regulates the activation of DDR1 and cell spreading

2009 ◽  
Vol 297 (2) ◽  
pp. C419-C429 ◽  
Author(s):  
Chau-Zen Wang ◽  
Yi-Chun Yeh ◽  
Ming-Jer Tang
Keyword(s):  
Small Interfering Rna ◽  
Cell Spreading ◽  
Cell Junctions ◽  
Cell Junction ◽  
Cell Behavior ◽  
P120 Catenin ◽  
Discoidin Domain Receptors ◽  
Collagen Receptors ◽  
Interfering Rna ◽  
E Cadherin

Discoidin domain receptors (DDRs) 1 and 2, collagen receptors, regulate cell adhesion and a broad range of cell behavior. Their adhesion-dependent regulation of signaling associated with adhesion proteins has not been elucidated. We report a novel mechanism: the cross talk of DDR1 and E-cadherin negatively and adhesion dependently regulated both DDR1 activity and DDR1-suppressed cell spreading. E-cadherin forms complexes with both DDR1 isoforms (a and b). E-cadherin regulates DDR1 activity associated with the cell-junction complexes formed between DDR1 and E-cadherin. These complexes are formed independently of DDR1 activation and of β-catenin and p120-catenin binding to E-cadherin; they are ubiquitous in epithelial cells. Small interfering RNA-mediated gene silencing of E-cadherin restores both DDR1 activity and DDR1-suppressed cell spreading and increases the apically and basally located DDR1 in E-cadherin-null cells. We conclude that E-cadherin-mediated adhesions decrease DDR1 activity, which subsequently eliminates DDR1-suppressed cell spreading, by sequestering DDR1 to cell junctions, which prevents its contact with collagen ligand.

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