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DDR2 overexpression is independently associated with tumor progression and poor survival rates in urothelial carcinoma patients.
The DDR2 E655K mutation can play a role in cancer progression.
collagen II-activated phosphorylated-DDR2 induces CYR61 (show CYR61 Proteins) through activation of transcription factor activator protein 1 (AP-1 (show FOSB Proteins)). The elevated CYR61 (show CYR61 Proteins), in turn, accelerates MMP1 (show MMP1 Proteins) production via ETS1 (ETS (show ETS1 Proteins) proto-oncogene (show RAB1A Proteins) 1).
these data suggest that biological collagen aging could increase tumor cell proliferation by reducing the activation of the key matrix sensor DDR2
Female ddr2-deficient mice homozygous for the slie mutation show inefficient spontaneous BC metastasis.
This study suggested that DDR1 (show DDR1 Proteins) and DDR2 knockdown alters brain immunity and significantly reduces the level of triggering receptor expressed on myeloid cells (TREM)-2 (show TREM2 Proteins) and microglia.
This work identifies DDR2 as a potential therapeutic target that controls breast cancer metastases through its action in both tumor cells and tumor-stromal cells at the primary tumor site.
The group of patients with colorectal cancer with high DDR2 expression had significantly higher frequencies of T4, lymph node metastasis, and peritoneal dissemination compared to the group with low DDR2 expression.
DDR2 showed high expression in gastric cancer tissues and cells. In xenograft models, DDR2 overexpression promoted tumor formation. Furthermore, DDR2 expression impacted on the invasion and motility of GC cells, accompanied by changes in EMT (show ITK Proteins) marker expression. Finally, our results revealed that DDR2 facilitates GC cell invasion and EMT (show ITK Proteins) through mTORC2 (show CRTC2 Proteins) activation and AKT (show AKT1 Proteins) phosphorylation.
DDR2 mediates collagen-induced activation of MT1-MMP (show MMP14 Proteins) in human fibroblasts
DDR2 is important for maintenance of osteoblast activity and suppression of marrow adipogenesis in vivo and these actions are related to changes in MAPK (show MAPK1 Proteins)-dependent RUNX2 (show RUNX2 Proteins) and PPARgamma (show PPARG Proteins) phosphorylation.
circulating fibroblast precursors expressing DDR2, in an exposure-induced model of pulmonary fibrosis, is reported.
The progressive process of articular cartilage degeneration was significantly delayed in the knee joints of Ddr2-deficient mice in comparison to their control littermates. Articular cartilage damage in the knee joints of the mice was associated with increased expression profiles of both Ddr2 and matrix metalloproteinase 13 (show MMP13 Proteins).
DDR2 mutation can drive lung cancer initiation in vivo and provide a novel mouse model for lung cancer therapeutics studies.
Study showed that Nrp1 (show NRP1 Proteins) expression paralleled with that of DDR2 during osteoblast differentiation. Nrp1 (show NRP1 Proteins) assisted the promoting role of DDR2 in osteoblast differentiation, via activation of DDR2-mediated downstream signaling.
Data show that discoidin domain receptor (DDR (show DDR1 Proteins)) 2 siRNA-mediated suppression of extracellular regulated kinase (ERK) 1 (show MAPK3 Proteins) and 2 and nuclear factor of kappa B (NF-kappaB (show NFKB1 Proteins)) could down-regulate the expressions of matrix metalloproteinase (MMP) 2 (show MMP2 Proteins) and 9.
RESULTS Data show that DDR2 (discoidin domain receptor 2) suppresses osteoclast differentiation and activity.
DDR2 signaling regulates cell proliferation and extracellular matrix synthesis, which are key aspects of fibroblast contribution to tissue healing [review]
Germline deletion of the DDR2 results in smaller hearts, shorter cardiomyocytes, lower interstitial cardiac collagen density and abnormalities in cardiac function.
DDR2 activation may be effected by single triple-helices rather than fibrillar collagen
Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain. Alternative splicing in the 5' UTR results in multiple transcript variants encoding the same protein.
CD167 antigen-like family member B
, cell migration-inducing protein 20
, discoidin domain receptor 2
, discoidin domain receptor family, member 2
, discoidin domain-containing receptor 2
, discoidin domain-containing receptor tyrosine kinase 2
, hydroxyaryl-protein kinase
, migration-inducing gene 16 protein
, neurotrophic tyrosine kinase receptor related 3
, neurotrophic tyrosine kinase, receptor-related 3
, receptor protein-tyrosine kinase TKT
, tyrosine-protein kinase TYRO10
, tyrosylprotein kinase
, discoidin domain receptor tyrosine kinase 2
, CD167b antigen
, tyrosine-protein kinase TYRO 10