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Validated All-in-One™ qPCR Primer for DDR2(NM_006182.4) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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. [provided by RefSeq].
Gene References into function
- gene expression analysis with DDR2 overexpression, using microarrays specific for human and mouse genes coding for extracellular matrix proteins or ECM-interacting factors
- DDR1 and DDR2 have roles in the regulation of collagen turnover mediated by SMCs in obstructive diseases of blood vessels and the lung
- Results describe a site-specific interaction of discoidin domain receptor 2 with collagen II and gives novel insight into the nature of the interaction of collagen II with matrix receptors.
- DDR2 2 mediates tumor cell cycle arrest induced by fibrillar collagen
- DDR2 autophosphorylation generates cytosolic domain phosphotyrosines that promote the formation of DDR2 cytosolic domain-Shc signaling complexes.
- the triple-helical region of collagen X contains a specific DDR2 binding site that is capable of receptor activation
- All these findings suggested that the fused expressed His-DR inhibited the activity of natural DDR2, and relevant MMP-1 and MMP-2 expression in synoviocytes and NIH3T3 cells provoked by collagen II.
- altered expression of DDR1 may contribute to malignant progression of non-small cell lung carcinoma
- This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.
- Overexpression of DDR2 is associated with papillary thyroid carcinomas
- the perpetuation of DDR-2 expression and activation can be seen as a vicious circle that ultimately leads to cartilage destruction in osteoarthritis
- DDR2 activation may be effected by single triple-helices rather than fibrillar collagen
- There are three missense mutations c.2254 C > T [R752C], c. 2177 T > G [I726R], c.2138C > T [T713I] and one splice site mutation [IVS17+1g > a] in the conserved sequence encoding the tyrosine kinase domain of the DDR2 gene.