Sep 12, 2023 · Discoidin domain receptor 1 (DDR1) is an important signal transducer that mediates crosstalk between cancer cells and their surrounding stroma. Due to the very high concentrations of its ligand, cleaved collagen (COL), DDR1 exerts a …

Discoidin domain receptor 1 (DDR1) is upregulated in multiple cancers and positively associated with chemoresistance. We explored the effect of DDR1a on the cytotoxicity induced by 5-FU in LoVo cells and the underlying mechanism.

Mar 30, 2025 · DDR1 (Discoidin Domain Receptor Tyrosine Kinase 1) is a Protein Coding gene. Diseases associated with DDR1 include Adenocarcinoma and Melanoma. Among its related pathways are GPCR Pathway and ERK Signaling.

Functional comparison of two splice variants of DDR1 (DDR1a and DDR1b) reveal novel differences in cell based glioma models. Overexpression of either DDR1a or DDR1b caused increased cell attachment.

Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2. J Neurooncol. 2006;76 (3):239-48.

Nov 1, 2019 · Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2

Of the five DDR1 isoforms, three (DDR1a, DDR1b, DDR1c) are functional receptors (Fig 1A). The longest isoform, termed DDR1c, contains 919 amino acids, while the most common isoforms, DDR1a and DDR1b, lack six amino acids in the kinase domain with respect to DDR1c.

Background: Although discoidin domain receptor 1 (DDR1) can enhance cell invasion in bladder cancer by regulating the expression of epithelial-mesenchymal transition (EMT)-related molecules, the isoforms responsible for the phenomenon are still unknown.

Discoidin domain receptor 1 (DDR1) is an important signal transducer that mediates crosstalk between cancer cells and their surrounding stroma. Duetotheveryhighconcentrationsofits ligand, cleaved collagen (COL), DDR1 exerts a profound effect on tumor metabolism.

While DDR1 has five isoforms (DDR1a, DDR1b, DDR1c, DDR1d, and DDR1e) different in the extent of glycosylation, protein interactions, expression patterns, phosphorylation, as well as functions, DDR2 has only a single isoform to date.