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Alterations in the expression of VEGF-A (show VEGFA Proteins) and bFGF (show FGF2 Proteins) systems suggest that angiogenic factors are involved in abnormal placental development in cloned gestations, contributing to impaired fetal development and poor survival rates.
These findings suggest that high levels of FGFR4 can increase glucose metabolism and lead to chemoresistance in breast cancer and reveal the mechanistic basis for targeting FGFR4 as a therapeutic opportunity for chemoresistant tumors.
Taken together, this study provides the first evidence that Blu9931 functions as a FGFR4-selective inhibitor in colorectal cancer (CRC (show CALR Proteins)) cells, and Blu9931 may be a new targeted drug.
Results show that FGFR4 promotes gastric cancer cell proliferation, migration and epithelial-to-mesenchymal transition. Its expression is negatively regulated by miR (show MLXIP Proteins)-491-5p through SNAIL protein (show SNAI1 Proteins).
Our findings indicate that the FGFR4-388Arg variant may play an important role in lung squamous cell carcinoma, which may be mediated by the overactivation of the MAPK (show MAPK1 Proteins) pathway.
FGFR4 rs351855 could be a novel independent prognostic factor of BCR (show BCR Proteins) after radical prostatectomy in the Chinese population.
This meta-analysis demonstrates the FGFR (show FGFR2 Proteins) rs351855 G>A polymorphism is associated with increased cancer risk.
Our results indicate that mRNA expression of FGFR4-related genes may be a biomarker to define the distinctive molecular phenotype of intrahepatic cholangiocarcinoma
The present study employed FGFR4 polymorphism to help identify treatments for high risk patients with stage III colon cancer.
Our data indicate that FGFR4 polymorphic isoforms mediate signaling that yields mitochondrial therapeutic targets of relevance to the actions of different somatostatin (show SST Proteins) analogs.
In radiosensitive SW480 and DLD1 cells, enforced expression of FGFR4 stabilized RAD51 (show RAD51 Proteins) protein levels resulting in enhanced clearance of gamma-H2AX (show H2AFX Proteins) foci and increased cell survival in the mismatch repair (MMR (show MRC1 Proteins))-proficient SW480 cells.
ileal FGF15/19 to hepatic FGFR4 axis is activated and promotes liver regeneration (LR) after partial hepatectomy (PH) in mice, supporting the potential of ileal FGF15/19 to hepatic FGFR4 axis-targeted therapy to enhance LR after PH
FRS2alpha (show FRS2 Proteins)-mediated pathways are essential for the FGF15/FGF19-FGFR4 signaling axis to control bile acid homeostasis.
Results indicate that FGFR4 is an important growth signal receptor in gastric cancer cells with high FGFR4 expression.
The findings suggest that the primary role of Fgfr3 (show FGFR3 Proteins) and Fgfr4 is to control the orderly formation of elastin (show ELN Proteins) fibers. In a normal lung, FGFR3 (show FGFR3 Proteins) and FGFR4 restrict the expression of MFAP5 (show MFAP5 Proteins), among other elastogenesis factors.
FGF23 (show FGF23 Proteins) augments pro-fibrotic signalling cascades in injury-primed renal fibroblasts via activation of FGFR4
the localization of FGF9 and its receptors at different embryonic and postnatal stages in mice testes, was examined.
Blocking FGFR4 inhibits cardiac calcineurin/NFAT (show NFATC1 Proteins) signaling and attenuates the development of LVH and cardiac fibrosis in a well-established animal model of CKD without significantly altering kidney function, blood pressure, or FGF23 (show FGF23 Proteins) levels.
The FGFR4 transmembrane polymorphic variants can modulate cellular growth and sensitivity to glucocorticoid hormone negative feedback.
FGFR4 deficiency in mice leads to improvement in glucose metabolism, insulin (show INS Proteins) sensitivity, and reduction in body weight under high fat conditions.
The FGFR4-R388 allele yields a receptor variant that preferentially promotes STAT3 (show STAT3 Proteins)/5 signaling.
Fgfr4 mediates a signal-transduction pathway between Wnt16 (show WNT16 Proteins) and Dlc, but not Dld, to regulate haematopoietic stem cells specification.
The analysis of receptor-ligand interactions between D. rerio fgf8 (show FGF8 Proteins) and its receptors, fgfr1 (show FGFR1 Proteins) and fgfr4, using combined spectroscopy methods are reported.
The protein encoded by this gene is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. The genomic organization of this gene, compared to members 1-3, encompasses 18 exons rather than 19 or 20. Although alternative splicing has been observed, there is no evidence that the C-terminal half of the IgIII domain of this protein varies between three alternate forms, as indicated for members 1-3. This particular family member preferentially binds acidic fibroblast growth factor and, although its specific function is unknown, it is overexpressed in gynecological tumor samples, suggesting a role in breast and ovarian tumorigenesis.
fibroblast growth factor receptor 4
, FGF receptor 4
, hydroxyaryl-protein kinase
, protein-tyrosine kinase
, tyrosine kinase related to fibroblast growth factor receptor
, tyrosylprotein kinase
, CTLA-2-beta protein
, fibroblast growth factor receptor 4 16 minus form
, protein-tyrosine kinase receptor MPK-11
, fibroblast growth factor receptor FREK
, fibroblast growth factor receptor-like embryonic kinase
, fibroblast growth factor receptor 4c