Search results for "Fibroblast growth factor receptor 4"
showing 3 items of 3 documents
Collagen membranes of dermal and pericardial origin-In vivo evolvement of vascularization over time.
2020
Aim of the study was to compare the evolvement of vascularization over time of collagen membranes (CMs) of dermal and pericardial origin in an in vivo animal study. Twenty-eight mice underwent implantation of three commercially available CM derived from porcine dermis (homogenous structure: CM1 (Control 1) and bilayer structure: CM2 [Control 2]), from porcine pericardium (CM3; Test 1) as well as CM3 sprayed with silica-enhanced nanostructured hydroxyapatite (CM4, Test 2). After 3, 6, 9, and 12 days, intravital fluorescence microscopy was conducted for determination of capillary diameter, density, flow, and length. At Day 12, samples were examined immunohistologically for expression of fibro…
Fibroblast growth factor-2 and its receptor expression in proliferating precursor cells of the subventricular zone in the adult rat brain
2008
Several findings have suggested the existence in the subventricular zone (SVZ) from sagittal sections of adult rat brain of a trophic mechanism, mediated by fibroblast growth factor-2 (FGF-2) and its multiple high-affinity FGF receptors (FGFRs), regulating neurogenesis mainly by controlling precursor cell proliferation. However, no clear data are available on the expression of FGF-2 and FGFRs in proliferating precursor cells of the SVZ. To address these questions we examined FGF-2 mRNA and its FGFR mRNA expression in proliferating precursor cells of the SVZ by using a double labeling procedure, combining in situ hybridization for FGF-2 and its FGFR mRNA with immunohistochemistry for bromode…
Expression and glycosylation studies of human FGF receptor 4
2001
Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large am…