Chapter 6 Distribution of acidic and basic fibroblast growth factors in the mature, injured and developing rat nervous system

Eckenstein, F.; Andersson, Carl Magnus; Kuzis, K; Woodward, William R.

doi:10.1016/s0079-6123(08)61126-7

Cited by 32 publications

(16 citation statements)

References 50 publications

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“…In the brain, FGFR1-IIIb is particularly abundant in hippocampal dentate gyrus and cerebellar granule neurons. This is noteworthy because FGFs 1 and 2 are known to stimulate neurite outgrowth from both populations of neurons in vitro (39). The detection of FGFR1-IIIb mRNAs in various types of neurons demonstrates that expression of this receptor variant is not restricted to epithelial cells.…”

Section: Discussionmentioning

confidence: 91%

Fibroblast Growth Factor (FGF) Receptor 1-IIIb Is a Naturally Occurring Functional Receptor for FGFs That Is Preferentially Expressed in the Skin and the Brain

Beer¹,

Vindevoghel²,

Gait³

et al. 2000

Journal of Biological Chemistry

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Fibroblast growth factors (FGFs) 1 comprise a growing family of structurally conserved mitogens, which currently includes 19 different members (1-10). With the exception of FGF-7, which appears to act specifically on epithelial cells (11), most members of the FGF family are broad-spectrum mitogens, and several also stimulate various processes such as cell migration, angiogenesis, neurite outgrowth, and neuroprotection (12). FGFs interact with three different types of binding proteins. These include a cystein-rich receptor of as yet unknown function, which binds various types of FGFs with high affinity (13), and heparan sulfate proteoglycans, which bind FGFs with low affinities, although this interaction is essential for the binding of these factors to their high-affinity receptors (12). There are four different genes encoding high-affinity transmembrane receptors. These receptors, designated as FGF receptors 1 to 4 (FGFR1-4), are characterized by the presence of two or three immunoglobulin (Ig)-like domains in the extracellular region and a tyrosine kinase domain in the intracellular region of the receptor (14). They are responsible for FGF-mediated signal transduction (14). Additional diversity in the FGF receptor family is generated by alternative splicing. Of particular importance are splice variants that differ in the second half of the third Ig-like domain, since these variants differ in their ligand binding specificity (15-17). Thus two transmembrane receptor variants have been identified for FGFR2 that were designated FGFR2-IIIb and FGFR2-IIIc. Whereas the IIIb variant of FGFR2 binds FGF-1, -3, -7, and -10 with appreciable affinity (15, 19 -21), the IIIc variant is a high-affinity receptor for 20). By analogy to FGFR2, IIIb and IIIc splice variants have also been identified for FGFR3 (17), whereas this type of alternative splicing does not occur with the FGFR4 transcripts (22). Interestingly, three different exons (designated IIIa, IIIb and IIIc) that might encode possible alternatives within the third Ig-like domain are present in both the human and murine FGFR1 genes, and receptors including the IIIa and the IIIc exon have been identified (23). The receptor that contains exclusively the IIIa exon is a soluble variant, which binds FGF-2 with higher affinity than FGF-1 (24). FGFR1-IIIc is a transmembrane receptor that binds . By contrast, a full-length receptor cDNA, which includes sequences encoding the IIIb exon of FGFR1 has as yet not been isolated. However, mRNAs encoding the FGFR1-IIIb exon have been found in mice and humans using RNase protection assays and reverse transcriptase polymerase chain reaction (16,23). These mRNAs encode the complete extracellular domain of FGFR1-IIIb, but it has as yet not been possible to demonstrate the presence of sequences encoding the intracellular domain. Thus it has been unclear whether FGFR1-IIIb is a soluble or a transmembrane receptor and whether it is a functional receptor for FGFs. To gain some insight into the properties of a putative FGFR1-IIIb, we had prev...

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Section: Discussionmentioning

confidence: 91%

Fibroblast Growth Factor (FGF) Receptor 1-IIIb Is a Naturally Occurring Functional Receptor for FGFs That Is Preferentially Expressed in the Skin and the Brain

Beer¹,

Vindevoghel²,

Gait³

et al. 2000

Journal of Biological Chemistry

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“…FGF1 and FGF2 are the best characterized members of the FGF family; they are important in many biological processes, including cell growth, proliferation, and neurogenesis (53, 54). The transcription factor that regulates FGF2 expression has been cloned and studied (55).…”

Section: Discussionmentioning

confidence: 99%

Regulation of FGF1 Gene Promoter through Transcription Factor RFX1

Hsu

Liao

Kao

et al. 2010

Journal of Biological Chemistry

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Fibroblast growth factor 1 (FGF1) has been suggested to have an important role in cell growth, proliferation, and neurogenesis. Human FGF1 gene 1B promoter (−540 to +31)-driven green fluorescence (F1BGFP) has been shown to monitor endogenous FGF1 expression. F1BGFP could also be used to isolate neural stem/progenitor cells from embryonic, neonatal, and adult mouse brains or to isolate glioblastoma stem cells (GBM-SCs) from human glioblastoma tissues. Here, we present evidence that transcription factor RFX1 could bind the 18-bp cis-elements (−484 to −467) of the F1B promoter, modulate F1BGFP expression and endogenous FGF1 expression, and further regulate the maintenance of GBM-SCs. These observations were substantiated by using yeast one-hybrid assay, electrophoretic mobility shift assay, chromatin immunoprecipitation assay, gain- and loss-of-function assays, and neurosphere assays. Overexpression of RFX1 was shown to down-regulate FGF-1B mRNA expression and neurosphere formation in human glioblastoma cells, whereas RNA interference knockdown of RFX1 demonstrated the opposite effects. Our findings provide insight into FGF1 gene regulation and suggest that the roles of FGF1 and RFX1 in the maintenance of GBM-SCs. RFX1 may negatively regulate the self-renewal of GBM-SCs through modulating FGF-1B and FGF1 expression levels by binding the 18-bp cis-elements of the F1B promoter.

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“…It activates the glial reaction in the injured brain, thus influencing the regulation of ECM components in the brain inflammatory process (20,21) In the central nervous system, FGF is found in the cytoplasm and nucleus of neurons and astrocytes (22,23) and exerts its biological action through the binding with FGF receptors (FGFRs), identified as low-and high-affinity receptors (24). FGF2 was shown to be elevated in Alzheimer's disease and localized in the plaques and neurofibrillary tangles (25).…”

Section: Differences In Extracellular Matrix Production and Basic Fibmentioning

confidence: 99%

Differences in Extracellular Matrix Production and Basic Fibroblast Growth Factor Response in Skin Fibroblasts from Sporadic and Familial Alzheimer’s Disease

Bellucci

Lilli

Baroni

et al. 2007

Mol Med

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Extracellular matrix (ECM) molecules and growth factors, such as fibroblast growth factor (FGF), play a crucial role in Alzheimer's disease (AD). The purpose of this investigation was to determine whether phenotypic alterations in ECM production are present in non-neuronal AD cells associated with different FGF expression and response. Synthesis of glycosaminoglycans (GAG) and collagen were measured in skin fibroblasts from patients with familial, sporadic AD (FAD and SAD respectively), and from agematched controls by radiolabeled precursors. Proteoglycans (PG), metalloprotease (MMP)-1, and FGF gene expressions were measured by reverse transcription-polymerase chain reaction. The results showed different ECM neosynthesis and mRNA levels in the two AD fibroblast populations. FAD accumulated more collagen and secreted less GAG than SAD. Biglycan PG was upregulated in FAD while betaglycan, syndecan, and decorin were markedly downregulated in SAD fibroblasts. We found a significant decrease of MMP1, more marked in FAD than in SAD fibroblasts. Constitutive FGF expression was greatly reduced in both pathological conditions (SAD > FAD). Moreover, an inverse high affinity/low affinity FGF receptor ratio between SAD and FAD fibroblasts was observed. FGF treatment differently modulated ECM molecule production and gene expression in the two cell populations. These observations in association with the changes in FGF gene expression and in the FGF receptor number, suggest that cellular mechanisms downstream from FGF receptor binding are involved in the two different forms of AD.

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Chapter 6 Distribution of acidic and basic fibroblast growth factors in the mature, injured and developing rat nervous system

Cited by 32 publications

References 50 publications

Fibroblast Growth Factor (FGF) Receptor 1-IIIb Is a Naturally Occurring Functional Receptor for FGFs That Is Preferentially Expressed in the Skin and the Brain

Fibroblast Growth Factor (FGF) Receptor 1-IIIb Is a Naturally Occurring Functional Receptor for FGFs That Is Preferentially Expressed in the Skin and the Brain

Regulation of FGF1 Gene Promoter through Transcription Factor RFX1

Differences in Extracellular Matrix Production and Basic Fibroblast Growth Factor Response in Skin Fibroblasts from Sporadic and Familial Alzheimer’s Disease

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