Fibroblast Growth Factors

The presence of basic fibroblast growth factor (bFGF) in the third and the lateral ventricular ependyma of the rat has been investigated under the light microscope using a polyclonal antibody against bFGF, through the unlabelled peroxidase-antiperoxidase procedure; bFGF-immunoreactivity (bFGF-IR) is observed in the entire ependymal cell layer of ventricles. Also ependymal tanycytes within the inferior portion of the wall and floor of the third ventricle show bFGF-IR. Tanycytic processes are in close contact with hypothalamic capillaries. The present study strongly suggests that brain ependymal bFGF plays unidentified roles unrelated to its angiogenic or mitogenic capacities.

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“…or other functions [15]. Despite the presence of bFGF in the CNS, the precise role of bFGF in the nervous system remains unclear.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Localization of Basic Fibroblast Growth Factor in Ependymal Cells of the Rat Lateral and Third Ventricles

Cuevas

Giménez‐Gallego

Martı́nez-Murillo

et al. 1991

Cells Tissues Organs

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“…FGF-2 induces proliferation of fibroblasts and keratinocytes and is a potent angiogenic and chemotactic agent for endothelial cells and fibroblasts (45,46). FGF-2 together with FGF-1, FGF-5, and FGF-7 are present in normal skin, and their expression levels increase upon injury (47).…”

Section: Rescue Of Reduced Cell Proliferation In Granulation Tissue Omentioning

confidence: 99%

Inhibition by the Soluble Syndecan-1 Ectodomains Delays Wound Repair in Mice Overexpressing Syndecan-1

Elenius

Götte

Reizes

et al. 2004

Journal of Biological Chemistry

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Wound repair is a tightly regulated process stimulated by proteases, growth factors, and chemokines, which are modulated by heparan sulfate. To characterize further the role of the heparan sulfate proteoglycan syndecan-1 in wound repair, we generated mice overexpressing syndecan-1 (Snd/Snd) and studied dermal wound repair. Wound closure, reepithelialization, granulation tissue formation, and remodeling were delayed in Snd/Snd mice. Soluble syndecan-1 was increased, and shedding was prolonged in wounds from Snd/Snd mice. Excess syndecan-1 increased the elastolytic activity of wound fluids. Additionally, cells in the granulation tissue and keratinocytes at wound edges showed markedly reduced proliferation rates in Snd/Snd mice. Skin grafting experiments between Snd/Snd and control mice indicated that the slower growth rate was mainly due to a soluble factor in the Snd/Snd mouse skin. Syndecan-1 immunodepletion and further degradation experiments identified syndecan-1 ectodomain as a dominant negative inhibitor of cell proliferation. These studies indicate that shed syndecan-1 ectodomain may enhance proteolytic activity and inhibit cell proliferation during wound repair.

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“…At the times indicated, the cell (C) and corresponding media (M) fractions were processed, immune complexes prepared using rabbit polyclonal anti-hCG␣ antibody, separated by 12% SDS-PAGE and the signal visualized by fluorography. The location of 14 C-labeled molecular size standards are indicated at the right.…”

Section: Cardenolides Inhibit Export Of Fgf-2 From Cos-1 Cells-inmentioning

confidence: 99%

“…It is also noteworthy to mention that the results presented here do not preclude the possibility that cytoplasmic interactions between FGF-2 and the ␣-subunit of Na ϩ ,K ϩ -ATPase reflects a heretofore unrecognized role for FGF-2 in modulating Na ϩ ,K ϩ -ATPase activity. The catalytic subunit of Na ϩ ,K ϩ -ATPase is ubiquitous in cells and tissues (28), much like FGF-2 (14) and it is often found at the basolateral membrane (33) where FGF-2 is deposited into the extracellular matrix.…”

Section: Fig 8 Varying the External Namentioning

confidence: 99%

“…Two prototypic members of the fibroblast growth factor (FGF) family of polypeptide growth factors, FGF-1 and FGF-2, do not contain a hydrophobic signal peptide sequence (13)(14)(15)). Yet, data from a variety of experiments indicate that both proteins are detected extracellularly, they interact with one or more integral plasma membrane receptors (16) and are exported from transfected cells in an ATP-dependent, brefeldin A-resistant, ER/Golgi-independent manner (9,10,12).…”

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confidence: 99%

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The Inhibition of Fibroblast Growth Factor-2 Export by Cardenolides Implies a Novel Function for the Catalytic Subunit of Na+,K+-ATPase

Florkiewicz¹,

Anchin²,

Baird³

1998

Journal of Biological Chemistry

136

111

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Basic fibroblast growth factor (FGF-2) is one of a select group of proteins that can exit cells through an alternate, endoplasmic reticulum/Golgi apparatus independent exocytic pathway. This alternate pathway has been termed protein export. In an attempt to better understand this process, we have identified a family of related compounds, "cardenolides," that inhibit FGF-2 export. The cardenolides inhibit FGF-2 export in a time and concentration dependent fashion. Inhibition of FGF-2 export is specific in that the cardenolides have no effect on conventional protein secretion as measured by their inability to block release of the secreted protein human chorionic gonadotropin-␣.Because cardenolides are known to inhibit ion transport activity mediated by Na Taken together, these data: 1) identify a novel activity for cardenolides; 2) suggest a previously unknown role for the ␣-subunit of Na ؉ , K ؉

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Fibroblast Growth Factors

Cited by 138 publications

References 230 publications

Immunohistochemical Localization of Basic Fibroblast Growth Factor in Ependymal Cells of the Rat Lateral and Third Ventricles

Immunohistochemical Localization of Basic Fibroblast Growth Factor in Ependymal Cells of the Rat Lateral and Third Ventricles

Inhibition by the Soluble Syndecan-1 Ectodomains Delays Wound Repair in Mice Overexpressing Syndecan-1

The Inhibition of Fibroblast Growth Factor-2 Export by Cardenolides Implies a Novel Function for the Catalytic Subunit of Na+,K+-ATPase

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