Initial characterization of endothelial mitogens produced by bovine corpora lutea from the estrous cycle

1993 ◽  
Vol 71 (5-6) ◽  
pp. 270-277 ◽  
Author(s):  
Anna T. Grazul-Bilska ◽  
Dale A. Redmer ◽  
S. Derek Killilea ◽  
Jing Zheng ◽  
Lawrence P. Reynolds
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Endothelial Cell Proliferation ◽  
Corpora Lutea ◽  
Dependent Manner ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Exchange Cation ◽  
Neutral Ph

To further characterize mitogenic factor(s) present in luteal extracts or luteal explant conditioned media (LCM), bovine corpora lutea (CL) were homogenized or incubated in explant culture, respectively. After evaluation of luteal extracts and LCM by using an endothelial cell proliferation bioassay, mitogenic activity was characterized by immunoneutralization with antibodies against heparin-binding (fibroblast) growth factor (HBGF) 1 or 2. LCM also were subjected to ultrafiltration, as well as anion-exchange, cation-exchange, and heparin-affinity chromatography. The presence of HBGF-2 in LCM also was evaluated by using a dot immunoblot assay. Extracts of luteal tissues and LCM stimulated (P < 0.05) proliferation of endothelial cells in a dose-dependent manner. Mitogenic activity of luteal extracts and LCM was decreased (P < 0.05) by treatment with specific antibodies against HBGF-2 or HBGF-1. LCM also contained immunoreactive HBGF-2. The mitogenic activity bound to anion exchangers, phenyl-Sepharose, and heparin–agarose, but not to cation exchangers, indicating that endothelial mitogenic activity is anionic at neutral pH, has some hydrophobic characteristics, and belongs to the HBGF family of proteins. Following ultrafiltration, endothelial mitogenic activity was retained by membranes having a 30 000 or 100 000 molecular weight cutoff. In addition, LCM was resolved into four peaks of heparin-binding endothelial mitogenic activity, each with a different affinity for heparin. These data demonstrate that bovine CL contain and produce endothelial mitogens of large molecular size, which may be important regulators of luteal function. These endothelial mitogens are heparin-binding and anionic at neutral pH. In addition, a large portion of the endothelial mitogenic activity produced by bovine CL appears to be immunologically related to HBGF-2 (basic fibroblast growth factor).Key words: angiogenesis, endothelial mitogens, corpus luteum, bovine.

Basic FGF activates phospholipase D in endothelial cells in the absence of inositol-lipid hydrolysis

1994 ◽  
Vol 266 (1) ◽  
pp. C206-C212 ◽  
Author(s):  
A. Ahmed ◽  
R. Plevin ◽  
M. A. Shoaibi ◽  
S. A. Fountain ◽  
R. A. Ferriani ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Phospholipase D ◽  
Growth Factor Receptor ◽  
Mitogenic Activity ◽  
Endothelial Cell Proliferation ◽  
Dependent Manner ◽  
Vascular Endothelial ◽  
Fibroblast Growth ◽  
Lipid Hydrolysis

In the absence of inositol-lipid hydrolysis, mitogenic concentrations of basic fibroblast growth factor (bFGF) stimulated phosphatidylbutanol formation in the presence of butan-1-ol in [3H]myristate-labeled human umbilical vascular endothelial (HUVE) cells, indicating that the fibroblast growth factor receptor was able to couple to the activation of phospholipase D (PLD). The ability of bFGF and 12-O-tetradecanoylphorbol-13-acetate (TPA) to stimulate PLD activity was completely abolished in cells pretreated with 400 nM TPA for 48 h to downregulate protein kinase C (PKC). bFGF-stimulated PLD activity was inhibited by genistein (5 microM; P < 0.02) and the PKC inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7, 5 microM; P < 0.001) as well as by the removal of calcium from extracellular environment. bFGF induced DNA synthesis in a dose-dependent manner, and pretreatment of cells with H-7 inhibited the mitogenic activity of bFGF. These results indicate that activation of PKC is responsible for bFGF-induced PLD activation and the mitogenic activity of bFGF in HUVE cells. A coupled PLD/3-sn-phosphatidate phosphohydrolase pathway may play a role in the regulation of endothelial cell proliferation.

Differential regulation of the fibroblast growth factor (FGF) family by α2-macroglobulin: evidence for selective modulation of FGF-2–induced angiogenesis

Blood ◽  
2001 ◽  
Vol 97 (11) ◽  
pp. 3450-3457 ◽  
Author(s):  
Iain R. Asplin ◽  
Sean M. Wu ◽  
Smitha Mathew ◽  
Gourab Bhattacharjee ◽  
Salvatore V. Pizzo
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Solid Phase ◽  
Cellular Growth ◽  
Endothelial Cell Proliferation ◽  
Dependent Manner ◽  
Fibroblast Growth ◽  
Collagen Gels ◽  
Α2 Macroglobulin ◽  
Extracellular Matrix Components

The fibroblast growth factor (FGF) family has an important role in processes such as angiogenesis, wound healing, and development in which precise control of proteinase activity is important. The human plasma proteinase inhibitor α2-macroglobulin (α2M) regulates cellular growth by binding and modulating the activity of many cytokines and growth factors. These studies investigate the ability of native and activated α2M (α2M*) to bind to members of the FGF family. Both α2M and α2M* bind specifically and saturably to FGF-1, -2, -4, and -6, although the binding to α2M* is of significantly higher affinity. Neither α2M nor α2M* bind to FGF-5, -7, -9, or -10. FGF-2 was chosen for more extensive study in view of its important role in angiogenesis. It was demonstrated that FGF-2 binds to the previously identified TGF-β binding site. The α2M* inhibits FGF-2–dependent fetal bovine heart endothelial cell proliferation in a dose-dependent manner. Unexpectedly, α2M* does not affect FGF-2–induced vascular tubule formation on Matrigel basement membrane matrix or collagen gels. Further studies demonstrate that FGF-2 partitions between fluid-phase α2M* and solid-phase Matrigel or collagen. These studies suggest that the ability of α2M* to modulate the activity of FGF-2 is dependent on an interplay with extracellular matrix components.

scholarly journals Decoding the Genetic Alterations in Genes of Fibroblast Growth Factor Family and Their Possible Association with HNSCC

2021 ◽  
pp. 698-710
Author(s):  
A. Akshaya ◽  
J. Vijayashree Priyadharsini ◽  
A. S. Smiline Girija ◽  
P. Sankar Ganesh ◽  
Nidhi Poddar
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Demographic Data ◽  
Primary Tumour ◽  
Genetic Alterations ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Fibroblast Growth Factor Family ◽  
Significant Difference ◽  
Cancer Phenotypes

Introduction: HNSCC is a type of cancer in the oral and pharynx region. Several mutations/variations are observed in these cancer phenotypes. Fibroblast growth factor belongs to the family of heparin binding growth factors. FGFs are multifunctional proteins with a wide variety of effects; they are most commonly mitogens. Their expression pattern correlates with invasion of HNSCC. Aim: To assess the genetic alterations in genes of the fibroblast growth factor family and their association with HNSCC. Materials and Methods: The demographic data and samples of 528 HNSCC patients was collected from the cBioportal database. Oncoprint analysis was done to assess the amplification and genetic alterations of the members of the FGF gene family. String analysis was performed to evaluate the protein-protein interaction. The information about previous reported mutation and correlation with novel and reported mutation was obtained using GnomAD analysis. Results and Discussion: FGF3,4 and 19 genes showed maximum variation (25%). FGF4 and FGF19 genes showed maximum amplification in addition to deletion mutation. Excitingly FGF3, FGF4 and FGF19 genes showed similar amplification patterns in most of the HNSCC patients. Statistical significant difference in the gene expression of FGF3 9.578 x 10-3 observed between normal and primary tumour. S.  Findings showed many novel mutations and also 4 reported mutations ie:FGF1, FGF12, FGF20, FGF21 Conclusion: Our present study concludes that more evidence is required to confirm their association with HNSCC.

scholarly journals Identification of a fibroblast growth factor-binding protein in Drosophila melanogaster.

1991 ◽  
Vol 11 (4) ◽  
pp. 2319-2323 ◽  
Author(s):  
J S Doctor ◽  
F M Hoffmann ◽  
B B Olwin
Keyword(s):  
Molecular Weight ◽  
Drosophila Melanogaster ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Binding Proteins ◽  
Specific Binding ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Acidic Fibroblast Growth Factor ◽  
Heparin Binding Growth Factors

As assessed by competitive binding and protein-crosslinking experiments, Drosophila melanogaster cells possess basic fibroblast growth factor (bFGF)-specific binding proteins that are similar to FGF receptors on vertebrate cells in molecular weight and binding affinity; these D. melanogaster cells, however, have no detectable binding proteins for acidic fibroblast growth factor (aFGF). Consistent with the presence of bFGF-specific binding proteins, D. melanogaster cells degrade bFGF but not aFGF. These results indicate the conservation of heparin-binding growth factors and receptors between vertebrates and D. melanogaster.

scholarly journals FHF1 is a bona fide fibroblast growth factor that activates cellular signaling in FGFR-dependent manner

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Martyna Sochacka ◽  
Lukasz Opalinski ◽  
Jakub Szymczyk ◽  
Marta B. Zimoch ◽  
Aleksandra Czyrek ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Cellular Signaling ◽  
Dependent Manner ◽  
Fibroblast Growth ◽  
Bona Fide
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