Heparin-binding (fibroblast) growth factors type one and two genes are co-expressed in proliferating normal human vascular endothelial and smooth muscle cells in culture

1990 ◽  
Vol 26 (2) ◽  
pp. 209-212 ◽  
Author(s):  
Per-Erik Mansson ◽  
Marlene Malark ◽  
Hidekazu Sawada ◽  
Mikio Kan ◽  
Wallace L. McKeehan
Keyword(s):  
Smooth Muscle ◽  
Growth Factors ◽  
Smooth Muscle Cells ◽  
Fibroblast Growth Factors ◽  
Muscle Cells ◽  
Vascular Endothelial ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Cells In Culture ◽  
Normal Human

Physiological Effects of Androgens on Human Vascular Endothelial and Smooth Muscle Cells in Culture

2011 ◽  
pp. P1-2-P1-2
Author(s):  
Lina Nheu ◽  
Shanhong Ling ◽  
Lester Nazareth ◽  
Rui Zhi Luo ◽  
Paul Alter Komesaroff
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Vascular Endothelial ◽  
Physiological Effects ◽  
Cells In Culture

Regulation Of Vascular Prostacyclin (PGI2) Synthesis

1981 ◽  
Author(s):  
S Coughlin ◽  
M Moskowitz ◽  
H N Antoniades ◽  
L Levine
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Cell Types ◽  
Feedback Mechanism ◽  
Vascular Endothelial ◽  
Serum Factor ◽  
Negative Feedback Mechanism ◽  
Cells In Culture ◽  
Other Substances

We have examined the possibility that substances released during platelet degranulation modify vascular PGI2 synthesis. PGI2 is a potent inhibitor of platelet function produced by vascular endothelial and smooth muscle cells. Regulation of PGI2 synthesis by blood vessels is not well understood. We report that a platelet- dependent factor in serum dramatically stimulates PGI2 synthesis by vascular endothelial and smooth muscle cells in culture. We further report that platelet-derived growth factor (PDGF), a releasable protein found in platelet alpha granules, stimulates PGI2 synthesis by the above cell types by over 100 fold. The concentration of PDGF required to elicit this effect is below that reported in human serum. The above mentioned serum factor is relatively heat stable, non-dialyzable, and cationic; preliminary studies indicate that anti-PDGF antiserum is capable of blocking stimulation of PGI2 synthesis by both PDGF and serum. These data suggest that the serum factor may indeed be PDGF. PDGF acts synergistically with other platelet granule constituents (serotonin, ATP) and with thrombin to stimulate PGI2 synthesis by vascular cells in culture. We thus postulate that platelet-released PDGF, in concert with other substances generated during clotting, acts to increase vessel wall PGI2 synthesis as part of a negative feedback mechanism controlling platelet aggregation. A defect in the ability of a blood vessel to increase PGI2 production in response to platelet degranulation, as may occur in atherosclerotic vessels, could perhaps contribute to the genesis of thromboembolic events.

IGF-I increases bFGF-induced mitogenesis and upregulates FGFR-1 in rabbit vascular smooth muscle cells

1996 ◽  
Vol 270 (4) ◽  
pp. H1141-H1148 ◽  
Author(s):  
T. J. Reape ◽  
J. M. Kanczler ◽  
J. P. Ward ◽  
C. R. Thomas
Keyword(s):  
Smooth Muscle ◽  
Growth Factors ◽  
Growth Factor ◽  
Smooth Muscle Cells ◽  
Dna Synthesis ◽  
Fibroblast Growth Factor ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Fibroblast Growth ◽  
Igf I

Insulin-like growth factor-I (IGF-I) and basic fibroblast growth factor (bFGF) have both been implicated in the abnormal proliferation of vascular smooth muscle cells (VSMC) that occurs after injury to the arterial wall in vivo. We have investigated the effects of these growth factors on proliferation of rabbit aortic smooth muscle cells (RASMC) in vitro. IGF-I, in contrast to bFGF, is a weak mitogen for RASMC. However, when IGF-I (10 ng/ml) was added in combination with bFGF for 24 h, the effect of the two growth factors on DNA synthesis was synergistic at all concentrations tested (P > 0.001 compared with summed values of bFGF alone plus IGF-I alone), and this synergy was also observed at the level of RASMC proliferation (P < 0.001). Time-course experiments indicated that although bFGF was able to stimulate DNA synthesis after 16 h, activity peaked at 24 h, and a synergistic response with IGF-I was not observed before 24 h. Northern blot analysis demonstrated that IGF-I (10 ng/ml) could selectively upregulate fibroblast growth factor receptor-1 (FGFR-1) mRNA 4.0 +/- 0.24-fold (P < 0.001) without a significant effect on FGFR-2, and this induction in FGFR-1 mRNA occurs in a time- and dose-dependent manner. In addition, IGF-I increases FGFR-1 protein levels in RASMC 2.7 +/- 0.12-fold (P < 0.01), as demonstrated by Western blotting, and this upregulation occurs before the peak in DNA synthesis. These results suggest that IGF-I may be capable of increasing the responsiveness of VSMC to bFGF through modulation of FGFR-1.

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