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Effect of Notoginsenoside Rl on the Synthesis of Tissue-Type Plasminogen Activator and Plasminogen Activator Inhibitor-1 in Cultured Human Umbilical Vein Endothelial Cells
| Content Provider | Semantic Scholar |
|---|---|
| Author | Zhang, Weijian Wojta, Johann Binder, Bernd R. |
| Copyright Year | 2005 |
| Abstract | Among other Chinese herb drugs, Panax notoginseng is used to treat cardiovascular diseases. To elucidate any possible effects of this drug on the hemostatic system in vitro, we analyzed the influence of one of its major active constituents on fibrinolytic parameters of cultured human umbilical vein endothelial cells (HUVECs). When confluent cultures of HUVECs (passages 2 to 3) were conditioned with purified notoginsenoside Rl (NR1), a dose(0.01 to 100 fig NRl/mL) and time-dependent increase in tissue-type plasminogen activator (TPA) synthesis was observed, which was significant from 0.1 jig NRl/mL and from 6 hours of incubation with 100 /xg NRl/mL on. TPA antigen increased from 3.9 ±0.2 ng per 1$ cells per 24 hours to 8.0±0.5 ng per 10 cells per 24 hours on addition of 100 /ig NRl/mL. In contrast, no change in urokinase-type plasminogen activator and plasminogen activator inhibitor-1 (PAI-1) antigen synthesis was seen. There was also no effect of NR1 on PAI-1 deposition in the extracellular matrix. As judged from fibrin autography and reverse fibrin The fibrinolytic system functions as a basic defense mechanism to control the deposition of fibrin in both vascular and extravascular systems. Proper functioning of the fibrinolytic system is necessary to prevent not only hemorrhagic as well as thrombotic phenomena but also the formation of interstitial fibrin deposits and subsequent scarring. Tissue-type plasminogen activator (TPA) is considered to play an important role in initiation of the extrinsic fibrinolytic route through conversion of the zymogen plasminogen to the active enzyme plasmin, which degrades fibrin. The fibrinolytic capacity of plasma is thus considered to be strongly dependent on the concentration of circulating TPA. Plasma TPA is presumed to be derived mainly from the vascular wall, where it is localized in endothelial cells (ECs). The availability of ECs in culture has provided an opportunity to study the regulation of TPA synthesis by these cells in more detail. Insight into the regulation of TPA Received January 21, 1994; revision accepted May 7, 1994. From the Laboratory for Clinical and Experimental Physiology, Department of Medical Physiology, University of Vienna (Austria) (W.Z., J.W., B.R.B.), and the Department of Physiology, Beijing University of Traditional Chinese Medicine (PROC) (W.Z.). Reprint requests to Johann Wojta, PhD, Laboratory for Clinical and Experimental Physiology, Department of Medical Physiology, Schwarzspanierstrasse 17, A-1090 Vienna, Austria. © 1994 American Heart Association, Inc. autography, TPA activity and TPA-PAI-1 complexes reached a maximal stimulation of more than threefold and twofold, respectively, at a concentration of 100 fig NRl/mL in conditioned media. On the contrary, NR1 induced a more than fivefold decrease in PAI-1 activity at the same concentration of NR1 in conditioned media. On Northern blot analysis of RNA obtained from NRl-stimulated and control HUVECs, NR1 induced a significant increase in TPA mRNA (192% of control value at 100 /xg NRl/mL) while PAI-1 mRNA remained unchanged. Our data indicate that in fact NR1 contained in the Chinese herb used to treat cardiovascular diseases can induce a profibrinolytic response in cultured HUVECs, an effect that may also be operative in vivo. (Arterioscler Thromb. 1994;14:1040-1046.) |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://atvb.ahajournals.org/content/atvbaha/14/7/1040.full.pdf |
| Alternate Webpage(s) | http://atvb.ahajournals.org/content/atvbaha/14/7/1040.full.pdf?download=true |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
