In vitro effects of radiation on human retinoblastoma cells

2001 ◽  
Vol 96 (S1) ◽  
pp. 7 ◽  
Author(s):  
Mei Zhang ◽  
Graham Stevens ◽  
Michele C. Madigan
1990 ◽  
Vol 45 (3) ◽  
pp. 250-257 ◽  
Author(s):  
Sabine Griegel ◽  
Kerstin Heise ◽  
Andrea Kindler-Röhrborn ◽  
Manfred F. Rajewsky

2020 ◽  
Vol 12 (2) ◽  
pp. 178-183
Author(s):  
Dongju Qin ◽  
Xiamuxiya Ainiwaer ◽  
Huling Pan ◽  
Qian Sha ◽  
Xiaojuan Zhou

This study aimed to investigate the effect of bruceine D on the proliferation and apoptosis of human retinoblastoma cells and its effect on miR-155 expression. Y79 human retinoblastoma cells were cultured in vitro and randomly divided into the blank control group, DMSO (Dimethyl Sulphoxide) group, bruceine D 10 μmol/L group, bruceine D 20 μmol/L group, and bruceine D 40 μmol/L group. MTT assay was used to detect cell hyperplasia, flow cytometry to detect the apoptosis rate, and qRT-PCR to detect the expression level of miR-155. Anti-miR-155 or miR-155 mimics were transfected into Y79 cells, and hyperplasia and apoptosis rates were detected by the above methods. Western blotting was used to detect Bcl-2, Bax, and caspase-3 expression. Bruceine D can reduce the viability of Y79 cells (P < 0.05), significantly increase the apoptosis rate (P < 0.05), promote the expression of Bax and caspase-3 (P < 0.05), and inhibit miR-155 and Bcl-2 (P < 0.05). Compared with the anti-miR-con group, in the anti-miR-155 group, cell vigor was evidently reduced (P < 0.05), the apoptosis rate was evidently increased (P < 0.05), and the Bcl-2 level was reduced (P < 0.05). Bax and caspase-3 levels were evidently increased (P < 0.05). Transfection with miR-155 mimics can reduce the influence of caspase D-3 in hyperplasia and apoptosis of Y79 cells. Bruceine D may reduce the hyperplasia of human retinoblastoma cells and regulate cell apoptosis by downregulating miR-155 expression.


Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
HM Lee ◽  
TG Ahn ◽  
CW Kim ◽  
HJ An
Keyword(s):  

1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.


1989 ◽  
Vol 61 (02) ◽  
pp. 254-258 ◽  
Author(s):  
Margaret L Rand ◽  
Peter L Gross ◽  
Donna M Jakowec ◽  
Marian A Packham ◽  
J Fraser Mustard

SummaryEthanol, at physiologically tolerable concentrations, inhibits platelet responses to low concentrations of collagen or thrombin, but does not inhibit responses of washed rabbit platelets stimulated with high concentrations of ADP, collagen, or thrombin. However, when platelet responses to high concentrations of collagen or thrombin had been partially inhibited by prostacyclin (PGI2), ethanol had additional inhibitory effects on aggregation and secretion. These effects were also observed with aspirin- treated platelets stimulated with thrombin. Ethanol had no further inhibitory effect on aggregation of platelets stimulated with ADP, or the combination of ADP and epinephrine. Thus, the inhibitory effects of ethanol on platelet responses in the presence of PGI2 were very similar to its inhibitory effects in the absence of PGI2, when platelets were stimulated with lower concentrations of collagen or thrombin. Ethanol did not appear to exert its inhibitory effects by increasing cyclic AMP above basal levels and the additional inhibitory effects of ethanol in the presence of PGI2 did not appear to be brought about by further increases in platelet cyclic AMP levels.


1987 ◽  
Vol 58 (03) ◽  
pp. 921-926 ◽  
Author(s):  
E Seifried ◽  
P Tanswell

SummaryIn vitro, concentration-dependent effects of rt-PA on a range of coagulation and fibrinolytic assays in thawed plasma samples were investigated. In absence of a fibrinolytic inhibitor, 2 μg rt-PA/ml blood (3.4 μg/ml plasma) caused prolongation of clotting time assays and decreases of plasminogen (to 44% of the control value), fibrinogen (to 27%), α2-antiplasmin (to 5%), FV (to 67%), FVIII (to 41%) and FXIII (to 16%).Of three inhibitors tested, a specific polyclonal anti-rt-PA antibody prevented interferences in all fibrinolytic and most clotting assays. D-Phe-Pro-Arg-CH2Cl (PPACK) enabled correct assays of fibrinogen and fibrinolytic parameters but interfered with coagulometric assays dependent on endogenous thrombin generation. Aprotinin was suitable only for a restricted range of both assay types.Most in vitro effects were observed only with rt-PA plasma concentrations in excess of therapeutic values. Nevertheless it is concluded that for clinical application, collection of blood samples on either specific antibody or PPACK is essential for a correct assessment of in vivo effects of rt-PA on the haemostatic system in patients undergoing fibrinolytic therapy.


1963 ◽  
Vol 09 (01) ◽  
pp. 164-174 ◽  
Author(s):  
Albert R Pappenhagen ◽  
J. L Koppel ◽  
John H Olwin

SummaryData have been presented on the in vitro effects of human chylomicra, low-density human plasma lipoproteins, and partially purified preparations of various phospholipids on human plasma euglobulin lysis. Euglobulin lysis was found to be accelerated by preparations of mixed soybean phospholipids (aso-lectin), cephalin, phosphatidyl inositol, phophatidyl serine and phosphatidyl ethanolamine. In contrast, it was found to be inhibited by preparations of human chylomicra, low-density human plasma liproproteins and lecithin. Inhibition of euglobulin lysis produced by any of these three agents could be diminished or completely overcome by the simultaneous presence of suitable levels of any one of the accelerating agents. In all cases studied, both inhibitory and accelerating effects were observed to be concentration-dependent. Evidence has been obtained to suggest that in the case of the accelerating agents the observed increased rate of euglobulin lysis is not a direct effect on lysis itself, but rather is due to more complete precipitation of plasminogen in the presence of these substances. On the other hand, it appears that the inhibitory effects observed are not related to the extent of plasminogen precipitation, but are actually true inhibitions of euglobulin lysis. The possible clinical significance of some of these observations has been briefly discussed.


2007 ◽  
Vol 55 (S 1) ◽  
Author(s):  
SA Mohamed ◽  
M Misfeld ◽  
T Hanke ◽  
W Kuehnel ◽  
HH Sievers

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