Inhibition of platelet aggregation byS-nitroso-cysteine via cGMP-independent mechanisms: evidence of inhibition of thromboxane A2synthesis in human blood platelets

FEBS Letters ◽  
1999 ◽  
Vol 442 (2-3) ◽  
pp. 162-166 ◽  
Author(s):  
Dimitrios Tsikas ◽  
Milos Ikic ◽  
Kathrin S. Tewes ◽  
Manfred Raida ◽  
Jürgen C. Frölich
Blood ◽  
1986 ◽  
Vol 67 (3) ◽  
pp. 672-675 ◽  
Author(s):  
GA Adams ◽  
SD Swenson ◽  
G Rock

Abstract Human blood platelets were stored for five days as concentrates in 60 mL of: (a) plasma; (b) non-plasma medium with anticoagulant; and (c) non-plasma medium without anticoagulant. All preparations were equally functional when tested for platelet aggregation and release reaction in response to single agonist or synergistic pairs of agonists in vitro. Platelets stored in non-plasma medium with anti-coagulant had lower kallikrein, fibrino(gen)peptide A, lactate, and beta-thromboglobulin than did plasma controls after five days. In vivo recovery and survival of platelets stored in non-plasma medium with anticoagulant were 51.2% +/- 4.3% and 8.7 +/- 0.3 days, respectively, which were not statistically different from plasma controls of 39.2% +/- 4.9% and 7.2 +/- 0.8 days, respectively. It is concluded that platelets can be stored for five days in a non-plasma medium and still have good in vivo recoveries and survivals.


Blood ◽  
1987 ◽  
Vol 69 (3) ◽  
pp. 950-952 ◽  
Author(s):  
EI Peerschke ◽  
DK Galanakis

Abstract The alpha chain 572–574 Arg-Gly-Asp sequence of fibrinogen appears to play only a minor role in platelet aggregation based on the ability of fibrinogen preparations lacking alpha chain carboxyterminal segments to support platelet aggregation, but synthetic Arg-Gly-Asp-Ser (RGDS) peptides are capable of inhibiting platelet aggregation and fibrinogen binding. The present study thus examined the ability of RGDS peptides to inhibit platelet interactions with a plasmic degradation product of fibrinogen (8D–50) that resembles an intermediate fragment X. Gel- filtered, human blood platelets suspended in 0.01 mol/L HEPES-buffered modified Tyrode's solution, pH 7.5, were stimulated with 20 mumol/L adenosine diphosphate and the binding of 125I-labeled 8D–50 or intact fibrinogen (0.01 to 0.6 mg/mL) assessed in the presence of 0 to 117 mumol/L RGDS. The data revealed that RGDS decreased the apparent affinity of 8D–50 and intact fibrinogen for platelets but did not affect the maximum number of binding sites. RGDS thus appears to be a competitive inhibitor not only of intact fibrinogen (Ki = 12 +/- 2 mumol/L) but also of 8D–50 (Ki = 15 +/- 3 mumol/L) (mean +/- SD, n = 3).


1976 ◽  
Vol 36 (01) ◽  
pp. 208-220 ◽  
Author(s):  
Stanley Heptinstall

Summary1. An ion-exchange resin, Chelex 100, has been used to prepare suspensions of human blood platelets in calcium and magnesium depleted plasma.2. Extracellular calcium is required for platelet aggregation when induced by adenosine diphosphate (ADP). Magnesium only supports aggregation provided that a small amount of calcium is present in the plasma.3. The extent of platelet aggregation depends upon the concentration of calcium in the plasma. There is an optimum concentration of calcium with which the maximum amount of aggregation is obtained in response to any single concentration of ADP. This optimum calcium concentration is below the physiological level. Higher calcium concentrations reduce the extent of aggregation by enhancing the rate of disaggregation and high magnesium concentrations have the same effect. It is possible that free ADP levels are reduced as a result of ADP-divalent cation complex formation.4. Platelets were found to contain 18.6 (S.D. ±1.1) × 10–6 mol Ca and 9.3 (S.D. ±1.0) × 10–6 mol Mg per 1011 cells.


1976 ◽  
Vol 193 (1112) ◽  
pp. 307-311 ◽  

Aggregation of human blood platelets induced by ADP was strongly inhibited by 2-azidoadenosine, a photolysable analogue of adenosine. The deamination of adenosine by adenosine deaminase (E. C. 3.5.4.4) was competitively inhibited by 2-azidoadenosine. In the presence of 2-azidoadenosine the enzyme was inactivated by u. v. radiation. The inactivation was diminished in the presence of a protein scavanger.


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