Interaction of Human Blood Platelets with the 2′,3′-Dialdehyde derivatives of Adenosine Diphosphate and Adenosine Triphosphate

1977 ◽  
Vol 5 (1) ◽  
pp. 138-139 ◽  
Author(s):  
P. HELEN PEARCE ◽  
MICHAEL C. SCRUTTON
Keyword(s):  
Adenosine Triphosphate ◽  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Derivatives Of ◽  
Human Blood Platelets

scholarly journals The synthetic RGDS peptide inhibits the binding of fibrinogen lacking intact alpha chain carboxyterminal sequences to human blood platelets

Blood ◽  
1987 ◽  
Vol 69 (3) ◽  
pp. 950-952 ◽  
Author(s):  
EI Peerschke ◽  
DK Galanakis
Keyword(s):  
Platelet Aggregation ◽  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Competitive Inhibitor ◽  
Minor Role ◽  
Solution Ph ◽  
Alpha Chain ◽  
A Minor ◽  
Human Blood Platelets

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).

The Use of a Chelating Ion-Exchange Resin to Evaluate the Effects of the Extracellular Calcium Concentration on Adenosine Diphosphate Induced Aggregation of Human Blood Platelets

1976 ◽  
Vol 36 (01) ◽  
pp. 208-220 ◽  
Author(s):  
Stanley Heptinstall
Keyword(s):  
Platelet Aggregation ◽  
Ion Exchange ◽  
Human Blood ◽  
Calcium Concentration ◽  
Exchange Resin ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Ion Exchange Resin ◽  
Extracellular Calcium ◽  
Human Blood Platelets

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.

Effects of Aggregating Agents, Cytochalasin B (CB) and Neuraminidase (N) on the Ultrastructure of Freeze Dried (FD) Human blood Platelets

1975 ◽  
Author(s):  
R. B. Davis
Keyword(s):  
Human Blood ◽  
Plasma Membranes ◽  
Platelet Rich Plasma ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Surface Complexes ◽  
Release Reaction ◽  
Cryoprotective Agents ◽  
Freeze Dried ◽  
Human Blood Platelets

Frozen and freeze dried human blood platelets remain intact morphologically when preserved by cryoprotective agents. These studies have investigated effects of 1) the release reaction, 2) discoid stabilization by CB, and 3) N on platelet morphology in FD specimens. Platelets were collected in 1/10 volume of acid citrate and platelet rich plasma (PRP) obtained by centrifugation. Aggregating agents (adenosine diphosphate, 2 × 10-6 M, epinephrine, 5 × 10-5 M, collagen, 30 μg/ml, thrombin 0.2 U/ml) CB (25 μg/ml), trypsin (3 mgs/ml), and N (20 U/ml), then cryoprotective agents, were added. Platelets were FD and the ultrastructure examined. Aggregating agents were associated with 1 ) the appearance of amorphous electron dense material within platelets extending via channels to the exterior; 2) membranous complexes contiguous to plasma membranes; 3) numerous organelles adjacent to the plasma membrane. Platelets in artificial thrombi also showed homogeneous electron opaque areas and membrane rich surface complexes. CB caused vacuolization and previously reported concentric membranous structures were noted in trypsinized platelets. N did not prevent interplatelet bridging. In conclusion, aggregated FD platelets differ from platelets fixed by traditional means, providing morphologic support that platelet organelles and membrane systems relate structurally to the platelet exterior as well as the canalicular system to provide a catalytic lipoprotein surface during the release reaction.

Adenosine Diphosphate in Red Cells as a Factor in the Adhesiveness of Human Blood Platelets

Nature ◽  
1961 ◽  
Vol 192 (4802) ◽  
pp. 531-532 ◽  
Author(s):  
A. GAARDER ◽  
J. JONSEN ◽  
S. LALAND ◽  
A. HELLEM ◽  
P. A. OWREN
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Red Cells ◽  
Human Blood Platelets

scholarly journals The synthetic RGDS peptide inhibits the binding of fibrinogen lacking intact alpha chain carboxyterminal sequences to human blood platelets

Blood ◽  
1987 ◽  
Vol 69 (3) ◽  
pp. 950-952
Author(s):  
EI Peerschke ◽  
DK Galanakis
Keyword(s):  
Platelet Aggregation ◽  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Competitive Inhibitor ◽  
Minor Role ◽  
Solution Ph ◽  
Alpha Chain ◽  
A Minor ◽  
Human Blood Platelets

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).

Effect of Dextran infusion on the Adenosine Diphosphate Induced Adhesiveness and the Spreading Capacity of Human Blood Platelets

1966 ◽  
Vol 15 (03/04) ◽  
pp. 451-456 ◽  
Author(s):  
S Bygdeman ◽  
R Eliasson ◽  
B Gullbring
Keyword(s):  
Human Blood ◽  
Normal Saline ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Platelet Adhesiveness ◽  
Dextran 70 ◽  
Platelet Spreading ◽  
Induced Changes ◽  
Plasma Factors ◽  
Human Blood Platelets

SummaryThe adenosine diphosphate induced platelet adhesiveness to glass and the platelet spreading capacity on a siliconized glass surface have been studied in 8 hypovolemic subjects after infusion of 500 ml 6% solution of dextran 70 (Macrodex®) or 500 ml normal saline. Infusion of dextran caused a significant decrease in platelet adhesiveness compared with the controls while no effect was noted on the spreading capacity.It is proposed that the observed effect on platelet adhesiveness is due to dextran induced changes in the activity of plasma factors involved in the mechanisms leading to platelet adhesiveness.

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