Effects of ethanol and of other factors on ADP-induced aggregation of human blood platelets in vitro

1980 ◽  
Vol 20 (4) ◽  
pp. 405-415 ◽  
Author(s):  
Ronald P. Quintana ◽  
Andrew Lasslo ◽  
Marion Dugdale ◽  
Lisa L. Goodin ◽  
Eric F. Burkhardt
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.


1980 ◽  
Vol 239 (4) ◽  
pp. H483-H483
Author(s):  
N. E. Owen ◽  
H. Feinberg ◽  
G. C. Le Breton

Human blood platelets isolated by albumin density gradient centrifugation take up Ca2+ during 10-6M epinephrine-induced primary aggregation but not during 10-6 M ADP-induced primary aggregation. Platelet uptake of Ca2+ is dose-dependent over a range of 10-7) to 10-5 M epinephrine. Antagonism of the platelet α-receptor by phentolamine (10-6 M) results in inhibition of both epinephrine-stimulated Ca2+ uptake and aggregation. The Ca2+ antagonist verapamil (50 μM) blocks Ca2+ uptake and epinephrine-induced aggregation, but not ADP-induced aggregation. The verapamil inhibition of aggregation is reduced on Ca2+ addition. These results suggest that epinephrine acts to stimulate primary platelet aggregation through a specific receptor interaction that results in a selective increase in platelet membrane permeability to Ca2+.


Vox Sanguinis ◽  
1957 ◽  
Vol 2 (2) ◽  
pp. 104-109 ◽  
Author(s):  
S. ROTHMAN ◽  
E. ADELSON ◽  
A. SCHWEBEL ◽  
R. D. LANGDELL

1974 ◽  
Vol 32 (02/03) ◽  
pp. 391-404
Author(s):  
M. R Hardeman ◽  
Carina J. L. Heynens

SummaryThe present paper is part of a study on the evaluation of the active serotonin uptake and the response to hypotonic shock as in vitro viability tests for human blood platelets.The extraction and fluorometric assay of serotonin in plasma and in platelets were further automated by the introduction of a dialyzer in the earlier described system. Furthermore, the influences of some external factors on both tests were investigated.The serotonin uptake as well as the hypotonic shock response were pH dependent and especially the latter was rather sensitive to small pH changes. Changes in the Na+ : K+ ratio were also found to influence both criteria significantly.The serotonin uptake appeared to be linearly dependent on the platelet number while, within a range of 200 X 103 - 450 X 103 platelets per fxl, the slope of the hypotonic shock response was the same.


1985 ◽  
Vol 54 (02) ◽  
pp. 397-401 ◽  
Author(s):  
Johannes Nimpf ◽  
Helmut Wurm ◽  
Gerhard M Kostner

SummaryThe interaction of β2-glycoprotein-I (β2-G-I), a plasma constituent of unknown function, with blood platelets was studied. The following results were obtained: 1) β2-G-I binds to washed human platelets isolated by centrifugation (WP) at one kind of specific, saturable binding sites. The dissociation constant was found to be approx. 1 × 10−6M.2) In the presence of physiological concentrations of Ca++ (2.5 mM), this specific binding is markedly reduced. Unspecific binding of β2-G-I to platelets, however, is not influenced by Ca++.3) Platelets prepared by gel filtration (GFP), differing in their in vitro aggregability from WP, exhibit no specific binding of β2-G-I. Binding to GFP is also not induced by activation with thrombin, collagen or ADP.4) β2-G-I causes significant alteration of the ADP-induced aggregation of GFP. Aggregation induced by thrombin, collagen, arachidonic acid or PAF-acether, however is not altered by β2G-I.It is suggested, that pelleting during centrifugation causes irreversible rearrangements in the membrane of platelets.


1992 ◽  
Vol 281 (2) ◽  
pp. 309-316 ◽  
Author(s):  
M Croset ◽  
Y Bayon ◽  
M Lagarde

Mass changes in the incorporation of linoleic (C18:2), eicosapentaenoic (C20:5) and docosahexaenoic (C22:6) acids in human blood platelet phospholipids were induced by incubating the cells and these fatty acids complexed to albumin. The remodelling of [14C]C18:2, [14C]C20:5 and [14C]C22:6 in classes, subclasses and molecular species of platelet phospholipids was studied in resting and thrombin-stimulated cells. More than 85% of the incorporation was located in phospholipids, representing 5-fold and 2.5-fold increases in the phospholipid C20:5 and C22:6 endogenous content respectively. Thrombin stimulation induced a 30% degradation of 1-acyl-2-C20:5-glycerophosphocholine (GPC) and 1-acyl-2-C22:6-GPC, but did not induce significant release of C18:2 from 1-acyl-2-C18:2-GPC. There was no change in the [14C]fatty acid composition of 1-alkyl-2-acyl-GPC. Thrombin-dependent increases in 1-alkenyl-2-C20:5-glycerophosphoethanolamine (GPE) and 1-alkenyl-2-C22:6-GPE of 2.1-fold and 2.5-fold respectively accounted for the rise in GPE radioactivity and partly compensated for the loss of these fatty acids from 1,2-diacyl-GPC: transfer to 1-alkenyl-2-acyl-GPE was 0.4 and 1.5 nmol/10(9) platelets for C20:5 and C22:6 respectively. [14C]C20:5 and [14C]C22:6 were incorporated into six different species of 1,2-diacyl-GPC, with acylation in the major endogenous forms (C18:1 +C16:0 and C18:0 species) representing 76% and 66% respectively of the total radioactivity present in 1,2-diacyl-GPC. Stimulation by thrombin induced significant release of these fatty acids from the main molecular species of 1,2-diacyl-GPC, but significantly stimulated the synthesis of alkenyl forms of GPE containing C18:1/C22:6 +C16:0/C22:6, C18:0/C22:6 and C18:0/C20:5. C18:0/C18:2, the major endogenous C18:2 molecular species, represented only 10.5% of the incorporation; none of the [14C]C18:2 molecular species was a substrate for transfer towards 1-alkenyl-2-acyl-GPE. It is concluded that when C20:5 and C22:6, but not C18:2, are acylated in 1,2-diacyl-GPC, they participate in thrombin-dependent phospholipid remodelling, and might compete with the turnover and release of arachidonic acid from platelet phospholipids and the subsequent activation of the cells.


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