Specific Binding Sites on Human Blood Platelets for Plasma Lipoproteins

1982 ◽  
Vol 363 (1) ◽  
pp. 395-406 ◽  
Author(s):  
Elisabeth KOLLER ◽  
Franz KOLLER ◽  
Walter DOLESCHEL
1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.


1975 ◽  
Vol 150 (1) ◽  
pp. 129-132 ◽  
Author(s):  
A H Drummond ◽  
J L Gordon

5-Hydroxytryptamine changes the shape of rat blood platelets by combination with a cinanserin-sensitive receptor which is not associated with the active uptake of 5-hydroxytryptamine. Binding of 5-hydroxy[3H]tryptamine to platelets at 4°C demonstrates the presence of three saturable sites, and the highest-affinity site is apparently this 5-hydroxytryptamine receptor.


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.


1989 ◽  
Vol 53 (2) ◽  
pp. 181-190 ◽  
Author(s):  
Ernst Malle ◽  
Anni Gries ◽  
Gerhard M. Kostner ◽  
K. Pfeiffer ◽  
Johannes Nimpf ◽  
...  

1975 ◽  
Vol 152 (3) ◽  
pp. 433.b1-433.b1
Author(s):  
A H Drummond ◽  
J L Gordon

Life Sciences ◽  
1986 ◽  
Vol 39 (20) ◽  
pp. 1885-1891 ◽  
Author(s):  
M. Del Zompo ◽  
F. Bernardi ◽  
U. Bonuccelli ◽  
R. Maggio ◽  
M. Bajorek ◽  
...  

1980 ◽  
Vol 106 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Byung K. Kim ◽  
Manfred Steiner ◽  
Mario G. Baldini

Sign in / Sign up

Export Citation Format

Share Document