Specific Binding Sites on Human Blood Platelets for Plasma Lipoproteins

Koller, Elisabeth; Koller, Franz; Doleschel, W

doi:10.1515/bchm2.1982.363.1.395

Cited by 86 publications

(33 citation statements)

References 26 publications

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Section: 10mentioning

confidence: 99%

“…HDL 3 , the major HDL subfraction in blood, is known to interact with specific binding sites on platelets that appear to be identical with GP IIb/IIIa. [11][12][13][14] In human platelets, HDL 3 was also shown to activate cellular phospholipases, resulting in the formation of DAG. [15][16][17][18] The involvement of both phosphatidylcholine-specific phospholipase C and phosphatidylcholine-specific phospholipase D was postulated.…”

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HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

Nofer

Walter

Kehrel

et al. 1998

ATVB

131

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Abstract-We demonstrate that physiological concentrations of HDL 3 inhibit the thrombin-induced platelet fibrinogen binding and aggregation in a time-and concentration-dependent fashion. The underlying mechanism includes HDL 3 -mediated inhibition of phosphatidylinositol 4,5-bis-phosphate turnover, 1,2-diacylglycerol and inositol 1,4,5-tris-phosphate formation, and intracellular calcium mobilization. The inhibitory effects of HDL 3 on inositol 1,4,5-tris-phosphate formation and intracellular calcium mobilization were abolished after covalent modification of HDL 3 with dimethylsuberimidate. Furthermore, they could be blocked by calphostin C and bis-indolylmaleimide, 2 highly selective and structurally unrelated protein kinase C inhibitors. However, the inhibitory effects of HDL 3 were not blocked by H89, a protein kinase A inhibitor. In addition, HDL 3 failed to induce cAMP formation but stimulated the phosphorylation of the protein kinase C 40-to 47-kD major protein substrate. We observed a close temporal relationship between the HDL 3 -mediated inhibition of thrombininduced inositol 1,4,5-tris-phosphate formation, intracellular calcium mobilization, and fibrinogen binding and the phosphorylation of the protein kinase C 40-to 47-kD major protein substrate. Taken together, these findings indicate that the HDL 3 -mediated inhibition of thrombin-induced fibrinogen binding and aggregation occurs via inhibition of phosphatidylinositol 4,5-bis-phosphate turnover and formation of 1,2-diacylglycerol and inositol 1,4,5-tris-phosphate. Protein kinase C may be involved in this process. (Arterioscler Thromb Vasc Biol. 1998;18:861-869.)Key Words: high-density lipoprotein Ⅲ protein kinase C Ⅲ signal transduction Ⅲ platelet aggregation Ⅲ fibrinogen B oth HDL and platelets are intimately involved in the pathogenesis of atherosclerosis, thrombosis, and coronary heart disease.1-3 Numerous observations demonstrated a direct effect of HDL on platelet functions.4 Platelet hyperreactivity was noted in subjects with hypoalphalipoproteinemia.5 Decreased activation of platelets by strong agonists such as thrombin and collagen has been reported in the presence of physiological concentrations of HDL.6-8 Furthermore, HDL inhibited thromboxane A 2 liberation, and addition of HDL to clotting blood diminished platelet thromboxane A 2 formation capacity. 9,10The mechanism underlying the effects of HDL on platelet function is little understood. HDL 3 , the major HDL subfraction in blood, is known to interact with specific binding sites on platelets that appear to be identical with GP IIb/IIIa. [11][12][13][14] In human platelets, HDL 3 was also shown to activate cellular phospholipases, resulting in the formation of DAG.15-18 The involvement of both phosphatidylcholine-specific phospholipase C and phosphatidylcholine-specific phospholipase D was postulated. 16 -18 Recently, the PKC-dependent enhancement of the Na ϩ /H ϩ antiport in the presence of HDL 3 has been reported. 19Both HDL 3 -induced DAG formation and Na ϩ /H ϩ exchange stimulation w...

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Section: 10mentioning

confidence: 99%

mentioning

confidence: 99%

HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

Nofer

Walter

Kehrel

et al. 1998

ATVB

131

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“…The small influence of temperature on binding and the rapid association of binding are in good accordance with our previous results with 123 I-HDL3. 32 In this ex vivo comparison of binding parameters in healthy subjects and FH patients, in contrast to our previous study we used the whole-plasma HDL fraction (d= 1.063-1.21 g/ml) and modified the platelet isolation and washing procedures. Therefore, the quantitative values for K^ and the number of apparent binding sites differ from our values obtained with HDL3.…”

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confidence: 99%

Binding of 111In-labeled HDL to platelets from normolipemic volunteers and patients with heterozygous familial hypercholesterolemia.

Virgolini

Borggrefe

et al. 1992

Arterioscler Thromb

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High density lipoproteins (HDLs; d= 1.063-1.21 g/ml) were isolated by ultracentrifugation and radiolabeled with '"In. The in vitro binding onto platelets from healthy volunteers (it=15) and patients (n=36) with heterozygous familial hypercholesterolemia (FH) was investigated. Binding was saturable and indicated high-affinity binding sites, which bound 1,882±361 ng protein of '"In-HDL/lC platelets (dissociation constant [£ d

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“…The mechanism by which LDL can affect platelet behaviour could involve an alteration in the properties and/or composition of the membrane by the exchange of lipids or peroxidative damage [37-401. Since platelet-lipoprotein interaction does not involve divalent cations, it cannot be ruled out that the effects we find are mediated by LDL still attached to the platelets [41,42]. As an alternative to a direct platelet-lipoprotein interaction, it has been recently proposed that the control of the ploidy of the megakaryocyte may be altered in disease resulting in a change in the size distribution and reactivity of the population of platelets in the circulation [43].…”

Section: Discussionmentioning

confidence: 98%

Platelet transmembrane signalling responses to collagen in familial hypercholesterolaemia

Cooper

Tan

Betteridge

1994

Eur J Clin Investigation

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Abstract.Washed platelets from patients with familial hypercholesterolaemia (FH) were found to be more reactive towards collagen than those from control subjects. The dose required to achieve half maximum aggregation was found to be 0.6 ml-' for FH patients whilst that for control subjects was 1.25 pg ml-'. In both types of platelet, intracellular Ca2+ levels, as monitored by the Ca2+-dependent photoprotein, aequorin, rose on stimulation with collagen and then fell to basal levels, probably due to resequestration by the reticular system. This effect was not due to exhaustion of the supply of aequorin since sustained Ca2+ influx induced by the ionophore, A23 187, gave a stable signal that did not return to baseline. Similarly, inositol 1,4,5, trisphosphate levels increased in the cytosol after stimulation and then fell to unstimulated values. When stimulated with collagen, platelets from FH patients showed a greater extent of cytoplasmic calcium mobilization ( P < 0-05) when compared to controls, coupled with a greater extent of inositol phospholipid hydrolysis ( P < 0.05). At doses of collagen sufficient to give either 100% or 50% aggregation, platelets from patients or control subjects showed the same amplitude of ATP release at either dose suggesting that the trigger for vesicle release is more sensitive in FH.

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Specific Binding Sites on Human Blood Platelets for Plasma Lipoproteins

Cited by 86 publications

References 26 publications

HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

Binding of 111In-labeled HDL to platelets from normolipemic volunteers and patients with heterozygous familial hypercholesterolemia.

Platelet transmembrane signalling responses to collagen in familial hypercholesterolaemia

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Specific Binding Sites on Human Blood Platelets for Plasma Lipoproteins

Cited by 86 publications

References 26 publications

HDL3-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

HDL3-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

Binding of 111In-labeled HDL to platelets from normolipemic volunteers and patients with heterozygous familial hypercholesterolemia.

Platelet transmembrane signalling responses to collagen in familial hypercholesterolaemia

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HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate

HDL₃-Mediated Inhibition of Thrombin-Induced Platelet Aggregation and Fibrinogen Binding Occurs via Decreased Production of Phosphoinositide-Derived Second Messengers 1,2-Diacylglycerol and Inositol 1,4,5-tris-Phosphate