Biochemical characterization of plasma membranes and intracellular membranes isolated from human platelets using Percoll gradients

Fauvel, Josette; Chap, Hugues; Roques, Véronique; Lévy-Toledano, S; Douste‐Blazy, Louis

doi:10.1016/0005-2736(86)90022-2

Cited by 57 publications

(48 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To rule out a possible involvement of protein kinase C, staurosporine, a potent protein kinase antagonist [36], was used, and did not antagonize the effect of PMA and OAG on Ca# + transport. In spite of the fact that PMA was shown to be antagonized by CsA in various cell lines [38,39], the activation of protein kinase C by PMA is not antagonized by CsA [39], suggesting that, if this drug is capable of modifying the effects produced by the diacylglycerol analogues, this does not occur via the protein kinase C pathway.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Uncoupling of Ca2+ transport ATPase in muscle and blood platelets by diacylglycerol analogues and cyclosporin A antagonism

1997

Biochemical Journal

View full text Add to dashboard Cite

The possibility that diacylglycerol analogues might have a wider spectrum of intracellular targets than the well-known protein kinase C was investigated with vesicles containing the Ca# + -ATPase derived from the dense tubular system in platelets and from the sarcoplasmic reticulum of skeletal muscle. The diacylglycerol analogues PMA and 1-oleoyl-2-acetyl-rac-glycerol (OAG) inhibited Ca# + accumulation by these vesicles, an effect that was antagonized by cyclosporin A. The inhibitory activity of PMA and OAG resulted from the uncoupling of the Ca# + -ATPase, characterized by a pronounced inhibition of Ca# + uptake accompanied by a discrete decrease in ATPase activity and by the inhibition of the enzyme's phosphorylation by P i , leading to both a decrease in ATP synthesis and an enhancement of Ca# +

show abstract

Section: Discussionmentioning

confidence: 99%

“…The effect of PMA does not seem to be mediated by protein kinase C, because the inhibition of Ca# + uptake by increasing concentrations of PMA was exactly the same in the presence and the absence of 0.25 mM staurosporine, a protein kinase C inhibitor [36].…”

Section: Figure 4 Correlation Between Ca 2 + Concentration and Pma Inmentioning

confidence: 92%

Uncoupling of Ca2+ transport ATPase in muscle and blood platelets by diacylglycerol analogues and cyclosporin A antagonism

1997

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Most of the N-terminal residues, including the first sulfatide-binding region, showed small or no significant perturbations (Ͻ0.04 ppm). To demonstrate that the observed spectral changes are not due to the slight change in DPC concentration and dilution of the Dab2 SBM sample, The platelet plasma membrane is similar in composition to that observed in other eukaryotic cells with phosphatidylcholine, sulfatides, and sphingomyelin found preferentially in the outer leaflet, whereas PtdSer and phosphatidylethanolamine are the most abundant lipids in the inner leaflet (35,36). Cholesterol is abundant in both layers with a molar ratio of cholesterol to phospholipid being about 0.5 (37).…”

Section: Dab2 Sbm Is the Minimal Functional Unit Of Dab2 N-ptb-mentioning

confidence: 99%

Structure, Sulfatide Binding Properties, and Inhibition of Platelet Aggregation by a Disabled-2 Protein-derived Peptide

Xiao

Charonko

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Binding of Dab2 to sulfatides results in platelet aggregation inhibition. Results: The structure of a Dab2-derived peptide (SBM) embedded in dodecylphosphocholine micelles, characterization of its minimal functional sulfatide-binding site, and its inhibitory platelet aggregation activity were determined. Conclusion: An amphipathic helical region of Dab2 SBM binds sulfatides, leading to platelet aggregation inhibition. Significance: Dab2 SBM may lead to the design of novel aggregatory inhibitors.

show abstract

“…Cell fractionation was performed by a method adapted from Fauvel et al (24). Washed platelets were prepared from one to two units of freshly obtained blood, resuspended in Buffer A (100 mM KCl͞25 mM Tris⅐HCl, pH 7.4͞3 mM ATP͞3 mM MgCl 2 ), and disrupted by nitrogen cavitation in a Parr bomb for 20 min at 70 atm (1 atm ϭ 101.3 kPa).…”

Section: Methodsmentioning

confidence: 99%

Eph kinases and ephrins support thrombus growth and stability by regulating integrin outside-in signaling in platelets

Prévost

Woulfe

Jiang

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

136

View full text Add to dashboard Cite

The ability of activated platelets to adhere to each other at sites of vascular injury depends on the integrin ␣IIb␤3. However, as aggregation continues, other signaling and adhesion molecules can contribute as well. We have previously shown that human platelets express on their surface the Eph receptor kinases EphA4 and EphB1 and the Eph kinase ligand ephrinB1. We now show that EphA4 is physically associated with ␣IIb␤3 in resting platelets, increases its surface expression when platelets are activated, and colocalizes with ␣IIb␤3 at sites of contact between platelets. We also show that Eph͞ephrin interactions can support the stable accumulation of platelets on collagen under flow and contribute to postengagement ''outside-in'' signaling through ␣IIb␤3 by stabilizing platelet aggregates and facilitating tyrosine phosphorylation of the ␤3 cytoplasmic domain. ␤3 phosphorylation allows myosin to bind to ␣IIb␤3 and clot retraction to occur. The data support a model in which the onset of aggregation permits Eph͞ephrin interactions to occur, after which signaling downstream from ephrinB1 and its receptors favors continued growth and stability of the thrombus by several mechanisms, including positive effects on outside-in signaling through ␣IIb␤3.

show abstract

Biochemical characterization of plasma membranes and intracellular membranes isolated from human platelets using Percoll gradients

Cited by 57 publications

References 42 publications

Uncoupling of Ca2+ transport ATPase in muscle and blood platelets by diacylglycerol analogues and cyclosporin A antagonism

Uncoupling of Ca2+ transport ATPase in muscle and blood platelets by diacylglycerol analogues and cyclosporin A antagonism

Structure, Sulfatide Binding Properties, and Inhibition of Platelet Aggregation by a Disabled-2 Protein-derived Peptide

Eph kinases and ephrins support thrombus growth and stability by regulating integrin outside-in signaling in platelets

Contact Info

Product

Resources

About