Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids.

Lecompte, M.F.; Bouix, G; Mann, Kenneth G.

doi:10.1016/s0021-9258(17)42112-0

Cited by 35 publications

(16 citation statements)

References 32 publications

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“…Electrochemical Measurements. Alternative current (ac) polarography was carried out as described previously (21), with the polarographic instrument already mentioned and in a Metrohm polarographic cell. A hanging mercury drop electrode (HMDE) was positioned in contact with the phospholipid monolayer; an Ag/AgCl saturated KCl electrode was the reference, and a platinum gauge was the auxiliary electrode.…”

Section: Methodsmentioning

confidence: 99%

“…We used alternative current (ac) polarography in order to investigate interactions between apoA-I and PL. It has the particular advantage of allowing discrimination between the modes of binding of a hydrosoluble protein at the PL polar headgroups-hydrocarbon chains interface, in terms of penetration or adsorption, as was shown in previous papers (21,22). We use this method under restricted conditions which allow the measurement of the differential capacity (dc) of the electrode in contact with a PL condensed monolayer.…”

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confidence: 98%

“…Such a system has potentialities of a biosensor. It has a high selectivity to the interaction between various PL and proteins with their different domains (21). This method has recently been used to show that the blood coagulation factor Va is engaged in both electrostatic and hydrophobic interactions with phospholipid monolayers, depending on bulk factor Va concentration (21).…”

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confidence: 99%

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Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

et al. 1998

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In whole HDL particles, the arrangement of apoA-I relative to phospholipids is of crucial interest with respect to the physiological formations of HDL. We report here new data concerning the nature of the interaction of apoA-I with condensed phospholipid (PL) monolayers (phosphatidylcholine and phosphatidylserine). The use of alternative current polarography allowed the detection for the first time of different binding steps which are dependent on apoA-I concentration. At low concentration (below 10 micrograms/mL), apoA-I adsorbs on PL polar headgroups, through electrostatic interactions. Above this threshold concentration, apoA-I penetrates within the monolayer (i.e., part of apoA-I crosses the PL polar headgroup/hydrocarbon chain interface). The process of penetration described here brings experimental evidence supporting Segrest's "snorkel" model. Penetrated helices are lying at the interface, their apolar face in contact with PL hydrocarbon chains and their polar face in contact with PL polar headgroups. In the absence of cholesterol, a second level of penetration was detected at higher apoA-I concentrations. It was facilitated in the presence of phosphatidylserine in comparison to phosphatidylcholine and disappeared in the presence of cholesterol. It is proposed that the C-terminal domain is involved in the first binding steps and that hinged domains may also be implicated. Furthermore, we propose that the apoA-I binding states stabilize the protein/phospholipid layer complex. These different binding states are discussed with respect to their roles in HDL metabolism.

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Section: Methodsmentioning

confidence: 99%

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Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

et al. 1998

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“…There has been much interest in studying the interfacial reactions of thiols/disulfides at noble metal electrode surfaces, such as gold, silver, and platinum as well as mercury. − It is generally found that thiols/disulfides adsorb very strongly to these metal surfaces and that the adsorption involves rather complicated surface reactions, mainly due to the fact that the sulfur functional groups readily react with these metal centers to form the corresponding, and energetically more stable, thiolate complexes. Such reactions enhance the adsorption of the molecules in turn, typifying the surface behavior of this group of molecules.…”

Section: Introductionmentioning

confidence: 99%

Reactions of Phospholipase A₂ at a Mercury Electrode Surface

Chen¹,

Abruña²

1997

J. Phys. Chem. B

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Cyclic voltammetric techniques (dc and ac) have been employed to probe the interfacial interaction of porcine pancreatic phospholipase A 2 (PLA 2 ) with mercury. A reaction mechanism based on the interaction of cystine residues (disulfide) with mercury is presented. It appears that the interfacial electrical properties play an important role in determining the surface behavior of adsorbed PLA 2 molecules. For instance, the predominant step of the electron transfer process is dependent on the electrode surface properties, including the surface concentration of PLA 2 and the fraction of free surface mercury sites. In addition, the local pH at the interface and interfacial buffer capacity were also found to be important factors in the surface reaction mechanism. Studies of the electron transfer kinetics showed that the transfer coefficient (R) was somewhat less than 0.50, and the rate constant (k) was of the order of 10 3 s -1 . From ac cyclic voltammetric studies it was determined that the adsorbed PLA 2 layer corresponded to a capacitor of about 6 µF/cm 2 and that the faradaic component of the interfacial capacitance was about 1 µF/cm 2 .

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“…The PtdSer recognition site of FVa and VIIIa is located in their N-terminal C2 domain [ 201 , 202 ]. The light chain and lipid interactions of FVa and FVIIIa involve electrostatic and hydrophobic binding [ 203 , 204 ]. Their light chains have the same domain homology, consisting of an A-type domain and two smaller C-type domains (Fig.…”

Section: Ptdser Involved In the Process Of Blood Coagulation And Anticoagulationmentioning

confidence: 99%

The role of phosphatidylserine on the membrane in immunity and blood coagulation

Wang

Zhuang

et al. 2022

Biomark Res

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The negatively charged aminophospholipid, phosphatidylserine (PtdSer), is located in the inner leaflet of the plasma membrane in normal cells, and may be exposed to the outer leaflet under some immune and blood coagulation processes. Meanwhile, Ptdser exposed to apoptotic cells can be recognized and eliminated by various immune cells, whereas on the surface of activated platelets Ptdser interacts with coagulation factors prompting enhanced production of thrombin which significantly facilitates blood coagulation. In the case where PtdSer fails in exposure or mistakenly occurs, there are occurrences of certain immunological and haematological diseases, such as the Scott syndrome and Systemic lupus erythematosus. Besides, viruses (e.g., Human Immunodeficiency Virus (HIV), Ebola virus (EBOV)) can invade host cells through binding the exposed PtdSer. Most recently, the Corona Virus Disease 2019 (COVID-19) has been similarly linked to PtdSer or its receptors. Therefore, it is essential to comprehensively understand PtdSer and its functional characteristics. Therefore, this review summarizes Ptdser, its eversion mechanism; interaction mechanism, particularly with its immune receptors and coagulation factors; recognition sites; and its function in immune and blood processes. This review illustrates the potential aspects for the underlying pathogenic mechanism of PtdSer-related diseases, and the discovery of new therapeutic strategies as well.

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Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids.

Cited by 35 publications

References 32 publications

Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

Reactions of Phospholipase A₂ at a Mercury Electrode Surface

The role of phosphatidylserine on the membrane in immunity and blood coagulation

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Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids.

Cited by 35 publications

References 32 publications

Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

Binding Steps of Apolipoprotein A-I with Phospholipid Monolayers: Adsorption and Penetration

Reactions of Phospholipase A2 at a Mercury Electrode Surface

The role of phosphatidylserine on the membrane in immunity and blood coagulation

Contact Info

Product

Resources

About

Reactions of Phospholipase A₂ at a Mercury Electrode Surface