Wyniki wyszukiwania

1

ATP-dependent phosphatidylserine formation in animal cells as a base exchange reaction

100%

Czarny M., Sabala P., Baranska J.

Acta Biochimica Polonica

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1993

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tom 40

|

nr 3

2

No increase of phosphatidylserine exposure accompanying the increased membrane fluidity in erythrocytes of ataxia telangiectasia gene [ATM] carriers

100%

Rybczynska M., Kaczmarek J., Pawlak A. L.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 2

3

Homing of annexin-labeled stem cells to apoptopic cells

75%

Gerasimou A., Ramella R., Brero A., Boero O., Sheiban I., Levi R., Gallo M. P.

Cellular and Molecular Biology Letters

|

2009

|

tom 14

|

nr 1

100-112

Ischemic diseases are characterized by the presence of pro-apoptotic stimuli, which initiate a cascade of processes that lead to cell injury and death. Several molecules and events represent detectable indicators of the different stages of apoptosis. Among these indicators is phosphatidylserine (PS) translocation from the inner to the outer leaflet of the plasma membrane, which can be detected by annexinV (ANXA5) conjugation. This is a widely used in vivo and in vitro assay marking the early stages of apoptosis. We report here on an original method that employs PS-ANXA5 conjugation to target stem cells to apoptotic cells. Mesenchymal stem cells (MSCs) from GFP-positive transgenic rats were biotinylated on membrane surfaces with sulfosuccinimidyl-6-(biotinamido) hexanoate (sulfo-NHS-LC-biot) and then bound to avidin. The avidin-biotinylated MSCs were labeled with biotin conjugated ANXA5. Bovine aortic endothelial cells (BAE-1 cells) were exposed to UVC to induce caspasedependent apoptosis. Finally, we tested the ability of ANXA5-labeled MSCs to bind BAE-1 apoptotic cells: suspended ANXA5-labeled MSCs were seeded for 1 hour on a monolayer of UV-treated or control BAE-1 cells. After washing, the number of MSCs bound to BAE-1 cells was evaluated by confocal microscopy. Statistical analysis demonstrated a significant increase in the number of MSCs tagged to apoptotic BAE-1 cells. Therefore, stem cell ANXA5 tagging via biotin-avidin bridges could be a straightforward method of improving homing to apoptotic tissues.

4

Involvement of Naplus-Hplus exchanger in desmopressin-induced platelet procoagulant response

75%

Tomasiak M. M., Stelmach H., Bodzenta-Lukaszyk A., Tomasiak M.

Acta Biochimica Polonica

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2004

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tom 51

|

nr 3

Desmopressin (DDAVP) action on platelets is associated with the development of procoagulant response but the underlying mechanism of this phenomenon is not known. We investigated whether this effect of DDAVP might be due to activation of plasma membrane Na+ /H+ exchanger. The DDAVP-induced platelet procoagulant response, measured as phospholipid-dependent thrombin generation, was dose dependent and significantly weaker than that produced by collagen or monensin (mimics Na+ /H+ antiport). Both the DDAVP- and collagen-produced procoagulant responses were less pronounced in the presence of EIPA, an Na+/H+ exchanger inhibitor. Flow cytometry studies revealed that in vitro treatment of platelets with DDAVP or collagen was associated with the appearance of both degranulated (and fragmented) and swollen cells. The DDAVP-evoked rise in size and granularity heterogeneity was similar to that produced by collagen or monensin and was not observed in the presence of EIPA. Using flow cytometry and annexin V-FITC as a probe for phosphatidylserine (PS) we demonstrated increased and uniform binding of this marker to all subsets of DDAVP-treated platelet population. The DDAVP-evoked PS expression was dose dependent, strongly reduced by EIPA and weaker than that caused by monensin or collagen. As judged by optical swelling assay, DDAVP in a dose dependent manner produced a rise in platelet volume. The swelling was inhibited by EIPA and its kinetics was similar to that observed in the presence of monensin. Electronic cell-sizing measurements showed an increase in mean platelet volume and a decrease in platelet count and platelet crit upon treatment with DDAVP. DDAVP elicited a slow (much slower than collagen) alkalinization of platelet cytosol. Altogether the data indicate an involvement of Na+/H+ exchanger in the generation of procoagulant activity in DDAVP-treated platelets.

5

Annexin VI, a novel ATP-dependent, phospholipid-binding protein

75%

Danieluk M., Sikorski A. F., Pikula S., Bandorowicz-Pikula J.

Cellular and Molecular Biology Letters

|

1999

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tom 04

|

nr 4

The determination of surface pressure (π) of a phosphatidylserine (PS) monolayer is used to study the interactions between specific phospholipid classes and various proteins. In the present study we show that ATP, but not ADP, in milimolar concentration ranges stimulate the increase of Δπ in a PS monolayer evoked by annexin VI (AnxVI)/Ca2+ at a moderate initial π (~11 mN/m). The obtained results are consistent with ATP being a functional ligand for AnxVI. To further study the ATP binding site of AnxVI, we have used fluorescein 5’-isothiocyanate (FITC). This is useful in the characterization of nucleotide-binding sites of many membrane integral and cytosolic proteins. Under our experimental conditions FITC did not affect the binding of AnxVI to membranes but abolished the interaction of the protein with ATP insolubilized on agarose. This observation can be interpreted in terms of AnxVI possessing an ATP-binding site functionally similar to nucleotide-binding domains characterized in other ATP-dependent proteins. We also provide evidence that two AnxVI isoforms are expressed constitutively in porcine liver differ from each other in respect to their ATP binding properties.

6

Sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate modulate phosphatidylserine homeostasis in glioma C6 cells

75%

Wojcik M., Baranska J.

Acta Biochimica Polonica

|

1999

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tom 46

|

nr 1

The effect of sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate on L-[U-14C]serine incorporation into phosphatidylserine and phosphatidylserine-derived phosphatidylethanolamine was investigated in intact glioma C6 cells. Sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate are potent signalling molecules which, due to their physicochemical features, may function as amphiphilic compounds. It has been found that sphingosine and sphingosylphosphorylcholine (amphiphilic cations) significantly increase [14C]phosphatidylserine synthesis and decrease the amount of 14C-labeled phosphatidylethanolamine. Sphingosine 1-phosphate (an amphiphilic anion) was without effect on phosphatidylserine synthesis but, similarly as sphingosine and sphingosylphosphorylcholine, reduced the conversion of phosphatidylserine to phosphatidylethanolamine. These results strongly suggest that sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate can modulate cellular phospholipid homeostasis by stimulation of phosphatidylserine synthesis and an interference with phosphatidylserine decarboxylase.

7

Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine

75%

Terlecki G., Gutowicz J.

Cellular and Molecular Biology Letters

|

2002

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tom 07

|

nr 3

Lactate dehydrogenase (LDH) is one of the glycolytic enzymes, which have been proved to have the capability to reverse non-specific adsorption on cellular membranous structures in vitro, as well as on the structural proteins of the contractile system of muscle cells. It has been suggested that this binding may play a physiological role, as it alters the enzyme’s kinetic properties. Our previous studies on this enzyme showed that its interaction with some anionic phospholipids reveals similar characteristics and similar effect on the activity of the enzyme to those wich had been observed for the interaction with membranous structures. Disruption of the lipid bilayers by nonionic detergent (Tween 20) restored the enzyme activity inhibited by the presence of phosphatidylserine (PS) liposomes. In this study, we used the measurement of enzyme tryptophanyl fluorescence spectra to monitor the interaction and possible changes in the enzyme conformation. The investigation provided further evidence of the importance of the bilayer structure in this interaction. Similarly to the effect on the activity of the enzyme, the addition of Tween 20 diminishes the quenching of the LDH tryptophanyl ﬂuorescence, and finally completely restores the fluorescence.

8

Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decarboxylase

63%

Dygas A., Zborowski J.

Acta Biochimica Polonica

|

1989

|

tom 36

|

nr 2

9

Participation of leukotriene C4 in the regulation of suicidal erythrocyte death

63%

Foller M., Mahmud H., Gu S., Wang K., Floride E., Kucherenko Y., Luik S., Laufer S., Lang F.

Journal of Physiology and Pharmacology

|

2009

|

tom 60

|

nr 3

135-143

Eryptosis, the suicidal death of erythrocytes, is characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine exposure at the erythrocyte surface. Eryptosis is triggered by increase in cytosolic Ca2+ concentration upon energy depletion. The present study explored the involvement of leukotrienes. Western blotting was employed to detect the cysteinyl-leukotriene receptor cysLT1, competitive immune assay to determine leukotriene release from erythrocytes, Fluo3 fluorescence to estimate cytosolic Ca2+ concentration, forward scatter to analyse cell volume and annexin V-binding to disclose phosphatidylserine exposure. As a result, erythrocytes expressed the leukotriene receptor CysLT1. Glucose depletion (24 hours) significantly increased the formation of the cysteinyl-leukotrienes C4/D4/E4. Leukotriene C4 (10 nM) increased Ca2+ entry, decreased forward scatter, activated caspases 3 and 8, and stimulated annexin V-binding. Glucose depletion similarly increased annexin V-binding, an effect significantly blunted in the presence of the leukotriene receptor antagonist cinalukast (1 µM) or the 5-lipoxygenase inhibitor BW B70C (1 µM). In conclusion, upon energy depletion erythrocytes form leukotrienes, which in turn activate cation channels, leading to Ca2+ entry, cell shrinkage and cell membrane scrambling. Cysteinyl-leukotrienes thus participate in the signaling of eryptosis during energy depletion.

10

Transmembrane segment M2 of glycine receptor as a model system for the pore-forming structure of ion channels

63%

Bednarczyk P., Szewczyk A., Dolowy K.

Acta Biochimica Polonica

|

2002

|

tom 49

|

nr 4

The glycine receptor belongs to the ligand-gated ion channel superfamily. It is a chloride conducting channel composed of four transmembrane domains. It was previously shown that the second transmembrane domain (M2) of the glycine receptor forms an ion conduction pathway throught lipid bilayers. The amino-acid sequence of the transmembrane segment M2 of the glycine receptor has a high homology to all receptors of the ligand-gated ion channel superfamily. In our report, we have used a synthetic M2 peptide. It was incorporated into a planar membrane of known lipid composition and currents induced by M2 were measured by the Black Lipid Membrane technique. When the planar lipid bilayer was composed of 75% phosphatidylethanolamine and 25% phosphatidylserine, the reversal potential measured in a 150/600 mM KCl (cis/trans) gradient was -19 mV suggesting that the examined pore was preferential to anions, Pk/Pci = 0.25. In contrast, when 75% phosphatidylserine and 25% phosphatidylethanolamine was used, the reversal potential was +20 mV and the pore was preferential to cations, Pk/Pci = 4.36. Single-channel currents were recorded with two predominant amplitudes corresponding to the main-conductance and sub-conductance states. Both conductance states (about 12 pS and 30 pS) were measured in a symmetric solution of 50 mM KCl. The observed single-channel properties suggest that the selectivity and conductance of the pore formed by the M2 peptide of the glycine receptor depend on the lipid composition of the planar bilayer.

11

The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies

63%

Terlecki G., Czapinska E., Gutowicz J.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr 3

Lactate dehydrogenase is one of the enzymes of the glycolytic path. It has been shown to be able to bind in vitro to cellular membranes. The presence of anionic phospholipids induces changes in the catalytic properties of the enzyme similar to those found when the enzyme is bound to natural membranes. In this study, a nonionic detergent (Tween 20), at concentrations not affecting the catalytic activity of LDH, was used to study the role of the lipid supra-molecular structure in the interaction between pig skeletal muscle lactate dehydrogenase and phosphatidylserine. Tween 20 changes the equilibrium of concentrations between the lipid supra-molecular forms. The detergent at the used concentration values did not alter the activity of the enzyme when it was used on its own, but did diminish the level of inhibition induced by the studied phospholipid. The obtained results showed that the interaction is reversible and that the bilayer structure of the lipid is essential for the inhibition.

12

Interaction of spectrin with phospholipids is inhibited by isolated erythrocyte ankyrin. A monolayer study

63%

Bialkowska K., Lesniewski J., Nietubyc M., Sikorski A. F.

Cellular and Molecular Biology Letters

|

1999

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tom 04

|

nr 2

It was previously found (Białkowska, K., Zembroń, A. and Sikorski, A. F. (1994) Biochim. Biophys. Acta 1191, 21-26.) that isolated erythrocyte ankyrin inhibited interaction of spectrin with phospholipid liposomes, mainly those prepared from lipid mixtures containing aminophospholipids. In this communication we report on the effect of isolated ankyrin on red blood cell spectrin interaction with phospholipids in monolayers. Our data indicate that spectrin interaction with monolayers containing PE and, to a smaller extent, PS is sensitive to inhibition by ankyrin while interaction with monolayers containing only PC is not. Tetrameric spectrin affects monolayer surface pressure similarly to the heterodimer. However, an interaction of tetrameric spectrin with phospholipids was much more effectively inhibited by purified ankyrin indicating that one site per spectrin tetramer engaged in this interaction. When interactions of purified individual spectrin subunits (α or β) with phospholipid monolayers was studied, the β-subunit caused a strong, saturable effect on the surface pressure of the PE/PC monolayer, in contrast to the α-chain which induced much smaller and monotonic changes on the surface pressure of the same monolayer. Also interactions of the β-subunit with amino-phospholipids/PC monolayers were more sensitive to inhibition by ankyrin than those with native αβ-heterodimer of spectrin, e.g. threefold lower concentration of ankyrin was necessary to induce the same effect, while interaction of the α-subunit with phospholipid monolayers was entirely insensitive to ankyrin. Phosphorylation of spectrin in vitro with either cAMP-dependent protein kinase, or metabolically in intact cells, induced a decrease in the effect of either dimer or tetramer on the surface pressure of phospholipid monolayers. The sensitivity of this interaction to ankyrin was also greatly diminished. When isolated ankyrin was phosphorylated by the same cAMP-dependent protein kinase its ability to compete with phospholipid for spectrin was also diminished. The described effects may indicate a physiological significance of spectrin’s interaction with phospholipids, particularly in situations when there is not enough functional ankyrin to accommodate all spectrin molecules in the membrane.

13

Interactions of spectrins with phospholipids: possible physiological role

63%

Sikorski A. F.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 2

14

Interactions of annexins IV and VI with erythrocyte membrane in the presence of Ca2. A biochemical and electron microscopy study

63%

Bandorowicz-Pikula J., Sobota A.

Cellular and Molecular Biology Letters

|

1996

|

tom 01

|

nr 1

Annexins IV and VI were found to interact with human erythrocyte membrane in a calcium-dependent manner. Chemical and enzymatic modification of the membrane constituents pointed to phosphatidylserine as a target membrane molecule responsible for the interaction of the annexin/Ca complexes with the membrane. The membrane-associated annexins were shown to form clusters reflecting, perhaps, the presence of PS microdomains in a lateral plane of membrane.

15

Reconstitution of flippase activity into liposomes

63%

Devaux P. F.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr 2

16

Interaction of annexin VI with membranes. Regulation by ATP in vitro

63%

Bandorowicz-Pikula J., Danieluk M., Wrzosek A., Bus R., Pikula S.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 4

Porcine liver annexin VI (AnxVI) has recently been described to bind in vitro ATP. The binding of nucleotide to protein is accompanied by modulation of AnxVI function, such as its' interaction with F-actin and membranes. In the present report, we show that ATP modulates AnxVI-driven aggregation of phosphatidylserine (PS) liposomes. In addition, we provide evidence using circular dichroism (CD) that the interaction of AnxVI with ATP evokes changes in secondary structure of the protein. The functional implications of these changes are also discussed.

17

Plasma membrane translocation of phosphatidylserine in human spermatozoa

63%

Kotwicka M., Jendraszak M., Warchol J. B.

Folia Histochemica et Cytobiologica

|

2002

|

tom 40

|

nr 2

18

The contribution of phosphatidylserine partition and transmembrane potential to the interaction of merocyanine 540 with lipid bilayers

63%

Rozalski M., Waczulikova I., Rievaj J., Nagyova K., Bryszewska M., Watala C.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr 2

19

D-K6L9 peptide combination with IL-12 inhibits the recurrence of tumors in mice

51%

Cichon T., Smolarczyk R., Matuszczak S., Barczyk M., Jarosz M., Szala S.

Archivum Immunologiae et Therapiae Experimentalis

|

2014

|

tom 62

|

nr 4

20

Potential roles of the NFkappaB and glutathione pathways in mature human erythrocytes

51%

Ghashghaeinia M., Toulany M., Saki M., Rodemann H. P., Mrowietz U., Lang F., Wieder T.

Cellular and Molecular Biology Letters

|

2012

|

tom 17

|

nr 1

Anucleated erythrocytes were long considered as oxygen-transporting cells with limited regulatory functions. Components of different nuclear signaling pathways have not been investigated in those cells, yet. Surprisingly, we repeatedly found significant amounts of transcription factors in purified erythrocyte preparations, i.e. nuclear factor κB (NFκB), and major components of the canonical NFκB signaling pathway. To investigate the functional role of NFκB signaling, the effects of the preclinical compounds Bay 11-7082 and parthenolide on the survival of highly purified erythrocytes were investigated. Interestingly, both inhibitors of the NFκB pathway triggered erythrocyte programmed cell death as demonstrated by enhanced phospholipid scrambling (phosphatidylserine exposure) and cell shrinkage. Anucleated erythrocytes are an ideal cellular model allowing the study of nongenomic mechanisms contributing to suicidal cell death. As NFκB inhibitors might also interfere with the anti-oxidative defense systems of the cell, we measured the levels of reduced glutathione (GSH) after challenge with the inhibitors. Indeed, incubation of erythrocytes with Bay 11-7082 clearly decreased erythrocyte GSH levels. In conclusion, the pharmacological inhibitors of the NFκB pathway Bay 11-7082 and parthenolide interfere with the survival of erythrocytes involving mechanisms other than disruption of NFκB-dependent gene expression. Besides affecting erythrocyte survival, NFκB inhibition and induction of erythrocyte phosphatidylserine exposure may influence blood clotting. Future studies will be aimed at discriminating between NFκB-dependent and NFκB-independent GSH-mediated effects of Bay 11-7082 and parthenolide on erythrocyte death.

Ograniczanie wyników

ATP-dependent phosphatidylserine formation in animal cells as a base exchange reaction

No increase of phosphatidylserine exposure accompanying the increased membrane fluidity in erythrocytes of ataxia telangiectasia gene [ATM] carriers

Homing of annexin-labeled stem cells to apoptopic cells

Involvement of Naplus-Hplus exchanger in desmopressin-induced platelet procoagulant response

Annexin VI, a novel ATP-dependent, phospholipid-binding protein

Sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate modulate phosphatidylserine homeostasis in glioma C6 cells

Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine

Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decarboxylase

Participation of leukotriene C4 in the regulation of suicidal erythrocyte death

Transmembrane segment M2 of glycine receptor as a model system for the pore-forming structure of ion channels

The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies

Interaction of spectrin with phospholipids is inhibited by isolated erythrocyte ankyrin. A monolayer study

Interactions of spectrins with phospholipids: possible physiological role

Interactions of annexins IV and VI with erythrocyte membrane in the presence of Ca2. A biochemical and electron microscopy study

Reconstitution of flippase activity into liposomes

Interaction of annexin VI with membranes. Regulation by ATP in vitro

Plasma membrane translocation of phosphatidylserine in human spermatozoa

The contribution of phosphatidylserine partition and transmembrane potential to the interaction of merocyanine 540 with lipid bilayers

D-K6L9 peptide combination with IL-12 inhibits the recurrence of tumors in mice

Potential roles of the NFkappaB and glutathione pathways in mature human erythrocytes