Effects of Phospholipase C on Gastric Vesicle Membranes Containing H+, K+-ATPase.

Olaisson, Hans; Mårdh, Sven; Arvidson, Gösta

doi:10.3891/acta.chem.scand.36b-0649

Cited by 8 publications

(6 citation statements)

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“…Besides phospholipids, plasma membranes contain a high amount of cholesterol, but the distribution of this lipid is still a subject of debate: some reports are in favour of an almost symmetrical repartition in the two leaflets (Blau and Pelletier et al, 1987Post et al, 1988Record et al, 1984Higgins and Evans, 1978Sessions and Horwitz, 1983Sessions and Horwitz, 1983Sessions and Horwitz, 1983 Olaisson et al, 1985Deutsch and Kelly, 1981Bollen and Higgins, 1980Dominski et al, 1983Buckland et al, 1978Marinetti et al, 1976Nilsson and Dallner, 1977 Crain and Marinetti, 1979Krebs et al, 1979Harb et al, 1981 an uneven distribution of cholesterol (Brasaemle et al, 1988;Fisher, 1976;Schroeder et al, 1991).…”

Section: Asymmetry In Various Membranes Plasma Membranesmentioning

confidence: 99%

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Zachowski

1993

Biochemical Journal

780

565

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Section: Asymmetry In Various Membranes Plasma Membranesmentioning

confidence: 99%

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Zachowski

1993

Biochemical Journal

780

565

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“…To evaluate the physiological significance of PtdEtn for Protein C activation on the surface of HUVECs, the cells were stimulated with thrombin and PtdEtn localization was investigated ( Figure 6). After treatment of HUVECs for 20 min with thrombin (0.5 units/ml), TNBS, a membrane-impermeant agent, was added to the culture, and the amount ofPtdEtn that could bind to TNBS was determined [26]. Without stimulation of HUVECs, approximately four-fifths of PtdEtn was localized on the inside of the membrane, as 4.30% and 17.30% of total phospholipids were PtdEtn reacted and not reacted with TNBS respectively.…”

Section: Resultsmentioning

confidence: 99%

“…The supernatant was centrifuged at 10500 g for 15 min and the resulting supernatant was further centrifuged for 1 h at 105000 g. The precipitated membrane-rich fraction was suspended in PBS and total lipids were extracted with chloroform/methanol (1:2, v/v). The insoluble fraction was discarded by centrifugation, then 0.15 M NaCl was added and the resulting chloroform layer was dried under a nitrogen stream [26]. The residue was spotted on silica gel 60F-254 (Merck) and developed first with chloroform/methanol/ammonium hydroxide (65:25:4, by vol.…”

Section: Extraction Of Phospholipids From Cultured Endothelial Cellsmentioning

confidence: 99%

Enhancement of thrombin-thrombomodulin-catalysed protein C activation by phosphatidylethanolamine containing unsaturated fatty acids: possible physiological significance of phosphatidylethanolamine in anticoagulant activity of thrombomodulin

Horie

Ishii

Hara

et al. 1994

Biochemical Journal

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The effects of phospholipid vesicles and their fatty acid compositions on the acceleration of Protein C activation by thrombin-thrombomodulin was studied in vitro. Four main phospholipid fractions were prepared from cultured human umbilical vein endothelial cells, and purified thrombomodulin from human placenta was reconstituted into vesicles consisting of phosphatidylcholine (PtdCho) alone, PtdCho plus phosphatidylethanolamine (PtdEtn), PtdCho plus phosphatidylserine (PtdSer) and PtdCho plus PtdIns (1:1, w/w in each case). Vesicles of PtdCho, PtdIns/PtdCho, PtdSer/PtdCho and PtdEtn/PtdCho increased thrombin-thrombomodulin-catalysed protein C activation by 1.2-, 1.9-, 4.3- and 8.4-fold respectively compared with that in the absence of phospholipid. This Protein C activation was not affected by distearoyl PtdEtn/distearoyl PtdCho, whereas it was markedly increased with increasing content of unsaturated fatty acid in PtdEtn. The thrombin-dependent Protein C activation by thrombomodulin reconstituted into dilinolenoyl PtdEtn/distearoyl PtdCho was 14.6 times that by thrombomodulin reconstituted into distearoyl PtdEtn/distearoyl PtdCho, as a result of a decrease in the dissociation constant (Kd) for thrombin and the Michaelis constant (Km) for Protein C of thrombomodulin. Binding of Protein C to PtdEtn/PtdCho fixed to a microwell plate required the presence of CaCl2 and increased with increasing degree of unsaturation of fatty acid in PtdEtn. As PtdEtn appeared on the outside of the plasma membrane in cultured human umbilical vein endothelial cells after thrombin stimulation, it was presumed that Protein C activation could be elevated by PtdEtn at the outer surface of the plasma membrane via an increased affinity between thrombomodulin, thrombin and Protein C, resulting from both increased formation of the thrombin-thrombomodulin complex via a conformational change in thrombomodulin and increased binding of Protein C to the membrane phospholipid in a Ca(2+)-dependent manner.

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“…It has been known for sometime that the gastric mucosa contains a H+-Kf-ATPase (53) and that the activity of the ATPase may be related to its lipid environment. A report by Olaisson et al (54), using gastric vesicle membranes, demonstrated that phospholipase C degraded 50% of the membrane phospholipids, leaving only sphingomyelin and PI intact. Concomitant with this breakdown was a 50% reduction in the H'-K+ ATPase activity.…”

Section: Membrane Lipid Composition and Changes In Ion Transportmentioning

confidence: 97%

Phospholipids and Electrolyte Transport

Yorio

Frazier²

1990

Experimental Biology and Medicine

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Our understanding of the role of phospholipids in ion transport processes is only beginning to be appreciated. Although the role of polyphosphoinositide and its derived second messenger molecules IP3, diacylglycerol, and arachidonic acid are well studied, we are still not certain as to how changes in the lipid bilayer structure influence the status of ion channels. This review focused on those studies which show a strong correlation with ion conductance changes and the status of the membrane phospholipids. In addition, a number of observations point to a major role of lipid second messengers that activate enzymes involved in protein phosphorylations, i.e., protein kinase C, as major regulators of a variety of ion channels and transporters. Such lipid second messengers provide a cellular mechanism whereby hormones, neurotransmitters, and pharmacologic agents functionally control the ionic environment and intracellular pH of target cells. Some of these pathways still remain to be elucidated; however, an appreciation for the participation of membrane phospholipids in these actions has been presented.

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Effects of Phospholipase C on Gastric Vesicle Membranes Containing H+, K+-ATPase.

Cited by 8 publications

References 0 publications

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Enhancement of thrombin-thrombomodulin-catalysed protein C activation by phosphatidylethanolamine containing unsaturated fatty acids: possible physiological significance of phosphatidylethanolamine in anticoagulant activity of thrombomodulin

Phospholipids and Electrolyte Transport

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