Effect of magnesium ions on red cell membrane properties

Beaven, G. H.; Parmar, J.; Nash, GB; Bennett, Pauline M.; Gratzer, Walter

doi:10.1007/bf01868609

Cited by 26 publications

(13 citation statements)

References 26 publications

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“…The presence of MgATP throughout ghost preparation resulted in membranes that exhibited significantly increased resistance to deformationinduced fragmentation. Mg 2ϩ by itself at mM concentrations has previously been proposed to stabilize red cell membranes (50). We also observed a small effect of MgCl 2 on stability of ghost membranes, but the stablization was about an order of magnitude less than that seen with MgATP (data not shown).…”

Section: Discussionsupporting

confidence: 59%

Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability

Manno

Takakuwa

Mohandas

2002

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

225

180

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Asymmetric distribution of phospholipids is ubiquitous in the plasma membranes of many eukaryotic cells. The majority of the aminophospholipids are located in the inner leaflet whereas the cholinephospholipids are localized predominantly in the outer leaflet. Several functional roles for asymmetric phospholipid distribution in plasma membranes have been suggested. Disruption of lipid asymmetry creates a procoagulant surface on platelets and serves as a trigger for macrophage recognition of apoptotic cells. Furthermore, the dynamic process of phospholipid translocation regulates important cellular events such as membrane budding and endocytosis. In the present study, we used the red cell membrane as the model system to explore the contribution of phospholipid asymmetry to the maintenance of membrane mechanical properties. We prepared two different types of membranes in terms of their phospholipid distribution, one in which phospholipids were scrambled and the other in which the asymmetric distribution of phospholipids was maintained and quantitated their mechanical properties. We documented that maintenance of asymmetric distribution of phospholipids resulted in improved membrane mechanical stability. The greater difficulty in extracting the spectrinactin complex at low-ionic strength from the membranes with asymmetric phospholipid distribution further suggested the involvement of interactions between aminophospholipids in the inner leaflet and skeletal proteins in modulating mechanical stability of the red cell membrane. These findings have enabled us to document a functional role of lipid asymmetry in regulating membrane material properties.A symmetric distribution of phospholipids is ubiquitous in the plasma membranes of many eukaryotic cells. The majority of the aminophospholipids, phosphatidylserine (PS) and phosphatidylethanolamine (PE), are located in the inner leaflet whereas the cholinephospholipids, phosphatidylcholine and sphingomyelin, are localized predominantly in the outer leaflet (1, 2). At least three distinct activities are involved in the regulation of membrane lipid sidedness. The MgATPdependent aminophospholipid translocase, (also known as flippase or ATPase II; ref. 3), is responsible for localization of PS and PE in the inner leaflet by rapidly translocating them from the outer to inner leaflet against the electrochemical gradient (4-6). PS is a better substrate than PE for the aminophospholipid translocase (7-9), and the stoichiometry between aminophospholipid translocation and ATP hydrolysis is close to one (10). The activity of the aminophospholipid translocase is inhibited by high concentrations of Ca 2ϩ (11)(12)(13), by the pseudosubstrates of P-type ATPase such as vanadate (14), acetyl phosphate, and p-nitrophenyl phosphate (15), and by sulfhydryl reactive reagents such as N-ethylmaleimide (16) and pyridyldithioethylamine (PDA), a specific inhibitor of phospholipid translocase (16)(17)(18)(19). The less specific MgATP-requiring phospholipid translocase, floppase, moves phospholipids f...

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Section: Discussionsupporting

confidence: 59%

Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability

Manno

Takakuwa

Mohandas

2002

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

225

180

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“…It is also a structural co-factor and stabilizes ribosomes, lipid membranes and nucleic acids (Beaven et al, 1990;Hartwig, 2001;Selmer et al, 2006). Mg 21 (which, unlike all the other biological metals discussed in this review, is not a transition metal) is highly abundant in bacterial cells.…”

Section: Magnesium (Mg 21 )mentioning

confidence: 99%

An overview of the biological metal uptake pathways in Pseudomonas aeruginosa

Schalk

Cunrath

2016

Environmental Microbiology

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Biological metal ions, including Co, Cu, Fe, Mg, Mn, Mo, Ni and Zn ions, are necessary for the survival and the growth of all microorganisms. Their biological functions are linked to their particular chemical properties: they play a role in structuring macromolecules and/or act as co-factors catalyzing diverse biochemical reactions. These metal ions are also essential for microbial pathogens during infection: they are involved in bacterial metabolism and various virulence factor functions. Therefore, during infection, bacteria need to acquire biological metal ions from the host such that there is competition for these ions between the bacterium and the host. Evidence is increasingly emerging of "nutritional immunity" against pathogens in the hosts; this includes strategies making access to metals difficult for infecting bacteria. It is clear that biological metals play key roles during infection and in the battle between the pathogens and the host. Here, we summarize current knowledge about the strategies used by Pseudomonas aeruginosa to access the various biological metals it requires. P. aeruginosa is a medically significant Gram-negative bacterial opportunistic pathogen that can cause severe chronic lung infections in cystic fibrosis patients and that is responsible for nosocomial infections worldwide.

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“…Mg 2+ is necessary for the association of actin with tropomyosin [124]. Also, Mg 2+ was shown to increase erythrocyte membrane stability [125]. It is noteworthy that spectrin has binding sites for both Mg 2+ and Ca 2+ [126] (Fig 3B).…”

Section: +mentioning

confidence: 99%

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Barvitenko

Adragna

Weber³

2005

Cell Physiol Biochem

135

104

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Erythrocytes play a key role in human and vertebrate metabolism. Tissue O₂ supply is regulated by both hemoglobin (Hb)-O₂ affinity and erythrocyte rheology, a key determinant of tissue perfusion. Oxygenation-deoxygenation transitions of Hb may lead to re-organization of the cytoskeleton and signalling pathways activation/deactivation in an O₂-dependent manner. Deoxygenated Hb binds to the cytoplasmic domain of the anion exchanger band 3, which is anchored to the cytoskeleton, and is considered a major mechanism underlying the oxygenation-dependence of several erythrocyte functions. This work discusses the multiple modes of Hb-cytoskeleton interactions. In addition, it reviews the effects of Mg²⁺, 2,3-diphosphoglycerate, NO, shear stress and Ca²⁺, all factors accompanying the oxygenation-deoxygenation cycle in circulating red cells. Due to the extensive literature on the subject, the data discussed here, pertain mainly to human erythrocytes whose O₂ affinity is modulated by 2,3-diphosphoglycerate, ectothermic vertebrate erythrocytes that use ATP, and to bird erythrocytes that use inositol pentaphosphate.

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Effect of magnesium ions on red cell membrane properties

Cited by 26 publications

References 26 publications

Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability

Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability

An overview of the biological metal uptake pathways in Pseudomonas aeruginosa

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

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