Impact of membranetropic compounds on the sensitivity of mammalian erythrocytes to the posthypertonic shock action

The effect of cationic trifluoperazine (TFP) and nonionic decyl-β,D-glucopyranoside (DGP) on the sensitivity of human, rabbit and rat erythrocytes to the action of posthypertonic shock (PHS) at 0 °C was studied in this research. Trifluoperazine shows a high antihemolytic activity under conditions of PHS of human and animal erythrocytes at slight differences of values of effective concentrations. The value of antihemolytic activity of TFP for human and rabbit erythrocytes is ~ 60 %, and for rat cells the efficiency of this compound is approximately 1.4 times higher. The values of antihemolytic activity of DGP under PHS conditions of human and rat erythrocytes are comparable and amounts to 62 and 66 %, respectively. Significant differences of this parameter (72 %) were found for rabbit cells compared with human erythrocytes. It was found that the size of plateau (the range of concentrations of amphiphilic compounds within the minimum level of erythrocyte hemolysis was observed) cationic TFP and nonionic DGP are significantly different. Thus, TFP has a narrow plateau (100–200 μmol/L), while DGP has a rather wide one (400–1600 μmol/L). In addition, a shift of the plateau concentrations of DGP to the region of higher values compared with TFP is observed, which is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP. Moreover, a shift of plateau concentrations of DGP to the region of higher values compared with TFP is observed, that is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP one. It was established that under PHS conditions of human erythrocyte, both compounds (TFP and DGP) show a commensurate antihemolytic activity. At the same time, for rabbit cells, DGP is more effective compared with TFP, and for rat erythrocytes, on the contrary, the efficiency of TFP is higher than DGP. This may be due to differences in the phospholipid composition of mammalian erythrocyte membranes. The results suggest that under PHS conditions the efficacy of membrane-tropic compounds is most likely due to their ability to incorporate into membrane to the defect formation areas, and thus significantly increase the critical hemolytic volume of cells, as a result, prevent their destruction.

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Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement

Biochemical Journal ◽

10.1042/bj2840169 ◽

1992 ◽

Vol 284 (1) ◽

pp. 169-176 ◽

Cited By ~ 60

Author(s):

T R Hughes ◽

S J Piddlesden ◽

J D Williams ◽

R A Harrison ◽

B P Morgan

Keyword(s):

Affinity Purification ◽

Membrane Attack Complex ◽

Erythrocyte Membranes ◽

Dependent Manner ◽

Inhibitory Protein ◽

Rat Erythrocytes ◽

Butanol Extract ◽

Isolation And Characterization ◽

Membrane Bound

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

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A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry

The Journal of Membrane Biology ◽

10.1007/s00232-014-9718-0 ◽

2014 ◽

Vol 247 (11) ◽

pp. 1181-1189 ◽

Cited By ~ 3

Author(s):

Savita Sharma ◽

Vinny Punjabi ◽

Surekha M. Zingde ◽

Sadashiv M. Gokhale

Keyword(s):

Mass Spectrometry ◽

Protein Profile ◽

Erythrocyte Membranes ◽

Mammalian Erythrocyte

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Phospholipid composition of dystrophic chicken erythrocyte plasmalemmae I. Isolation of a unique lipid in dystrophic erythrocyte membranes

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(84)90454-1 ◽

1984 ◽

Vol 778 (1) ◽

pp. 112-120 ◽

Cited By ~ 6

Author(s):

Mark Kester ◽

C.A. Privitera

Keyword(s):

Phospholipid Composition ◽

Erythrocyte Membranes ◽

Chicken Erythrocyte ◽

Dystrophic Chicken

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Colocalization of GAPDH and band 3 (AE1) proteins in rat erythrocytes and kidney intercalated cell membranes

AJP Renal Physiology ◽

10.1152/ajprenal.1992.262.5.f892 ◽

1992 ◽

Vol 262 (5) ◽

pp. F892-F896 ◽

Cited By ~ 4

Author(s):

L. Ercolani ◽

D. Brown ◽

A. Stuart-Tilley ◽

S. L. Alper

Keyword(s):

Plasma Membrane ◽

Cell Membranes ◽

Basolateral Membrane ◽

Integral Membrane Protein ◽

Band 3 ◽

Erythrocyte Membranes ◽

Rat Erythrocytes ◽

Kidney Medulla ◽

Multifunctional Protein ◽

Alternatively Spliced

Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.2.12) (GAPDH) is a multifunctional protein that associates with the cytoplasmic face of intact human erythrocyte membranes. This association has been postulated to be critically dependent on the interaction of GAPDH with the highly acidic NH2-terminal domain of the principal integral membrane protein of the erythrocyte plasma membrane, the band 3 anion exchanger (AE1). This domain is not conserved in murine erythrocyte AE1 and is fully deleted in the alternatively spliced AE1 isoform that is expressed in the kidney. The lack of conservation of this domain has been proposed to explain the reported absence of GAPDH association with rodent erythrocyte membranes. To determine whether GAPDH could be associated with AE1 proteins in rodent cell membranes, specific rabbit antibodies to peptide sequences of rat GAPDH and mouse AE1 were used to immunolocalize these proteins in sequential semithin sections of rat erythrocytes and kidney medulla. In rat erythrocytes, GAPDH immunoreactivity was predominantly membrane associated and colocalized with AE1. In the kidney medulla, GAPDH was concentrated in the basolateral membrane of type A intercalated cells, where it colocalized with the alternatively spliced kidney form of AE1. GAPDH immunoreactivity was not detected in the plasma membrane of any other cell type in the kidney, indicating its predominant association with AE1-rich membranes. If this membrane interaction occurs via AE1 binding, then GAPDH must have binding sites in addition to those previously described for such binding in human AE1.

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Studies of the antioxidant and antihemolytic activity of quinoline derivatives in a model of oxidative damage to erythrocyte membranes

Pharmaceutical Chemistry Journal ◽

10.1007/s11094-009-0220-4 ◽

2009 ◽

Vol 43 (1) ◽

pp. 7-10 ◽

Cited By ~ 13

Author(s):

M. G. Malakyan ◽

S. A. Badzhinyan ◽

L. A. Vardevanyan ◽

D. S. Grigoryan ◽

D. É. Egiazaryan ◽

...

Keyword(s):

Oxidative Damage ◽

Erythrocyte Membranes ◽

Quinoline Derivatives ◽

Antihemolytic Activity

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Effects of n-Octyl-β-D-Glucopyranoside on Human and Rat Erythrocyte Membrane Stability Against Hemolysis

The Open Biology Journal ◽

10.2174/1874196701205010001 ◽

2012 ◽

Vol 5 (1) ◽

pp. 1-5 ◽

Cited By ~ 4

Author(s):

Cesare Sblano ◽

Silvia Micelli ◽

Daniela Meleleo

Keyword(s):

Erythrocyte Membrane ◽

Practical Importance ◽

Human Erythrocytes ◽

Erythrocyte Membranes ◽

Ionic Surfactant ◽

Hypotonic Medium ◽

Rat Erythrocytes ◽

Biphasic Effect ◽

Dose Dependent

The practical importance for the pharmaceutical and cosmetics industries of the interactions between biological membranes and surfactant molecules has led to intensive research within this area. The interactions of non-ionic surfactant n-octyl-β-D-glucopyranoside (OG) with the human and rat erythrocyte membranes were studied. The in vitro hemolytic and antihemolytic activities were determined by employing a method in which both erythrocytes were added to the hypotonic medium containing OG at different concentrations, and the amount of haemoglobin released was determined. noctyl- β-D-glucopyranoside was found to have a biphasic effect on both types of erythrocyte membrane. We also investigated the interactions of OG with the erythrocyte membrane in isotonic medium; the dose-dependent curves show similar behaviour in both human and rat erythrocytes. Our results showed that OG has greater antihemolytic potency on rat than on human erythrocytes; furthermore, rat erythrocytes were more sensitive than human erythrocytes to hypotonic shock. How the different lipoprotein structure of these erythrocytes determines a difference in antihemolytic activity is discussed.

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