Hot-cold hemolysis: The role of positively charged membrane phospholipids

Meduski, J; Hochstein, Paul

doi:10.1007/bf01931879

Experientia

1972

DOI: 10.1007/bf01931879

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Hot-cold hemolysis: The role of positively charged membrane phospholipids

J Meduski

Paul Hochstein

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1974

1993

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Cited by 6 publications

(2 citation statements)

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“…The hemolytic activity of alpha-toxin is observed by incubating the toxin with sheep erythrocytes at 37°C and then chilling the preparation to below 10°C (the phenomenon of hot-cold hemolysis) (47). Meduski and Hochstein (27) reported that hot-cold hemolysis is the response of erythrocytes to agents which alter or remove -N+(CH3)3 groups of the membrane lipids. Smyth et al (45) reported that treatment of erythrocyte ghosts with the toxin caused the appearance of droplets which remained associated with membranes treated with the toxin.…”

mentioning

confidence: 99%

Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes

1993

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When rabbit erythrocytes were exposed to low concentrations of Clostridium perfringens alpha-toxin, hot-cold hemolysis was observed. The toxin induced production of phosphatidic acid (PA) in a dose-dependent manner when incubated with erythrocytes at 37rC. When erythrocyte membranes were incubated with the toxin and ['y32P]ATP in the presence or absence of ethanol, [32PJPA formation was maximal within 30 s, then sharply decreased, and began again after 5 min of incubation. Ethanol had no effect on the early appearance (at -5 min) of PA formation induced by the toxin but significantly inhibited formation of PA over 10 min of incubation. Treatment of erythrocyte membranes with alpha-toxin resulted in the biphasic formation of 1,2-diacylglycerol and PA as well as an increase of inositol-1,4,5-trisphosphate (1P3) and decrease of phosphatidylinositol-4,5-bisphosphate (PIP2) within 30 s. Neomycin inhibited the toxin-induced increase in turbidity of egg yolk suspensions but did not inhibit the toxin-induced hemolysis of intact erythrocytes. On the other hand, neomycin inhibited the toxin-induced hemolysis of saponin-treated erythrocytes. In addition, neomycin inhibited PA formation induced by the toxin in erythrocyte membranes. IP3 was released by incubation of PIP2 with erythrocyte membranes but not by incubation of PIP2 with the toxin. The toxin stimulated the membrane-induced release of IP3 from PIP2. These data suggest that the toxin-induced hemolysis is dependent on the action of phospholipase C in erythrocyte membranes.

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confidence: 99%

Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes

1993

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“…The nature of this hot-cold effect, despite its early cognizance (4,9), has as yet eluded satisfactory explanation, although there have been several hypotheses (2,18,21,40).…”

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Phenomenon of hot-cold hemolysis: chelator-induced lysis of sphingomyelinase-treated erythrocytes

Smyth¹,

Möllby²,

Wadström³

1975

Infect Immun

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Staphylococcus aureus produces a phospholipase C specific for sphingomyelin (beta-hemolysin). Erythrocytes with approximately 50% sphingomyelin in their membranes, e.g., from sheep, have been shown to have up to 60% of this phospholipid hydrolyzed by this enzyme at 37 C in isotonic buffered saline without hemolysis. Cooling of sphingomyelinase C-treated erythrocytes to 4 C causes complete lysis of the cells, a phenomenon known as hot-cold hemolysis. The addition of ethylenediaminetetraacetate (EDTA) to sheep erythrocytes preincubated with sphingomyelinase C was found to induce rapid hemolysis at 37 C. The treated cells became susceptible to chelator-induced hemolysis and to hot-cold hemolysis simultaneously, and the degree of lysis of both mechanisms increased equally with prolonged preincubation with sphingomyelinase C. Erythrocytes of species not readily susceptible to hot-cold hemolysis were equally insusceptible to chelator-induced lysis. Chelators of the EDTA series were the most effective, whereas chelators more specific for Ca2+, Zn2+, Fe2+, Cu2+, and Mg2+ were without effect. The rate of chelator-induced lysis was dependent on the preincubation period with beta-hemolysin and on the concentration of chelator added. The optimal concentration of EDTA was found to equal the amount of exogenously added Mg2+, a cation necessary for sphingomyelinase C activity. Hypotonicity increased the rate of chelator-induced hemolysis, whereas increasing the osmotic pressure to twice isotonic completely inhibited chelator-induced lysis. The data suggest that exogenously added and/or membrane-bound divalent cations are important for the stability of sphingomyelin-depleted membranes. The phenomenon of hot-cold hemolysis may be a consequence of the temperature dependence of divalent ion stabilization.

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Glucose-6-phosphate dehydrogenase deficiency: A novel role for thyroxine in peroxide-induced hemolysis

Walls

Hochstein

1974

Life Sciences

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Hot-cold hemolysis: The role of positively charged membrane phospholipids

Cited by 6 publications

References 5 publications

Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes

Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes

Phenomenon of hot-cold hemolysis: chelator-induced lysis of sphingomyelinase-treated erythrocytes

Glucose-6-phosphate dehydrogenase deficiency: A novel role for thyroxine in peroxide-induced hemolysis

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