The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
The interaction of hemin and bilirubin with the human red cell membrane
Abstract
The incubation of 0.5% suspension of fresh normal erythrocytes with hemin or bilirubin resulted in substantial hemolysis. The amount of hemolysis achieved depended on the concentration of the lytic agents. In each concentration maximum hemolysis was reached within half an hour. The hemolytic effect was somewhat dependent on temperature. Comparison with the hemolytic effect of hemin on mice (Chau, A.C. and Fitch, C.D. (1980) J. Clin. Invest. 66, 856-858) showed that although both cells undergo hemolysis by hemin, the behaviour of each red cell type is different. Centrifugation and fluorescence quenching of membrane embedded probe revealed that both hemin and bilirubin bind to the red cell membrane, hemin having higher affinity. The reaction was found to be hydrophobic and therefore independent of ionic strength. The high affinity of the membrane for hemin was shown by its ability to compete successfully with globin for hemin. Electron microscopy of the red cells which underwent hemolysis indicated cell damage and some membrane destruction. Red cell ghosts were totally disrupted when saturated with hemin. These results suggest an explanation for hemolytic events occurring in cases such as elevation of serum bilirubin or abnormalities leading to hemin release by hemoglobin.
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“In erythrocytes, free heme disrupts the cell membrane, resulting in hemolysis by a colloid-osmotic mechanism: the cell no longer maintains ion gradients, potassium leaks out, and water enters due to the osmotic gradient (18, 49, 99).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [49]
Citations
Cites
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Cited by
Free heme toxicity and its detoxification systems in human
Kumar, S., & Bandyopadhyay, U. (2005) · Toxicology Letters · doi:10.1016/j.toxlet.2005.03.004 · Cited by 852
The Toxicities of Native and Modified Hemoglobins
Everse, J., & Hsia, N. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00499-6 · Cited by 346
Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
Anzaldi, L. L., & Skaar, E. P. (2010) · Infection and Immunity · doi:10.1128/iai.00613-10 · Cited by 295
Jarolim, P., Lahav, M., Liu, S., & Palek, J. (1990) · Blood · doi:10.1182/blood.v76.10.2125.2125 · Cited by 110
The Hog1 Mitogen-Activated Protein Kinase Mediates a Hypoxic Response in Saccharomyces cerevisiae
Hickman, M. J., Spatt, D., & Winston, F. (2011) · Genetics · doi:10.1534/genetics.111.128322 · Cited by 68
Metadata
- Authors
- Kirschner-Zilber, I., Rabizadeh, E., & Shaklai, N.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 1982-08
- Volume
- 690
- Issue
- 1
- Pages
- 20-30
- ISSN
- 0005-2736
- Cited by
- 70
- References
- 29
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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- Kirschner-Zilber, I., Rabizadeh, E., & Shaklai, N. (1982). The interaction of hemin and bilirubin with the human red cell membrane. Biochimica et Biophysica Acta (BBA) - Biomembranes. https://doi.org/10.1016/0005-2736(82)90234-6
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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