Red blood cell permeabilization by hypotonic treatments, saponin, and anticancer avicins

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 6, 2010, Pages 1189-1196

  Arias, Mauricio ^a   Quijano, Jairo C ^a,b   Haridas, Valsala ^c   Gutterman, Jordan U ^c   Lemeshko, Victor V ^a  

^a UNIVERSIDAD NACIONAL DE COLOMBIA   (Colombia)

^b Politecnico Colombiano JIC   (Colombia)

^c UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

Author keywords

Avicins; Hemolysis; Light dispersion; Plasma membrane; Pore size; Red blood cells; Saponin

Indexed keywords

AVICIN D; AVICIN G; HEMOGLOBIN; HYPOTONIC SOLUTION; MACROGOL; MACROGOL 8000; SAPONIN; TRITERPENOID; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; ARTICLE; CANCER CELL CULTURE; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL PROTECTION; CELL SWELLING; CELL VIABILITY; CHANNEL GATING; CONTROLLED STUDY; CULTURE MEDIUM; CYTOSOL; CYTOTOXICITY; DISPERSION; ERYTHROCYTE MEMBRANE; HEMOLYSIS; HUMAN; HUMAN CELL; HYDRODYNAMICS; INCUBATION TIME; MALE; MEMBRANE BINDING; MOLECULAR WEIGHT; OSMOSIS; PRIORITY JOURNAL; PROSTATE CANCER;

ANIMALS; ANTINEOPLASTIC AGENTS; CELL LINE, TUMOR; CELL MEMBRANE PERMEABILITY; DRUG SCREENING ASSAYS, ANTITUMOR; ERYTHROCYTE MEMBRANE; HEMOLYSIS; HUMANS; HYPOTONIC SOLUTIONS; MALE; OSMOTIC PRESSURE; POLYETHYLENE GLYCOLS; PROSTATIC NEOPLASMS; RATS; RATS, SPRAGUE-DAWLEY; SAPONINS;

RATTUS;

EID: 77952550950     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.03.018     Document Type: Article

References (42)

1. Orcutt R.H., Thurmond T.S., Ferslew K.E. Mathematical modeling of the osmotic fragility of rabbit red blood cells. J. Pharmacol. Toxicol. Methods 1995, 34:169-174.
2. Segal R., Mansour M., Zaitschek D.V. Effect of ester groups on the haemolytic action of some saponins and sapogenins. Biochem. Pharmacol. 1966, 15:1411-1416.
3. Helmerhorst E.J., Reijnders I.M., van 't Hof W., Veerman E.C.I., Amerongen A.V.N. A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides. FEBS Lett. 1999, 449:105-110.
4. Chapman D., Buxser S. Effects of membrane partitioning and other physical chemical properties on the apparent potency of "membrane active" compounds evaluated using red blood cell lysis assays. Anal. Biochem. 2002, 303:153-166.
5. Raghuraman H., Chattopadhyay A. Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem. Phys. Lipids 2005, 134:183-189.
6. Drabkin D. The standardization of hemoglobin measurement. Am. J. Med. Sci. 1949, 217:710-711.
7. Lenfant F., Bureau A., Lahet J.-J., Bouyer F., Chaillot B., Freysz M. Effects of an oxidative stress on human hemoglobin: a multiwavelength visible spectrometry study. Biomed. Pharmacother. 2005, 59:230-232.
8. Li Q., Dong C., Deng A., Katsumata M., Nakadai A., Kawada T., Okada S., Clayberger C., Krensky A.M. Hemolysis of erythrocytes by granulysin-derived peptides but not by granulysin. Antimicrob. Agents Chemother. 2005, 49:388-397.
9. Yamaji-Hasegawa A., Makino A., Baba T., Senoh Y., Kimura-Suda H., Sato S.B., Terada N., Ohno S., Kiyokawa E., Umeda M., Kobayashi T. Oligomerization and pore formation of a sphingomyelin-specific toxin, Lysenin. J. Biol. Chem. 2003, 278:22762-22770.
10. Aranda F.J., Teruel J.A., Ortiz A. Further aspects on the hemolytic activity of the antibiotic lipopeptide iturin A. Biochim. Biophys. Acta 2005, 1713:51-56.
11. Zakharov S.D., Kotova E.A., Antonenko Y.N., Cramer W.A. On the role of lipid in colicin pore formation. Biochim. Biophys. Acta 2004, 1666:239-249.
12. Preté P.S.C., Malheiros S.V.P., Meirelles N.C., de Paula E. Quantitative assessment of human erythrocyte membrane solubilization by Triton X-100. Biophys. Chem. 2002, 97:1-5.
13. Young J.D., Leong L.G., DiNome M.A., Cohn Z.A. A semiautomated hemolysis microassay for membrane lytic proteins. Anal. Biochem. 1986, 154:649-654.
14. Lang S., Palmer M. Characterization of Streptococcus agalactiae CAMP factor as pore-forming toxin. J. Biol. Chem. 2003, 278:38167-38173.
15. Casallanovo F., de Oliveira F.J.F., de Souza F.C., Ros U., Martínez Y., Pentón D., Tejuca M., Martínez D., Pazos F., Pertinhez T.A., Spisni A., Cilli E.M., Lanio M.E., Alvarez C., Schreier S. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin Sticholysin II. Biopolymers (Peptide Science) 2006, 84:169-180.
16. Hawkins C.L., Brown B.E., Davies M.J. Hypochlorite- and hypobromite-mediated radical formation and its role in cell lysis. Arch. Biochem. Biophys. 2001, 395:137-145.
17. Yang X.-S., Kamino K. Photometric assessment of volume changes coupled with membrane potential in valinomycin-incorporated red blood cells. Jpn. J. Physiol. 1997, 47:217-230.
18. Dourmashkin R.R., Dougherty R.M., Harris R.J. Electro microscopic observation on Rous sarcoma virus and cells membranes. Nature 1962, 194:1116-1119.
19. Bangham A.D., Horne R.W., Glauert A.M., Dingle J.T., Lucy J.A. Action of saponin on biological cell membranes. Nature 1962, 196:952-955.
20. Quijano J.C., Lemeshko V.V. Hemoglobin precipitation by polyethylene glycols leads to underestimation of membrane pore sizes. Biochim. Biophys. Acta 2008, 1778:2775-2780.
21. Mujoo K., Haridas V., Hoffman J.J., Wachter G.A., Hutter L.K., Lu Y., Blake M.E., Jayatilake G.S., Bailey D., Mills G.B., Gutterman J.U. Triterpenoid saponins from Acacia victoriae (Bentham) decrease tumor cell proliferation and induce apoptosis. Cancer Res. 2001, 61:5486-5490.
22. Li X.X., Davis B., Haridas V., Gutterman J.U., Colombini M. Proapototic triterpene electrophiles (avicins) form channels in membranes: cholesterol dependence. Biophys. J. 2005, 88:2577-2584.
23. Lemeshko V.V., Haridas V., Quijano J.C., Gutterman J.U. Avicins, natural anticancer saponins, permeabilize mitochondrial membranes. Arch. Biochem. Biophys. 2006, 454:114-122.
24. Haridas V., Li X., Mizumachi T., Higuchi M., Lemeshko V.V., Colombini M., Gutterman J.U. Avicins, a novel plant-derived metabolite lowers energy metabolism in tumor cells by targeting the outer mitochondrial membrane. Mitochondrion 2007, 7:234-240.
25. Jayatilake G.S., Freeberg D.R., Liu Z., Richheimer S.L., Blake (Nieto) M.E., Bailey D.T., Haridas V., Gutterman J.U. Isolation and structures of avicins D and G: in vitro tumor-inhibitory saponins derived from Acacia victoriae. J. Nat. Prod. 2003, 66:779-783.
26. Rudenko S.V., Nipot E.E. Protection by chlorpromazine, albumin and bivalent cations against haemolysis induced by melittin, [Ala-14] melittin and whole bee venom. Biochem. J. 1996, 317:747-754.
27. Arias M., Orduz S., Lemeshko V.V. Potential-dependent permeabilization of plasma membrane by the peptide BTM-P1 derived from the Cry11Bb1 protoxin. Biochim. Biophys. Acta 2009, 1788:532-537.
28. Pfeiffer D.R., Gudz T.I., Novgorodov S.A., Erdahl W.L. The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition. J. Biol. Chem. 1995, 270:4923-4932.
29. Matsuzawa T., Ikarashi Y. Haemolysis of various mammalian erythrocytes in sodium chloride, glucose and phosphate-buffer solutions. Lab. Anim. 1979, 13:329-331.
30. Coldman M.F., Gent M., Good W. The osmotic fragility of mammalian erythrocytes in hypotonic solution of sodium chloride. Comp. Biochem. Physiol. 1969, 31:605-609.
31. Nelson G.J. Lipid composition of erythrocytes in various mammalian species. Biochim. Biophys. Acta 1967, 144:221-232.
32. Zwaal R.F.A., Van Deenen L.L.M. Protein patterns of red cell membranes from different mammalian species. Biochim. Biophys. Acta 1968, 163:44-49.
33. Coldman M.F., Gent M., Good W. Relationships between osmotic fragility and other species-specific variables of mammalian erythrocytes. Comp. Biochem. Physiol. 1970, 34:759-772.
34. Wessels J.M.C., Veerkamp J.H. Some aspects of the osmotic lysis of erythrocytes. III. Comparison of glycerol permeability and lipid composition of red blood cell membranes from eight mammalian species. Biochim. Biophys. Acta 1973, 291:190-196.
35. Heubush P., Jung C.Y., Green F.A. The osmotic response of human erythrocytes and the membrane cytoskeleton. J. Cell. Physiol. 1985, 122:266-272.
36. Young J.D., Leong L.G., DiNome M.A., Cohn Z.A. A semiautomated hemolysis microassay for membrane lytic proteins. Anal. Biochem. 1986, 154:649-654.
37. Chwalek M., Lalun N., Bobichon H., Plé K., Voutquenne-Nazabadioko L. Structure-activity relationships of some hederagenin diglycosides: haemolysis, cytotoxicity and apoptosis induction. Biochim. Biophys. Acta 2006, 1760:1418-1427.
38. Sparg S.G., Light M.E., van Staden J. Biological activities and distribution of plant saponins. J. Ethnopharmacol. 2004, 94:219-243.
39. Baumann E., Stoya G., Völkner A., Richter W., Lemke C., Linss W. Hemolysis of human erythrocytes with saponin affects the membrane structure. Acta Histochem. 2000, 102:21-35.
40. Seeman P., Cheng D., Iles G.H. Structure of membranes holes in osmotic and saponin hemolysis. J. Cell Biol. 1973, 56:519-527.
41. Winter W.P., Mason K.T., Ford T.D. Mechanism of saponin-induced red cell hemolysis: a reexamination. Blood 1993, 82(Suppl. 1):1829. Abstr.
42. Hao S.J., Hou J.F., Zhang G.J. Effect of solute hydrogen bonding capacity on osmotic stability of lysosomes. Biochemistry (Mosc.) 2009, 74:1363-1367.