Mechanism of hemolysis induced by ferriprotoporphyrin IX.
Open Access
- 1 September 1981
- journal article
- research article
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 68 (3) , 672-677
- https://doi.org/10.1172/jci110302
Abstract
Incubation of a 0.5% suspension of washed, normal mouse erythrocytes with ferriprotoporphyrin IX (FP) at 37 degrees C and pH 7.4 caused potassium loss, swelling, increased susceptibility to hypotonic lysis, and finally hemolysis. Hemolysis was not inhibited by incubation in the dark, malonyldialdehyde was not produced, and various free radical scavengers had no effect on the hemolysis. Only the sulfhydryl compounds, cysteine, dithiothreitol, and mercaptoethanol protected erythrocytes from FP. Potassium loss reached 90% within 30 min of exposure to 5 microM FP. This amount of FP caused greater than 50% hemolysis within 2.5 h. Sucrose (0.1 M) completely prevented hemolysis but had no effect on potassium loss. Likewise, reducing the temperature from 37 to 25 degrees C greatly retarded hemolysis but had no effect on potassium loss. These observations indicate that FP impairs the erythrocyte's ability to maintain cation gradients and induces hemolysis by a colloid-osmotic mechanism.This publication has 24 references indexed in Scilit:
- The role of the superoxide anion as a toxic species in the erythrocytePublished by Elsevier ,2004
- Hemolysis of mouse erythrocytes by ferriprotoporphyrin IX and chloroquine. Chemotherapeutic implications.Journal of Clinical Investigation, 1980
- Ferriprotoporphyrin IX Fulfills the Criteria for Identification as the Chloroquine Receptor of Malaria Parasites.Biochemistry, 1980
- Assay of picomole amounts of ATP, ADP, and AMP using the luciferase enzyme systemAnalytical Biochemistry, 1975
- Chloroquine-Resistant Plasmodium falciparum : Effect of Substrate on Chloroquine and Amodiaquin AccumulationAntimicrobial Agents and Chemotherapy, 1974
- Evidence for an irreversible reaction between nitrite and human methemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobinsJournal of Clinical Investigation, 1970
- Altered sulfhydryl reactivity of hemoglobins and red blood cell membranes in congenital heinz body hemolytic anemiaJournal of Clinical Investigation, 1968
- EFFECTS OF SULFHYDRYL INHIBITION ON RED BLOOD CELLS. I. MECHANISM OF HEMOLYSIS*Journal of Clinical Investigation, 1962
- A new method of hemin isolationBiochimica et Biophysica Acta, 1957