Linked Life Data

7619793

Source:http://linkedlifedata.com/resource/pubmed/id/7619793

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1995-8-30
pubmed:abstractText
Hemolysis of human erythrocytes induced by free radicals initiated from water-soluble, 2,2'-azobis(amidinopropane) dihydrochloride (AAPH) has been investigated. The formation of the radical detected as DMPO (5,5-dimethyl-1-pyrroline N-oxide) adduct depended on temperature and AAPH concentration in a similar manner as hemolysis. The curve for the formation of DMPO--radical adduct, however, did not correspond directly to the hemolysis curve. The product of thiobarbituric acid-reactive materials, which reflect the extent of lipid peroxidation, could not be related directly to the hemolysis curve, too. During the hemolysis, the fluidity of the erythrocyte membrane did not change in appearance. To study whether band 3 proteins participate in the hemolysis or not, eosin-5-maleimide (EMI)-labeled ghosts were incubated in the presence of AAPH. High molecular weight band 3 was formed, and the induced circular dichrosim spectrum of the bound EMI was changed, indicating a conformational change of band 3. It was observed that ascorbic acid suppressed the hemolysis and the oxidation of band 3 dose dependently to produce an induction period. This result shows that specifically blocking band 3 oxidation inhibits the hemolysis, despite lipid peroxidation. Further, it was observed that the EMI-labeled erythrocytes revealed distinct clusters by incubation with AAPH. This means a redistribution of band 3 proteins to form hemolytic holes in the membrane. However, the time course of the conformational change of band 3 during the redistribution was not also correspondent to the hemolysis curve. These results indicate that either lipid peroxidation or redistribution of oxidized band 3 is not attributed only by itself to the hemolysis. Thus, the hemolysis was interpreted by a simple competitive reaction model between lipid peroxidation and redistribution of oxidized band 3. This model explained well the hemolysis curves.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8940-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7619793-Amidines, pubmed-meshheading:7619793-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:7619793-Ascorbic Acid, pubmed-meshheading:7619793-Circular Dichroism, pubmed-meshheading:7619793-Cyclic N-Oxides, pubmed-meshheading:7619793-Electron Spin Resonance Spectroscopy, pubmed-meshheading:7619793-Erythrocytes, pubmed-meshheading:7619793-Free Radicals, pubmed-meshheading:7619793-Hemolysis, pubmed-meshheading:7619793-Humans, pubmed-meshheading:7619793-Kinetics, pubmed-meshheading:7619793-Lipid Peroxidation, pubmed-meshheading:7619793-Membrane Lipids, pubmed-meshheading:7619793-Oxidation-Reduction, pubmed-meshheading:7619793-Protein Conformation, pubmed-meshheading:7619793-Solubility, pubmed-meshheading:7619793-Spin Labels, pubmed-meshheading:7619793-Thermodynamics, pubmed-meshheading:7619793-Water
pubmed:year
1995
pubmed:articleTitle
Mechanism of free radical-induced hemolysis of human erythrocytes: hemolysis by water-soluble radical initiator.
pubmed:affiliation
Pharmaceutical Institute, Tohoku University, Sendai, Japan.
pubmed:publicationType
Journal Article, In Vitro