Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes

S. M. Waugh, B. M. Willardson, R. Kannan, R. J. Labotka, P. S. Low

Research output: Contribution to journalArticlepeer-review

88 Scopus citations


In earlier model studies we demonstrated that artificially denatured hemoglobin binds to and clusters the protein, band 3, in the plane of the erythrocyte membrane. To determine whether denatured hemoglobin also clusters band 3 in vivo, we have compared the locations of denatured hemoglobin aggregates (Heinz bodies) with band 3 in sickle cells using phase contrast and immunofluorescence microscopy. We report that where Heinz bodies are found associated with the cytoplasmic surface of the membrane, clusters of band 3 are usually colocalized within the membrane. In contrast, normal erythrocyte membranes and regions of sickle cell membranes devoid of Heinz bodies display an uninterrupted staining of band 3. Similarly, ankyrin and glycophorin are periodically seen to aggregate at Heinz body sites, but the degree of colocalization is lower than for band 3. These data demonstrate that the binding of denatured hemoglobin to the membrane forces a redistribution of several major membrane components.

Original languageEnglish (US)
Pages (from-to)1155-1160
Number of pages6
JournalJournal of Clinical Investigation
Issue number5
StatePublished - 1986

ASJC Scopus subject areas

  • Medicine(all)


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