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Immunostaining-Based Detection of Dynamic Alterations in Red Blood Cell Proteins
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Erythrocyte nitric oxide transport reduced by a submembrane cytoskeletal barrier

Tae H Han1, Andrew Pelling, Tae-Joon Jeon

  • 1Department of Chemical Engineering, 5531 Boelter Hall, University of California, Los Angeles, CA 90095-1592, USA.

Biochimica Et Biophysica Acta
|March 22, 2005
PubMed

Encapsulation of hemoglobin (Hb) within red blood cells (RBCs) preserves nitric oxide (NO) bioactivity. With encapsulation, millimolar concentrations of Hb quench only a fraction of NO bioactivity, whereas mere micromolar concentrations of cell-free Hb completely quench NO bioactivity. A submembrane cytoskeletal barrier has been hypothesized to account for the lowered quenching of NO bioactivity. In order to substantiate this hypothesis, here, the underlying submembrane cytoskeletal barrier was physically reduced and the rate of NO entry into the modified RBC measured. The submembrane cytoskeletal barrier of normal and depleted RBCs was characterized using atomic force microscopy and the lipid to protein ratio measured. The reduction in the submembrane cytoskeletal barrier resulted in an increase in the rate of NO entry. We suggest that the underlying submembrane cytoskeleton may be a key component of RBC mediated regulation of NO bioavailability.

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