Comparative proteomics reveals deficiency of NHE-1 (Slc9a1) in RBCs from the beta-adducin knockout mouse model of hemolytic anemia

Blood Cells Mol Dis. 2011 Aug 15;47(2):85-94. doi: 10.1016/j.bcmd.2011.03.008. Epub 2011 May 18.

Abstract

Hemolytic anemia is one of the most common inherited disorders. To identify candidate proteins involved in hemolytic anemia pathophysiology, we utilized a label-free comparative proteomic approach to detect differences in RBCs from normal and beta-adducin (Add2) knock-out mice. We detected 7 proteins that were decreased and 48 proteins that were increased in the beta-adducin knock-out RBC ghost. Since hemolytic anemias are characterized by reticulocytosis, we compared reticulocyte-enriched samples from phenylhydrazine-treated mice with mature RBCs from untreated mice. Label-free analysis identified 47 proteins that were increased in the reticulocyte-enriched samples and 21 proteins that were decreased. Among the proteins increased in Add2 knockout RBCs, only 11 were also found increased in reticulocytes. Among the proteins decreased in Add2 knockout RBCs, beta- and alpha-adducin showed the greatest intensity difference, followed by NHE-1 (Slc9a1), the sodium-hydrogen exchanger. We verified these mass spectrometry results by immunoblot. This is the first example of a deficiency of NHE-1 in hemolytic anemia and suggests new insights into the mechanisms leading to fragile RBCs. Our use of label-free comparative proteomics to make this discovery demonstrates the usefulness of this approach as opposed to metabolic or chemical isotopic labeling of mice.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Retracted Publication

MeSH terms

  • Amino Acid Sequence
  • Anemia, Hemolytic / chemically induced
  • Anemia, Hemolytic / genetics*
  • Anemia, Hemolytic / metabolism
  • Anemia, Hemolytic / pathology
  • Animals
  • Blotting, Western
  • Calmodulin-Binding Proteins* / deficiency
  • Calmodulin-Binding Proteins* / genetics
  • Cation Transport Proteins / deficiency
  • Cation Transport Proteins / genetics*
  • Disease Models, Animal
  • Erythrocyte Count
  • Erythrocyte Membrane / genetics
  • Erythrocyte Membrane / metabolism
  • Erythrocytes / cytology
  • Erythrocytes / metabolism*
  • Gene Expression Profiling
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Molecular Sequence Data
  • Osmotic Fragility / genetics*
  • Phenylhydrazines / adverse effects*
  • Phenylhydrazines / pharmacology
  • Protein Isoforms / genetics*
  • Protein Isoforms / metabolism
  • Proteomics / methods*
  • Reticulocyte Count
  • Reticulocytes / cytology
  • Reticulocytes / metabolism*
  • Sodium-Hydrogen Exchanger 1
  • Sodium-Hydrogen Exchangers / genetics*
  • Tandem Mass Spectrometry

Substances

  • Calmodulin-Binding Proteins
  • Cation Transport Proteins
  • Phenylhydrazines
  • Protein Isoforms
  • Slc9a1 protein, mouse
  • Sodium-Hydrogen Exchanger 1
  • Sodium-Hydrogen Exchangers
  • adducin
  • phenylhydrazine