The erythrocyte skeletons of beta-adducin deficient mice have altered levels of tropomyosin, tropomodulin and EcapZ

FEBS Lett. 2004 Oct 8;576(1-2):36-40. doi: 10.1016/j.febslet.2004.08.057.

Abstract

The erythrocyte membrane cytoskeleton is organized as a polygonal spectrin network linked to short actin filaments that are capped by adducin at the barbed ends. We have constructed a mouse strain deficient in beta-adducin having abnormal erythrocytes. We show here that the levels of several skeletal proteins from beta-adducin mutant erythrocytes are altered. In fact, CapZ, the main muscle actin-capping protein of the barbed ends that in the erythrocytes is cytoplasmic, is 9-fold upregulated in mutant skeletons of erythrocytes suggesting a compensatory mechanism. We also detected upregulation of tropomodulin and downregulation of alpha-tropomyosin and actin. In addition, purified adducin can be re-incorporated into adducin-deficient ghosts.

MeSH terms

  • Actins / metabolism*
  • Animals
  • Calmodulin-Binding Proteins / deficiency*
  • Calmodulin-Binding Proteins / metabolism*
  • Carrier Proteins / metabolism*
  • Down-Regulation
  • Erythrocyte Membrane / chemistry*
  • Erythrocyte Membrane / genetics
  • Erythrocyte Membrane / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Microfilament Proteins / metabolism*
  • Protein Folding
  • Tropomodulin
  • Tropomyosin / metabolism*
  • Up-Regulation

Substances

  • Actins
  • Calmodulin-Binding Proteins
  • Carrier Proteins
  • Microfilament Proteins
  • Tmod1 protein, mouse
  • Tropomodulin
  • Tropomyosin
  • adducin