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Original Article

Biochemistry of ATP-dependent red cell membrane shape change

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Pages 139-144 | Published online: 08 Jul 2009

References

  • Allan D., Michcll R. H. A calcium-activated polyphos-phoinositide phosphodiesterasc in the plasma membrane of human and rabbit erythrocyte. Biochim. Biophys. Acta 1978; 508: 277–286
  • Allan D, Thomas P., Michcll R. H. Rapid trans-hilaycr diffusion of 1,2-diacylglycerol and its relevance to control of membrane curvature. Nature 1978; 276: 289–290
  • Avruch J., Fairbanks G., Crapo L. M. Regulation of plasma membrane protein phosphorylation in two mammalian cell types. J. Cell. Physiol 1976; 89: 815–826
  • Birchmeier W., Singer S. I. On the mechanism of ATP-induccd shape changes in human erythrocyte membranes. II. The role of ATP. J. Cell Biol 1977; 73: 647–659
  • Buckley J. T. Properties of human crythrocyte phospho-tidylinoritol kinase and inhibition by adenosine. ADP. and related compounds. Biochim. Biophys. Actu 1977; 498: 1–9
  • Evans E. A., Hochmuth R. M. A solid-liquid composite model of the red cell membrane. J. Membrane Biol 1977; 30: 351–362
  • Fairbanks G., Avruch J., Dino J. E., Patel V. P. Phosphorylation and dcphosphorylation of spectrin. J. Supramolec. Struct, 9: 97–112
  • Fairhanks G., Steck T. L., Wallach D. F.H. Electrophoretic analysis of the major polypeptide of the human erythrocyte mcmbrane. Biochemistry 1971; 10: 2606–2617
  • Garrett N. E., Garrett R. J.B., Talwalker R. T., Lester R. L. Rapid breakdown of diphosphoinositide and triphosphoinositidc in erythrocyte membranes. J. Cell Physiol 1976; 87: 63–70
  • Garrett R. J.B., Redman C. M. Localization of cnzymes involved in polyphosphoinositide metabolism on thc cytoplasmic surface of the human erythrocyte membrane. Biochim. Biophys. Acta 1975; 382: 58–64
  • Haest C. W.M., Plasa G., Kamp D., Deutickc B. Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane,. Biochim. Biophys. Acta 1978; 509: 21–32
  • Hayashi H., Jarrett H. W., Penniston J. T. Peripheral proteins and smooth membrane from erythrocyte ghost. Segregation of ATP-utilizing enzymes into smooth membrane. J. Cell Biol 1978; 76: 105–115
  • Hokin L. E., Hokin M. R. The incorporation of 32P from (γ-32P] adenosine triphosphate into polyphos-phoinositidcs and phosphatidic acid in Erythrocyte membranes. Biochim. Biophys. Acta 1964; 84: 563–575
  • Johnson R. M., Taylor G., Meyer D. B. Shape and volume changes in erythrocyte ghosts and spectrin-actin networks. J. Cell Biol 1980; 86: 371–376
  • Kirkpatrick F. H. Spectrin: Current understanding of its physical. biochemical, and functional properties. Life Sciences 1976; 19: 1–18
  • Korn E. D. Biochemistry of actomyosin-dependent cell motility. Proc. Natn. Acad. Sci. USA 1978; 75: 588–599
  • Lux S. E. Spectrin-actin membrane skeleton of normal and ahnormal red blood cells. Semin. Hematol 1979; 16: 21–51
  • Nakao M., Nakao T., Tatibana M., Yoshikawa H. Shape transformation of erythrocyte ghosts on addition of adenosine triphosphate to the medium. J. Biochem. (Tokyo) 1964; 47: 694–695
  • Patel V. P., Fairbanks G. Spectrin phosphorylation and shape change of human erythrocyte ghosts. J. Cell Biol 1981; 88: 430–440
  • Shectz M. P., Sawyer D., Jackowski S. The ATP-dependent red cell membrane shape change. A molecular explanation. The Red Cell, G. J. Brewer. Alan R. Liss, New York 1978; 431–450
  • Sheetz M. P., Singer S. J. On the mechanism of ATP-induced shape changes in human erythrocyte membranes. I. The role of the Spectrin complex. J. Cell Biol 1977; 73: 636–646
  • Weed R. I., La Celle P. L., Merrill E. W. Metabolic dependence of red cell deformability. J. Clin. Invest 1969; 48: 795–809

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