Osmotic resistance of high-density erythrocytes in transglutaminase 2-deficient mice

Francesca Bernassola, Giovanna Boumis, Marco Corazzari, Giuseppe Bertini, Gennaro Citro, Richard A. Knight, Gino Amiconi, Gerry Melino

Research output: Contribution to journalArticlepeer-review


Transglutaminase 2 (TGase 2) is a Ca2+-dependent enzyme responsible for the posttransttranslational modification of proteins by transamidation of specific polypeptide-bound glutamine residues. Elevating the intracellular concentration of Ca2+-ions in human erythrocytes leads to the formation of cytoskeletal and cytoplasmic protein polymers. The Ca2+-dependent TGase 2-dependent cross-linking activity has been proposed for its involvement in erythrocyte aging, by inducing irreversible modification of their cell shape and deformability. Accordingly, we found that high-density ("old") TGase 2-/- red blood cells (RBCs) were more resistant to osmotic stress-induced hemolysis than those from wild type mice. In addition, elevating the intracellular concentration of Ca2+ by treatment of total RBCs with ionophore A23187 resulted in enhanced resistance of TGase 2-deficient erythrocytes compared to their normal counterpart. These findings indicate that TGase 2 may have a role in regulating structural flexibility of RBCs, possibly affecting their life span in physiopathological conditions, such as erythrocyte senescence, which are accompanied by increases in intracellular Ca2+ concentration.

Original languageEnglish
Pages (from-to)1123-1127
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number5
Publication statusPublished - 2002


  • Cell fragility
  • Cell shape
  • Erythrocytes
  • Intracellular calcium
  • Osmotic resistance
  • Red blood cells
  • Transglutaminase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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