| First Author | Bernassola F | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 291 |
| Issue | 5 | Pages | 1123-7 |
| PubMed ID | 11883932 | Mgi Jnum | J:75566 |
| Mgi Id | MGI:2177073 | Doi | 10.1006/bbrc.2002.6558 |
| Citation | Bernassola F, et al. (2002) Osmotic resistance of high-density erythrocytes in transglutaminase 2-deficient mice. Biochem Biophys Res Commun 291(5):1123-7 |
| abstractText | Transglutaminase 2 (TGase 2) is a Ca(2+)-dependent enzyme responsible for the posttransttranslational modification of proteins by transamidation of specific polypeptide-bound glutamine residues. Elevating the intracellular concentration of Ca(2+)-ions in human erythrocytes leads to the formation of cytoskeletal and cytoplasmic protein polymers. The Ca(2+)-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(minus sign/minus sign) 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 Ca(2+) 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 Ca(2+) concentration. |
