2011
DOI: 10.1002/9781118105771.ch9
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Transglutaminase‐Mediated Remodeling of the Human Erythrocyte Membrane Skeleton: Relevance for Erythrocyte Diseases with Shortened Cell Lifespan

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Cited by 3 publications
(5 citation statements)
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“…As a result, in Ca 2+ overloaded RBCs formation of numerous polymeric protein complexes such as Glut1-adducin-dematin adducts as well as cross-linked complexes of Band 3-ankyrin-spectrin and glycophorin C -band 4.1-p55 occurs [85]. This Ca 2+ induced remodelling of the cytoskeletal structure and concomitant changes in cell shape and membrane plasticity are suggested to contribute to premature RBC clearance.…”
Section: Ca2+-sensitive Proteins In Rbcsmentioning
confidence: 99%
See 1 more Smart Citation
“…As a result, in Ca 2+ overloaded RBCs formation of numerous polymeric protein complexes such as Glut1-adducin-dematin adducts as well as cross-linked complexes of Band 3-ankyrin-spectrin and glycophorin C -band 4.1-p55 occurs [85]. This Ca 2+ induced remodelling of the cytoskeletal structure and concomitant changes in cell shape and membrane plasticity are suggested to contribute to premature RBC clearance.…”
Section: Ca2+-sensitive Proteins In Rbcsmentioning
confidence: 99%
“…Cross-linked polymers have been observed in RBCs of patients with SCD suggesting hyperactivation of transglutaminase [85]. …”
Section: Ca2+ Dysbalance and Haemolytic Anaemiamentioning
confidence: 99%
“…If Ca ++ accumulates, many harmful results occur, including activation of the protease calpain, activation of a K + efflux channel (the Gardos channel), inhibition of flippase/activation of scramblase, vesicle formation, transglutaminase activation [30], and decreased deformability. Ca ++ -dependent pathways are important for RBC in some disease states such as sickle cell disease and may contribute to RBC senescence [31].…”
Section: Biology Of Red Blood Cell Survivalmentioning
confidence: 99%
“…Hemoglobin (Hb)-Köln disease is one of the hemoglobinopathies as a result of mutation of the b-globin of Hb and is characterized by changes in cell shape, increased density, and also by a loss of deformability. When cell membranes were isolated from erythrocytes of a patient with Hb-Köln disease (neither parent had the disease), the presence of high MW-crosslinked membrane structures, such as were found in the calcium-enriched model described above, was demonstrated (26). It is not difficult to conclude that the characteristic cell changes were caused by anything other than TG2-mediated formation of crosslinked supramolecular membrane proteins and that the resultant stiffening of the erythrocyte membrane by these polymers contributes to the extra-rapid clearing of erythrocytes from the circulation and hence, the shortened lifespan of Hb-Köln erythrocytes, from 120 to 31 d (26).…”
Section: The Human Erythrocyte Paradigm and Hemoglobin-köln Diseasementioning
confidence: 92%
“…Inasmuch as we currently do not have any means of hydrolyzing isopeptide crosslinks between proteins, detailed analysis of such large structures presents a formidable analytic problem. A modicum of success to identify the constituent molecules in such large crosslinked assemblies can be achieved by using immunoassays and mass spectrometry, both of which have their limitations (26).…”
Section: The Human Erythrocyte Paradigm and Hemoglobin-k öLn Diseasementioning
confidence: 99%