Band 3/Complement-mediated Recognition and Removal of Normally Senescent and Pathological Human ErythrocytesArese P. · Turrini F. · Schwarzer E.
Department of Genetics, Biology and Biochemistry, University of Torino Medical School, Torino Corresponding Author
Band 3 modifications that normally occur during physiological red blood cell (RBC) senescence in humans, and occasionally in pathological conditions are described in the context of their role in enhancing RBC recognition and phagocytic removal. Band 3 modifications are mostly due to oxidative insults that gradually accumulate during the RBC lifespan or impact massively in a shorter time period in pathological conditions. The oxidative insults that impact on the RBC, the protective mechanisms that counteract those damages and the phenotypic modifications that accumulate during the RBC lifespan are described. It is shown how specific oxidative as well as non-oxidative band 3 modifications enhance RBC membrane affinity for normally circulating anti-band 3 antibodies, and how membrane-bound anti-band 3 antibodies bring about a limited complement activation and membrane deposition of complement C3 fragments. The partially covalent complexes between anti-band 3 antibodies and complement C3 fragments are very powerful opsonins readily recognized by the CR1 complement receptor on the phagocyte. Band 3 modifications typically encountered in old RBCs have crystallized to a number of band 3-centered models of RBC senescence. One of those band 3-centered models, the so-called ‘band 3/complement RBC removal model’ first put up by Lutz et al. is discussed in more detail. Finally, it is shown how the genetic deficiency of glucose-6-phosphate dehydrogenase (G6PD) plus fava bean consumption, and a widespread RBC parasitic disease, P. falciparum malaria, may lead to massive and rapid destruction of RBCs by a mechanism comparable to a dramatic, time-compressed enhancement of normal RBC senescence.
© 2005 S. Karger AG, Basel
Department of Genetics, Biology and Biochemistry
University of Torino Medical School, Torino
Via Santena 5 bis, 10126 Torino (Italy)
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Accepted: October 20, 2005
Number of Print Pages : 14
Number of Figures : NIL, Number of Tables : NIL, Number of References : NIL
Cellular Physiology and Biochemistry (International Journal of Experimental Cellular Physiology, Biochemistry andPharmacology)
Vol. 16, No. 4-6, Year 2005 (Cover Date: 2005)
Journal Editor: F. Lang, Tübingen
ISSN: 1015–8987 (print), 1421–9778 (Online)
For additional information: http://www.karger.com/journals/cpb