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Interactions between vertebrate hemoglobins and red cell proteins: Possible roles in regulating cellular metabolism and rheology

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  • Zoofysiologi, Biologisk Institut

Red blood cells (RBCs) play a vital role in vertebrate metabolism. Tissue O2 delivery depends on their O2 transporting properties and rheology, an integral determinant of tissue perfusion. The mechanical characteristics and key metabolic characteristics of RBCs (such as glycolysis rate, pentose phosphate and several ion transport pathways) have themselves been shown to exhibit dependence on haemoglobin(Hb) oxygenation state1. This coupling results, at least partly, from reactions between Hb and RBC membrane proteins, such as the polyanionic N-terminal cytoplasmic domain of Band 3 (cdB3) that binds either to the positively-charged phosphate binding sites of deoxygenated vertebrate Hbs2 at low O2 saturation, or to glycolytic enzymes (like aldolase, GAPDH and PFK) at high O2 saturation, whereby Hb may function as a transducer regulating RBC glycolysis in an O2-dependent manner. The effects of trout, chicken and human cdB3 peptides on O2 binding properties of fish, bird and mammalian Hbs are consistent with such a role in endothermic, but not in ectothermic, vertebrates3. Measurements of the interaction between Hbs and anionic domains of Band 3, other membrane proteins and intracellular proteins (band 4.1, glycophorin, aquaporin, sodium-proton exchanger, actin, tubulin) will be discussed as regards the oxygenation dependence of RBC ion-transporting functions and rheological properties.

OriginalsprogEngelsk
TidsskriftAbstracts / Comparative Biochemistry and Physiology, Part A
Vol/bind146
Nummer4
Sider (fra-til)S160-S161
DOI
StatusUdgivet - 2007

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