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High-altitude adaptations in vertebrate hemoglobins. In: Oxygen Delivery at High Altitude: An Integrated Perspective

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  • Zoofysiologi, Biologisk Institut
Vertebrates at high altitude are subjected to hypoxic conditions that challenge aerobic metabolism. O2 transport from the respiratory surfaces to
tissues requires matching between the O2 loading and unloading tensions and theO2-affinity of blood, which is an integrated function of hemoglobin’s
intrinsic O2-affinity and its allosteric interaction with cellular effectors (organic phosphates, protons and chloride). Whereas short-term altitudinal
adaptations predominantly involve adjustments in allosteric interactions, long-term, genetically-coded adaptations typically involve changes in the
structure of the haemoglobin molecules. The latter commonly comprise substitutions of amino acid residues at the effector binding sites, the hemeprotein
contacts, or at intersubunit contacts that stabilize either the low-affinity (‘Tense’) or the high-affinity (‘Relaxed’) structures of the molecules.
Molecular heterogeneity (multiple isoHbs with differentiated oxygenation properties) can further broaden the range of physico-chemical conditions
where Hb functions under altitudinal hypoxia. This treatise reviews the molecular and cellular mechanisms that adapt haemoglobin-oxygen affinities
in mammals, birds and ectothermic vertebrates at high altitude.
OriginalsprogEngelsk
TidsskriftRespiratory Physiology & Neurobiology
Vol/bind158
Sider (fra-til)132-142
Antal sider11
ISSN1569-9048
StatusUdgivet - 2007

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