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

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High-altitude adaptations in vertebrate hemoglobins. In: Oxygen Delivery at High Altitude: An Integrated Perspective. / Weber, Roy E.

I: Respiratory Physiology & Neurobiology , Bind 158, 2007, s. 132-142.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

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@article{23fb0c075fd74709a607618f81897bf7,
title = "High-altitude adaptations in vertebrate hemoglobins.: In: Oxygen Delivery at High Altitude: An Integrated Perspective",
abstract = "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{\textquoteright}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 ({\textquoteleft}Tense{\textquoteright}) or the high-affinity ({\textquoteleft}Relaxed{\textquoteright}) 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.",
author = "Weber, {Roy E.}",
year = "2007",
language = "English",
volume = "158",
pages = "132--142",
journal = "Respiratory Physiology & Neurobiology",
issn = "1569-9048",
publisher = "Elsevier BV",

}

RIS

TY - JOUR

T1 - High-altitude adaptations in vertebrate hemoglobins.

T2 - In: Oxygen Delivery at High Altitude: An Integrated Perspective

AU - Weber, Roy E.

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

M3 - Review

VL - 158

SP - 132

EP - 142

JO - Respiratory Physiology & Neurobiology

JF - Respiratory Physiology & Neurobiology

SN - 1569-9048

ER -