Evolution of Haemoglobin Function: Molecular Adaptations to Environment

Wells, R. M. G.

doi:10.1046/j.1440-1681.1999.03091.x

Cited by 29 publications

(11 citation statements)

References 23 publications

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“…In fact the Hbs of these animals display values of oxygenation enthalpy in the physiological pH range, much less exothermic than those reported for human adults [1] and other mammalian species [6]. This property has been tentatively related to a mechanism of adaptation to marked variations of the temperature of their habitat [5,8,25].…”

Section: Discussionmentioning

confidence: 84%

Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula

Clementi¹,

Petruzzelli

Filippucci

et al. 2003

Pflugers Arch - Eur J Physiol

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The oxygen binding properties of Dryomys nitedula hemoglobin (Hb) were investigated as a function of pH both in the absence and in the presence of its physiological cofactors (i.e. chloride ions and 2,3-biphosphoglyceric acid) and at different temperatures. Moreover, the alpha- and beta-chains of the Dryomys Hb were partially sequenced. The results obtained show that the effects of Bohr protons, chloride ions, organic phosphates and temperature are significantly lower for Dryomys Hb than for human Hb. Thus, the increase in Hb oxygen affinity, resulting from the reduction of red cell organic phosphates and body temperature that occurs during hibernation, is advantageous for loading oxygen at the lung level without compromising oxygen release at the tissues, as could occur if Dryomys Hb had similar functional properties to those of other non-hibernating mammals. Furthermore, it is possible that the reduced Bohr effect may moderate the potential effects of increased CO(2) associated with prolonged apnea on the loading and unloading of oxygen. Moreover, the overall heat of oxygenation (Delta H) for Dryomys Hb is much less exothermic than that of the human Hb and it is completely independent of the 2,3-biphosphoglyceric acid concentration.

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Section: Discussionmentioning

confidence: 84%

Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula

Clementi¹,

Petruzzelli

Filippucci

et al. 2003

Pflugers Arch - Eur J Physiol

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“…Therefore, it is necessary to develop an alternative treatment, which is effective even for diabetic patients with exercise intolerance. Carbon dioxide (CO 2 ) therapy has long been used in Europe as an effective treatment for cardiac disease and skin lesions (Riggs 1960;Goodman et al 1975;Wells 1999). Exposure to CO 2 elevates blood flow and microcirculation in many tissues as well as partially increases O 2 pressure in the local tissues, a phenomenon known as the Bohr effect (Riggs 1960;Wells 1999;Jensen 2004;Izumi et al 2015).…”

Section: Introductionmentioning

confidence: 99%

Transcutaneous carbon dioxide attenuates impaired oxidative capacity in skeletal muscle in hyperglycemia model

Matsumoto

Tanaka²,

Nakanish³

et al. 2019

gpb

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Hyperglycemia impairs oxidative capacity in skeletal muscle. Muscle oxidative capacity is regulated by peroxisome proliferator-activated receptor-γ co-activator-1α (PGC-1α). Transcutaneous carbon dioxide (CO 2 ) enhances PGC-1α expression in skeletal muscle. Therefore, the aim of this study was to clarify the effects of CO 2 therapy on muscle oxidative capacity impaired by streptozotocin (STZ)induced hyperglycemia. Eight-week-old male Wistar rats were randomly divided into 4 groups: control, CO 2 treatment, STZ-induced hyperglycemia, and STZ-induced hyperglycemia treated with CO 2 . STZinduced hyperglycemia resulted in a decrease of muscle oxidative capacity and decreased PGC-1α and cytochrome c oxidase subunit 4 (COX-4) expression levels; while, application of transcutaneous CO 2 attenuated this effect, and enhanced the expression levels of endothelial nitric oxide synthesis (eNOS). These results indicate that transcutaneous CO 2 improves impaired muscle oxidative capacity via enhancement of eNOS and PGC-1α-related signaling in the skeletal muscle of rats with hyperglycemia.

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“…The hemoglobin molecule has evidently been optimized for oxygen binding under vastly different environmental and physiological conditions by the structural and functional divergence of the vertebrate globin chains [1-3]. The tetrameric hemoglobin consists of two α and two β subunits each containing eight alpha helices (A-H), and the amino acids are numbered either from the N-terminus (excluding the N-terminal Met) or according to helical positions.…”

Section: Introductionmentioning

confidence: 99%

The conserved Phe GH5 of importance for hemoglobin intersubunit contact is mutated in gadoid fish

et al. 2014

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BackgroundFunctionality of the tetrameric hemoglobin molecule seems to be determined by a few amino acids located in key positions. Oxygen binding encompasses structural changes at the interfaces between the α1β2 and α2β1 dimers, but also subunit interactions are important for the oxygen binding affinity and stability. The latter packing contacts include the conserved Arg B12 interacting with Phe GH5, which is replaced by Leu and Tyr in the αA and αD chains, respectively, of birds and reptiles.ResultsSearching all known hemoglobins from a variety of gnathostome species (jawed vertebrates) revealed the almost invariant Arg B12 coded by the AGG triplet positioned at an exon-intron boundary. Rare substitutions of Arg B12 in the gnathostome β globins were found in pig, tree shrew and scaled reptiles. Phe GH5 is also highly conserved in the β globins, except for the Leu replacement in the β1 globin of five marine gadoid species, gilthead seabream and the Comoran coelacanth, while Cys and Ile were found in burbot and yellow croaker, respectively. Atlantic cod β1 globin showed a Leu/Met polymorphism at position GH5 dominated by the Met variant in northwest-Atlantic populations that was rarely found in northeast-Atlantic cod. Site-specific analyses identified six consensus codons under positive selection, including 122β(GH5), indicating that the amino acid changes identified at this position may offer an adaptive advantage. In fact, computational mutation analysis showed that the replacement of Phe GH5 with Leu or Cys decreased the number of van der Waals contacts essentially in the deoxy form that probably causes a slight increase in the oxygen binding affinity.ConclusionsThe almost invariant Arg B12 and the AGG codon seem to be important for the packing contacts and pre-mRNA processing, respectively, but the rare mutations identified might be beneficial. The Leu122β1(GH5)Met and Met55β1(D6)Val polymorphisms in Atlantic cod hemoglobin modify the intradimer contacts B12-GH5 and H2-D6, while amino acid replacements at these positions in avian hemoglobin seem to be evolutionary adaptive in air-breathing vertebrates. The results support the theory that adaptive changes in hemoglobin functions are caused by a few substitutions at key positions.

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Evolution of Haemoglobin Function: Molecular Adaptations to Environment

Cited by 29 publications

References 23 publications

Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula

Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula

Transcutaneous carbon dioxide attenuates impaired oxidative capacity in skeletal muscle in hyperglycemia model

The conserved Phe GH5 of importance for hemoglobin intersubunit contact is mutated in gadoid fish

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