Hemoglobins from Bats (Myotis myotis and Rousettus aegyptiacus): A Possible Example of Molecular Adaptation to Different Physiological Requirements

Condò, Saverio G.; El-Sherbini, Said; Shehata, Yousef M.; Corda, Marcella; Pellegrini, Maria Grazia; Brix, Ole; Giardina, Bruno

doi:10.1515/bchm3.1989.370.2.861

Cited by 11 publications

(3 citation statements)

References 12 publications

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“…Otherwise, the protein's tertiary structure will be changed and oxygen affinity will be lower at high temperature. Certainly, different bat species have different physiological requirements, so their Hb function should also be variable (Condo et al 1989). Flight modes vary with habitat, foraging behavior, and diet, and different flight modes have different energy requirements (Norberg and Rayner 1987).…”

Section: Discussionmentioning

confidence: 99%

“…During flight, bats' bodies generate a lot of heat, and because their Hb has evolved low temperature sensitivity, it functions normally when body temperature rises (Arevalo et al 1991). In the order Chiroptera, different bat species also have different physiological needs, and their heat sensitivity also differs (Condo et al 1989). According to Arevalo et al (1991), temperature coefficients are -5.98 Kcal mol -1 in Rhinolophus ferrumequinum, -6.68 Kcal mol -1 in Miniopterus schreibersi, and -7.39 Kcal mol -1 for Pipistrellus pipistrellus, which are distinctly lower than the range of values (-12 to -15 Kcal mol -1 ) reported for the hemoglobin of other mammals.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Cloning and Evolutionary Analysis of Hemoglobin α-Chain Genes in Bats

et al. 2009

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Bats are the only mammals with the capacity for powered flight. When flying, they need abundant energy and oxygen. According to previous works, the hemoglobin (Hb) oxygen loading function of bats is insensitive to variations in body temperature, although different bat species have different heat sensitivity. We cloned Hb alpha-chain sequences from eight bat species to investigate whether they have different characteristics. We found that Hb in the bat lineages is under purifying selection, which accords with the importance of its function in bats. Three turn regions in bat Hb, however, have distinct evolutionary rates compared with those of other mammals, and the codons in these regions have an accelerated rate of evolution. These codons are under divergent selection in bats. These changes in Hb may have occurred in response to the physiological requirements of the species concerned, as adaptations to different lifestyles.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Evolutionary Analysis of Hemoglobin α-Chain Genes in Bats

et al. 2009

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“…The suborder Megachiroptera includes a single family, Pteropodidae; these are blossom-and fruit-eating bats and flying foxes that live mainly in the tropics and subtropics of the Old World. Megachiroptera may be closely related to primates (Pettigrew et al 1989) and although mitochondrial and nuclear genomic studies do not entirely reject a monophyletic origin for Megachiroptera and Microchiroptera (Teeling et al 2000), the haemoglobin systems of the two suborders seem to exemplify molecular adaptation to the different physiological requirements of the two taxa (Condo et al 1989). The red blood cells (RBC) of bats are anucleated and morphologically similar to those of other mammalian species (Riedesel 1977;O'Brien and Endean 2000), but the Megachiroptera are unique in having to respond to very high demands for oxygen supply; during flight the oxygen demand may exceed 30 times that of basal resting conditions (Thomas and Suthers 1972).…”

Section: Introductionmentioning

confidence: 99%

Oxidant Defence in the Red Blood Cells of the Greyheaded Flying Fox, Pteropus poliocephalus

O'Brien¹,

Ogawa

Agar

2001

Comparative Haematology International

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The red blood cells (RBC) of bats (Order Chiroptera) are morphologically similar to those of other mammals, but the suborder Megachiroptera are unique in responding to very high demands for oxygen supply, more than 30 times that of resting conditions. Although greater efficiency of these cells to transport oxygen is advantageous to the animal, it could potentially expose the RBC to higher than average risk of oxidant damage. The aim of the present study was to investigate the capacity of RBCs of Pteropus poliocephalus, the greyheaded flying fox, to defend itself against oxidant stress. RBC of flying fox and human were challenged with 2,2'-azobis(2-amidinopropane) dihydrochloride (AAPH). The RBC from the two species were found to have similar reduced glutathione (GSH) reduction kinetics and succumbed to haemolysis at similar rates. However, haemoglobin oxidation was much faster in the flying fox suggesting that the RBC of flying fox may not enjoy as good protection as those of humans in the event of an oxidant stress.

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Vertebrate Hemoglobins

Ingermann¹

1997

Comprehensive Physiology

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Hemoglobins from Bats (Myotis myotis and Rousettus aegyptiacus): A Possible Example of Molecular Adaptation to Different Physiological Requirements

Cited by 11 publications

References 12 publications

Molecular Cloning and Evolutionary Analysis of Hemoglobin α-Chain Genes in Bats

Molecular Cloning and Evolutionary Analysis of Hemoglobin α-Chain Genes in Bats

Oxidant Defence in the Red Blood Cells of the Greyheaded Flying Fox, Pteropus poliocephalus

Vertebrate Hemoglobins

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