Asymmetric Hemoglobins, Their Thiol Content, and Blood Glutathione of the Scalloped Hammerhead Shark, Sphyrna lewini

Dafré, Alcir Luiz; Reischl, Evaldo

doi:10.1016/s0305-0491(96)00215-5

Cited by 13 publications

(3 citation statements)

References 30 publications

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“…Such a scenario is consistent with the fact that Hb multiplicity has also been documented in cartilaginous fish (Fyhn and Sullivan 1975; Mumm et al 1978; Weber et al. 1983; Galderisi et al 1996; Dafre and Reischl 1997). Our results indicate that the common ancestor of ray-finned fish possessed a fairly diverse globin gene repertoire, and in teleosts, this inherited repertoire was further augmented by the TGD, which produced dual sets of α - and β -like globin genes on two paralogous chromosomes.…”

Section: Resultssupporting

confidence: 85%

Whole-Genome Duplication and the Functional Diversification of Teleost Fish Hemoglobins

Opazo

Butts

Nery

et al. 2012

Molecular Biology and Evolution

107

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Subsequent to the two rounds of whole-genome duplication that occurred in the common ancestor of vertebrates, a third genome duplication occurred in the stem lineage of teleost fishes. This teleost-specific genome duplication (TGD) is thought to have provided genetic raw materials for the physiological, morphological, and behavioral diversification of this highly speciose group. The extreme physiological versatility of teleost fish is manifest in their diversity of blood–gas transport traits, which reflects the myriad solutions that have evolved to maintain tissue O2 delivery in the face of changing metabolic demands and environmental O2 availability during different ontogenetic stages. During the course of development, regulatory changes in blood–O2 transport are mediated by the expression of multiple, functionally distinct hemoglobin (Hb) isoforms that meet the particular O2-transport challenges encountered by the developing embryo or fetus (in viviparous or oviparous species) and in free-swimming larvae and adults. The main objective of the present study was to assess the relative contributions of whole-genome duplication, large-scale segmental duplication, and small-scale gene duplication in producing the extraordinary functional diversity of teleost Hbs. To accomplish this, we integrated phylogenetic reconstructions with analyses of conserved synteny to characterize the genomic organization and evolutionary history of the globin gene clusters of teleosts. These results were then integrated with available experimental data on functional properties and developmental patterns of stage-specific gene expression. Our results indicate that multiple α- and β-globin genes were present in the common ancestor of gars (order Lepisoteiformes) and teleosts. The comparative genomic analysis revealed that teleosts possess a dual set of TGD-derived globin gene clusters, each of which has undergone lineage-specific changes in gene content via repeated duplication and deletion events. Phylogenetic reconstructions revealed that paralogous genes convergently evolved similar functional properties in different teleost lineages. Consistent with other recent studies of globin gene family evolution in vertebrates, our results revealed evidence for repeated evolutionary transitions in the developmental regulation of Hb synthesis.

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Section: Resultssupporting

confidence: 85%

Whole-Genome Duplication and the Functional Diversification of Teleost Fish Hemoglobins

Opazo

Butts

Nery

et al. 2012

Molecular Biology and Evolution

107

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“…Nonetheless, some present asymmetric hemoglobins, exhibiting at least three different globin chains in a single-hemoglobin molecule (19,43).…”

Section: Fish Hemoglobinsmentioning

confidence: 99%

“…Thus, the number of isoforms can be significantly elevated by this property, observed both in vivo and in vitro (43,(45)(46)(47). Changes in the relative quantities of different hemoglobins, with the corresponding adjustment of oxygen-binding properties may represent adaptations to environmental factors such as temperature (48).…”

Section: Fish Hemoglobinsmentioning

confidence: 99%

Fish hemoglobins

Souza

Bonilla-Rodriguez

2007

Braz J Med Biol Res

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Vertebrate hemoglobin, contained in erythrocytes, is a globular protein with a quaternary structure composed of 4 globin chains (2 alpha and 2 beta) and a prosthetic group named heme bound to each one. Having myoglobin as an ancestor, hemoglobin acquired the capacity to respond to chemical stimuli that modulate its function according to tissue requirements for oxygen. Fish are generally submitted to spatial and temporal O 2 variations and have developed anatomical, physiological and biochemical strategies to adapt to the changing environmental gas availability. Structurally, most fish hemoglobins are tetrameric; however, those from some species such as lamprey and hagfish dissociate, being monomeric when oxygenated and oligomeric when deoxygenated. Fish blood frequently possesses several hemoglobins; the primary origin of this finding lies in the polymorphism that occurs in the globin loci, an aspect that may occasionally confer advantages to its carriers or even be a harmless evolutionary remnant. On the other hand, the functional properties exhibit different behaviors, ranging from a total absence of responses to allosteric regulation to drastic ones, such as the Root effect.

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