Vertebrate Hemoglobins

Ingermann, Rolf L.

doi:10.1002/cphy.cp130106

Cited by 9 publications

(12 citation statements)

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“…Since embryonic/fetal Hbs and adult-expressed Hbs exhibit consistent differences in O 2 - affinity and sensitivity to allosteric regulators (Ingermann 1997), convergence in stage-specific expression also likely entailed convergence in functional properties. Similarly, adult α - and β -globin genes that encode the subunits of cathodic Hbs of European eel and dusky notothen are clearly not 1:1 orthologs (fig.…”

Section: Resultsmentioning

confidence: 99%

“…Relative to air-breathing vertebrates, fish generally contend with far greater vicissitudes of environmental O 2 availability, which is largely because O 2 solubility (and hence, the availability of dissolved O 2 for respiration) varies as a function of water temperature. During ontogeny, regulatory changes in blood-O 2 transport are mediated by the expression of multiple, functionally distinct hemoglobin (Hb) isoforms that are adapted to the particular O 2 -transport challenges encountered by the developing embryo or fetus (in viviparous or oviparous species) and in free-swimming larvae and adults (reviewed by Ingermann 1997; Jensen et al 1998). As in other vertebrates, the developmental regulation of Hb synthesis in fish involves differential expression of duplicated genes that encode the α- and β-chain subunits of distinct tetrameric α 2 β 2 Hb isoforms (Chan et al 1997; Brownlie et al 2003; Maruyama, Yasumasu, and Iuchi 2004; Maruyama, Yasumasu, Naruse, et al 2004; Tiedke et al 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Experimental evidence for some species suggests that regulatory changes in intraerythrocytic Hb isoform composition may play a role in the acclimatization response to environmental hypoxia (e.g., Rutjes et al 2007), but it has not been possible to formulate any broadly consistent empirical generalizations (Weber and Jensen 1988; Weber, 1990, 2000; Ingermann 1997; Wells 2009). A remarkable feature of nearly all anodic Hb isoforms of teleost fish is the Root effect, an extreme reduction in Hb-O 2 binding capacity at low pH, even when blood O 2 tension remains high.…”

Section: Introductionmentioning

confidence: 99%

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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: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…[10][11][12] However, there are three specific points which warrant attention with regard to differences in O 2 and CO 2 transport in elasmobranchs as compared to the basic model. 86 Although it appears that in most cartilaginous fishes urea has a minimal effect on Hb function, 80,86 there are exceptions. While their plasma Na + and Clconcentrations are much lower than seawater values, their plasma is isosmotic with their seawater environment because of the high plasma urea concentrations, typically up to 0.5 M. 85 Urea at these levels usually denatures proteins, but urea concentrations even up to 5 M appear to have minimal effects on Hb-O 2 transport function.…”

Section: The Elasmobranchsmentioning

confidence: 99%

Regulation of erythrocyte function: Multiple evolutionary solutions for respiratory gas transport and its regulation in fish

2019

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Gas transport concepts in vertebrates have naturally been formulated based on human blood. However, the first vertebrates were aquatic, and fish and tetrapods diverged hundreds of millions years ago. Water-breathing vertebrates live in an environment with low and variable O 2 levels, making environmental O 2 an important evolutionary selection pressure in fishes, and various features of their gas transport differ from humans. Erythrocyte function in fish is of current interest, because current environmental changes affect gas transport, and because especially zebrafish is used as a model in biomedical studies, making it important to understand the differences in gas transport between fish and mammals to be able to carry out meaningful studies. Of the close to thirty thousand fish species, teleosts are the most species-numerous group.However, two additional radiations are discussed: agnathans and elasmobranchs.The gas transport by elasmobranchs may be closest to the ancestors of tetrapods. The major difference in their haemoglobin (Hb) function to humans is their high urea tolerance. Agnathans differ from other vertebrates by having Hbs, where cooperativity is achieved by monomer-oligomer equilibria. Their erythrocytes also lack the anion exchange pathway with profound effects on CO 2 transport. Teleosts are characterized by highly pH sensitive Hbs, which can fail to become fully O 2 -saturated at low pH. An adrenergically stimulated Na + /H + exchanger has evolved in their erythrocyte membrane, and plasma-accessible carbonic anhydrase can be differentially distributed among their tissues. Together, and differing from other vertebrates, these features can maximize O 2 unloading in muscle while ensuring O 2 loading in gills. K E Y W O R D Sadrenergically stimulated Na + /H + exchange, anion exchange, Bohr effect, carbonic anhydrase, erythrocyte, oxygen equilibrium curve (OEC), Root effect 2 of 16 | NIKINMAA et Al.3 40 ) stabilize the T-state (these so-called allosteric effectors bind to sites other than the O 2 binding site). The overall OEC of Hb molecules is determined by the probabilities of T-or R-state occurrence; the equilibrium between T-and R-states is virtually instantaneous.F I G U R E 4 O 2 equilibrium curves of rainbow trout (A) at resting plasma pH (7.65) and (B) at pH 7.40, where the Root effect has been induced (ie, O 2 saturation approaches asymptotically a value below full saturation, in this case maximal O 2 saturation is 69%, ie, Root effect 31%; data from 98 )

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“…1,2 In cats, chloride is the major modifier of hemoglobin affinity. [1][2][3][4][5][6] The effect of storage on hemoglobin affinity of cat blood has not been investigated. It was hypothesized because chloride is an inorganic anion that its concentration would not change with storage.…”

Section: Introductionmentioning

confidence: 99%

The effect of storage on the P₅₀ of feline blood

Wong

Haskins

2006

J Vet Emergen Crit Care

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Objective: To determine the effect of storage on the P50 of feline hemoglobin. Design: Prospective, in vitro, laboratory study. Subjects: Venous blood from 4 clinically healthy cats. Measurements: Blood was collected into CPDA‐1 anticoagulant/preservative and maintained at 4°C for 5 weeks. Measurements were made on Days 0, 2, 4, 7, 14, 21, 28, and 35. The blood samples were equilibrated in a tonometer to gas mixtures containing 2.5%, 4%, 5%, or 8% oxygen, with 5% carbon dioxide balance nitrogen; pH was adjusted to 7.4. Chloride, partial pressure of oxygen, and hemoglobin saturation were measured; P50 was calculated. Results: Chloride decreased from 124.3±2.1 to 88.5±1.9 mEq/L immediately after dilution with CPDA‐1, and did not change for the 5 weeks thereafter. The P50 decreased from an average of 35.0±1.2 to between 31 and 32 mmHg after 7 days, and did not change further for 4 weeks thereafter. Conclusions: The decrease in P50 of feline hemoglobin was minor compared with that of blood from species in which 2,3‐diphosphoglycerate (2,3‐DPG) is a major modifier of hemoglobin affinity for oxygen. The decrease in P50 in the present study was attributed to an initial decrease in chloride and a subsequent loss of modest quantities of red cell 2,3‐DPG.

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Vertebrate Hemoglobins

Cited by 9 publications

References 576 publications

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

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

Regulation of erythrocyte function: Multiple evolutionary solutions for respiratory gas transport and its regulation in fish

The effect of storage on the P₅₀ of feline blood

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Vertebrate Hemoglobins

Cited by 9 publications

References 576 publications

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

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

Regulation of erythrocyte function: Multiple evolutionary solutions for respiratory gas transport and its regulation in fish

The effect of storage on the P50 of feline blood

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Resources

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The effect of storage on the P₅₀ of feline blood