Hemoglobin polymorphism in the deer mouse,Peromyscus maniculatus

Rasmussen, David I.; Jensen, J. Neil; Koehn, Richard K.

doi:10.1007/bf01458453

Cited by 19 publications

(4 citation statements)

References 10 publications

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“…However, in natural populations of deer mice, the frequency of different Hb structural variants and the intraerythrocytic DPG/Hb ratio both covary with altitude (Snyder, 1982), which makes it difficult to disentangle the relative contributions of structural and regulatory factors to adaptive altitudinal variation in blood-O 2 affinity. There would seem to be ample scope for genetically based variation in Hb-O 2 affinity as electrophoretic surveys of deer mouse populations across western North America have revealed extremely high levels of allelic polymorphism at multiple -and -globin genes (Rasmussen et al, 1968;Snyder, 1978;Snyder et al, 1988). More recently, genomic studies have characterized the complete globin gene repertoire of deer mice (Hoffmann et al, 2008b;, and surveys of polymorphism at the nucleotide level have revealed the specific amino acid changes that distinguish the previously characterized -and -globin electromorphs (Storz et al, 2007;Storz and Kelly, 2008;Storz et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Genetic differences in hemoglobin function between highland and lowland deer mice

Storz

Runck

Moriyama

et al. 2010

Journal of Experimental Biology

130

173

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SUMMARY In high-altitude vertebrates, adaptive changes in blood–O2 affinity may be mediated by modifications of hemoglobin (Hb) structure that affect intrinsic O2 affinity and/or responsiveness to allosteric effectors that modulate Hb–O2 affinity. This mode of genotypic specialization is considered typical of mammalian species that are high-altitude natives. Here we investigated genetically based differences in Hb–O2 affinity between highland and lowland populations of the deer mouse (Peromyscus maniculatus), a generalist species that has the broadest altitudinal distribution of any North American mammal. The results of a combined genetic and proteomic analysis revealed that deer mice harbor a high level of Hb isoform diversity that is attributable to allelic polymorphism at two tandemly duplicated α-globin genes and two tandemly duplicated β-globin genes. This high level of isoHb diversity translates into a correspondingly high level of interindividual variation in Hb functional properties. O2 equilibrium experiments revealed that the Hbs of highland mice exhibit slightly higher intrinsic O2 affinities and significantly lower Cl– sensitivities relative to the Hbs of lowland mice. The experiments also revealed distinct biochemical properties of deer mouse Hb related to the anion-dependent allosteric regulation of O2 affinity. In conjunction with previous findings, our results demonstrate that modifications of Hb structure that alter allosteric anion sensitivity play an important role in the adaptive fine-tuning of blood–O2 affinity.

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Section: Introductionmentioning

confidence: 99%

Genetic differences in hemoglobin function between highland and lowland deer mice

Storz

Runck

Moriyama

et al. 2010

Journal of Experimental Biology

130

173

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“…Recent publications (Thompson et al, 1966;Foreman, 1968;Rasmussen et al, 1968; Self A., 1968) have revealed not only hemoglobin variation between species of the same genus but also the occurrence of polymorphism within a given species in the order Rodentia. This type of variation, however, is not always the case, as there is a remarkable homogeneity between the hemoglobins of Microchiroptera (Manwell and Kerst, 1966; Valdivieso et al, 1969; this study).…”

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confidence: 99%

Hemoglobin electrophoresis in the systematics of bats (Microchiroptera) /

Tamsitt¹,

Valdivieso²

1969

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Electrophoresis is a most useful procedure for systematically comparing proteins of different organisms, and data from electrophoretic studies of blood proteins have aided in the clarification of phylogenetic relationships and in grouping higher taxonomic categories (Foreman, 1960; Dessauer, 1966; Johnson, 1968). Hemoglobins, unlike some serum proteins, are not affected by diet, age, reproductive state, temperature or other variables. There are, however, few electrophoretic data on bat hemoglobin. Manwell and Kerst (1966) and Mitchell (1966) found considerable individual variation and only minor differences between species in the hemoglobins of temperate bats of the family Vespertilionidae. Valdivieso et al. (1969) compared electrophoretic properties of hemoglobin from Puerto Rican bats of the families Phyllostomatidae, Vespertilionidae and Molossidae and found differences and similarities correlated with taxonomic affinity. Although hemoglobins of closely related species were indistinguishable, Valdivieso et al. (op. cit.) concluded that hemoglobin electrophoresis may be used to add additional evidence to estimates of relationships derived from traditional criteria. Two distinct electrophoretic phenotypes of hemoglobin occur in bats of the family Vespertilionidae (Manwell and Kerst, op. cit.; Mitchell, op. cit.; Valdivieso et al., op.

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“…Hemoglobin polymorphism has been reported in natural populations of P. boylii rowleyi in Arizona (Rasmussen et al, 1968). Polymorphism or geographic variation was not observed within or among populations of P. boylii, P. polius, and P. attwateri, but some interspecific differences were observed (Fig.…”

Section: Protein Variationmentioning

confidence: 82%