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  • 1
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    Physiology: Myoglobin's new clothes (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cossins, Andrew -- Berenbrink, Michael -- England -- Nature. 2008 Jul 24;454(7203):416-7. doi: 10.1038/454416a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18650904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia/*metabolism ; Mice ; Mice, Knockout ; Myoglobin/deficiency/genetics/*metabolism ; Nitric Oxide/*metabolism ; Nitrites/*metabolism ; Oxidation-Reduction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Evolution of oxygen secretion in fishes and the emergence of a complex physiological system (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: We have reconstructed the events that led to the evolution of a key physiological innovation underpinning the large adaptive radiation of fishes, namely their unique ability to secrete molecular oxygen (O2). We show that O2 secretion into the swimbladder evolved some 100 million years after another O2-secreting system in the eye. We unravel the likely sequence in which the functional components of both systems evolved. These components include ocular and swimbladder countercurrent exchangers, the Bohr and Root effects, the buffering power and surface histidine content of hemoglobins, and red blood cell Na+/H+ exchange activity. Our synthesis reveals the dynamics of gains and losses of these multiple traits over time, accounting for part of the huge diversity of form and function in living fishes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berenbrink, Michael -- Koldkjaer, Pia -- Kepp, Oliver -- Cossins, Andrew R -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1752-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK. michaelb@liv.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774753" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Air Sacs/blood supply/*physiology ; Amino Acid Sequence ; Animals ; *Biological Evolution ; Buffers ; Capillaries/physiology ; Choroid/blood supply/physiology ; Diffusion ; Environment ; Erythrocytes/physiology ; Fishes/anatomy & histology/classification/*physiology ; Hemoglobins/chemistry/*metabolism ; Histidine/analysis ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Oxygen/*metabolism ; Oxyhemoglobins/metabolism ; Phylogeny ; Sodium-Hydrogen Antiporter/blood/metabolism ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Evolution of mammalian diving capacity traced by myoglobin net surface charge (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-06-15
    Description: Extended breath-hold endurance enables the exploitation of the aquatic niche by numerous mammalian lineages and is accomplished by elevated body oxygen stores and adaptations that promote their economical use. However, little is known regarding the molecular and evolutionary underpinnings of the high muscle myoglobin concentration phenotype of divers. We used ancestral sequence reconstruction to trace the evolution of this oxygen-storing protein across a 130-species mammalian phylogeny and reveal an adaptive molecular signature of elevated myoglobin net surface charge in diving species that is mechanistically linked with maximal myoglobin concentration. This observation provides insights into the tempo and routes to enhanced dive capacity evolution within the ancestors of each major mammalian aquatic lineage and infers amphibious ancestries of echidnas, moles, hyraxes, and elephants, offering a fresh perspective on the evolution of this iconic respiratory pigment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mirceta, Scott -- Signore, Anthony V -- Burns, Jennifer M -- Cossins, Andrew R -- Campbell, Kevin L -- Berenbrink, Michael -- Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2013 Jun 14;340(6138):1234192. doi: 10.1126/science.1234192.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23766330" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; *Diving ; Evolution, Molecular ; Mammals/*genetics/*physiology ; Models, Biological ; Molecular Sequence Data ; Muscle, Skeletal/chemistry ; Myoglobin/analysis/*chemistry/*classification ; Phylogeny
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Gene Turnover in the Avian Globin Gene Families and Evolutionary Changes in Hemoglobin Isoform Expression (2015)
    Oxford University Press
    Details
    Publication Date: 2015-04-01
    Description: The apparent stasis in the evolution of avian chromosomes suggests that birds may have experienced relatively low rates of gene gain and loss in multigene families. To investigate this possibility and to explore the phenotypic consequences of variation in gene copy number, we examined evolutionary changes in the families of genes that encode the α- and β-type subunits of hemoglobin (Hb), the tetrameric α 2 β 2 protein responsible for blood-O 2 transport. A comparative genomic analysis of 52 bird species revealed that the size and membership composition of the α- and β-globin gene families have remained remarkably constant during approximately 100 My of avian evolution. Most interspecific variation in gene content is attributable to multiple independent inactivations of the α D -globin gene, which encodes the α-chain subunit of a functionally distinct Hb isoform (HbD) that is expressed in both embryonic and definitive erythrocytes. Due to consistent differences in O 2 -binding properties between HbD and the major adult-expressed Hb isoform, HbA (which incorporates products of the α A -globin gene), recurrent losses of α D -globin contribute to among-species variation in blood-O 2 affinity. Analysis of HbA/HbD expression levels in the red blood cells of 122 bird species revealed high variability among lineages and strong phylogenetic signal. In comparison with the homologous gene clusters in mammals, the low retention rate for lineage-specific gene duplicates in the avian globin gene clusters suggests that the developmental regulation of Hb synthesis in birds may be more highly conserved, with orthologous genes having similar stage-specific expression profiles and similar functional properties in disparate taxa.
    Print ISSN: 0737-4038
    Electronic ISSN: 1537-1719
    Topics: Biology
    Published by Oxford University Press
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