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Goldfish (Carassius auratus) may survive in aquatic environments with low oxygen partial pressures. We investigated the contribution of respiratory proteins to hypoxia tolerance inC. auratus. We determined the complete coding sequence of hemoglobinaandband myoglobin, as well as partial cDNAs from neuroglobin and cytoglobin. | ỊFEBS Journal Globins and hypoxia adaptation in the goldfish Carassius auratus Anja Roesner1 Stephanie A. Mitz1 2 Thomas Hankeln3 and Thorsten Burmester2 1 Institute of Zoology University of Mainz Germany 2 Institute of Zoology University of Hamburg Germany 3 Institute of Molecular Genetics University of Mainz Germany Keywords cytoglobin goldfish hemoglobin myoglobin neuroglobin Correspondence T. Burmester Institute of Zoology University of Hamburg Biozentrum Grindel Martin-Luther-King-Platz 3 D-20146 Hamburg Germany Fax 49 40 42838 3937 Tel 49 40 42838 3913 E-mail thorsten.burmester@uni-hamburg.de Database The nucleotide sequences have been submitted to the GenBank database EMBL Data Bank under accession numbers AM933143 Hba AM933144 Hbp AM747267 Mb1 AM747268 Mb2 AM933145 Ngb and AM933146 Cygb1 Received 6 March 2008 revised 6 May 2008 accepted 15 May 2008 doi 10.1111 j.1742-4658.2008.06508.x Goldfish Carassius auratus may survive in aquatic environments with low oxygen partial pressures. We investigated the contribution of respiratory proteins to hypoxia tolerance in C. auratus. We determined the complete coding sequence of hemoglobin a and b and myoglobin as well as partial cDNAs from neuroglobin and cytoglobin. Like the common carp Cypri-nus carpio C. auratus possesses two paralogous myoglobin genes that duplicated within the cyprinid lineage. Myoglobin is also expressed in nonmuscle tissues. By means of quantitative real-time RT-PCR we determined the changes in mRNA levels of hemoglobin myoglobin neuroglobin and cytoglobin in goldfish exposed to prolonged hypoxia 48 h at Po2 6.7 kPa 8 h at Po2 1.7 kPa 16 h at Po2 6.7 kPa at 20 C. We observed small variations in the mRNA levels of hemoglobin neuroglobin and cytoglobin as well as putative hypoxia-responsive genes like lactate dehydrogenase or superoxide dismutase. Hypoxia significantly enhanced only the expression of myoglobin. However we observed about fivefold higher neuroglobin protein levels in goldfish brain
