PUBLICATION
Globins and hypoxia adaptation in the goldfish, Carassius auratus
- Authors
- Roesner, A., Mitz, S.A., Hankeln, T., and Burmester, T.
- ID
- ZDB-PUB-080616-11
- Date
- 2008
- Source
- The FEBS journal 275(14): 3633-3643 (Journal)
- Registered Authors
- Keywords
- cytoglobin, goldfish, hemoglobin, myoglobin, neuroglobin
- MeSH Terms
-
- Adaptation, Physiological*/genetics
- Amino Acid Sequence
- Animals
- Blotting, Western
- Cell Hypoxia
- Cloning, Molecular
- Fish Proteins/chemistry
- Fish Proteins/genetics
- Fish Proteins/metabolism*
- Gene Expression Regulation
- Globins/chemistry
- Globins/genetics
- Globins/metabolism*
- Goldfish/genetics
- Goldfish/metabolism*
- Hemoglobins/metabolism
- Molecular Sequence Data
- Myoglobin/chemistry
- Myoglobin/metabolism
- Nerve Tissue Proteins/metabolism
- RNA, Messenger/metabolism
- Sequence Homology, Amino Acid
- PubMed
- 18537818 Full text @ FEBS J.
Citation
Roesner, A., Mitz, S.A., Hankeln, T., and Burmester, T. (2008) Globins and hypoxia adaptation in the goldfish, Carassius auratus. The FEBS journal. 275(14):3633-3643.
Abstract
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 alpha and beta and myoglobin, as well as partial cDNAs from neuroglobin and cytoglobin. Like the common carp (Cyprinus 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 Po(2) approximately 6.7 kPa, 8 h at Po(2) approximately 1.7 kPa, 16 h at Po(2) approximately 6.7 kPa) at 20 degrees 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 compared with zebrafish, although there was no significant difference in intrinsic myoglobin levels. These observations suggest that both myoglobin and neuroglobin may contribute to the tolerance of goldfish to low oxygen levels, but may reflect divergent adaptive strategies of hypoxia preadaptation (neuroglobin) and hypoxia response (myoglobin).
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping