Adaptive evolution of hepcidin genes in antarctic notothenioid fishes.

@article{Xu2008AdaptiveEO,
  title={Adaptive evolution of hepcidin genes in antarctic notothenioid fishes.},
  author={Qianghua Xu and C-H Christina Cheng and Peng Hu and Hua Ye and Zuozhou Chen and Lixue Cao and Lei Chen and Yu Shen and Liangbiao Chen},
  journal={Molecular biology and evolution},
  year={2008},
  volume={25 6},
  pages={
          1099-112
        }
}
Hepcidin is a small bioactive peptide with dual roles as an antimicrobial peptide and as the principal hormonal regulator of iron homeostasis in human and mouse. Hepcidin homologs of very similar structures are found in lower vertebrates, all comprise approximately 20-25 amino acids with 8 highly conserved cysteines forming 4 intramolecular disulfide bonds, giving hepcidin a hairpin structure. Hepcidins are particularly diverse in teleost fishes, which may be related to the diversity of aquatic… CONTINUE READING

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Expansion of capacities for iron transport and sequestration reflects plasma volumes and heart mass among white-blooded notothenioid fishes.

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Hepcidin and Its Roles in Fishes

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Antimicrobial Peptides from Fish

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