Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken

Proceedings of the National Academy of Sciences of the United States of America
Krzysztof B Wicher, Erik Fries

Abstract

Hemoglobin (Hb) released from erythrocytes may cause oxidation of lipids and proteins. Haptoglobin (Hp), which occurs in the plasma of all mammals, binds free Hb and inhibits its oxidative activity. It is not known whether this protective protein also exists in lower vertebrates. By analyzing available genomic sequences, we have found that bony fish, but not more primitive animals, have a gene coding for a protein homologous to mammalian Hp. Furthermore, we show that this protein is present in the plasma of Japanese pufferfish (Takifugu rubripes) and that it binds Hb. These results, together with a phylogenetic analysis, suggest that Hp evolved from a complement-associated protein (mannose-binding lectin-associated serine proteinase, MASP), with the emergence of fish. Surprisingly, we found that both chicken (Gallus gallus) and the Western clawed frog (Xenopus tropicalis) lack the Hp gene. In chicken plasma, however, we identified a different type of Hb-binding protein, PIT54, which has been reported to be a potent antioxidant. PIT54 is a soluble member of the family of scavenger receptor cysteine-rich proteins, and we found that its gene exists only in birds. We also show that the plasma of ostrich (Strutio camelus), a primiti...Continue Reading

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Citations

Oct 9, 2007·Journal of Molecular Evolution·Krzysztof B Wicher, Erik Fries
Oct 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Amit TripathiAlessio Fasano
Apr 16, 2013·Avian Pathology : Journal of the W.V.P.A·Zutao ZhouZili Li
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