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Evolutionary aspects of hemoglobin scavengers
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2010 (English)In: Antioxidants and Redox Signaling, ISSN 1523-0864, E-ISSN 1557-7716, Vol. 12, no 2, 249-259 p.Article, review/survey (Refereed) Published
Abstract [en]

With the evolution of fish, systems appeared for the disposal of the hemoglobin (Hb) that was inevitably released from erythrocytes. Thus, a plasma protein that bound free Hb with great affinity, haptoglobin (Hp), evolved from a protease of the innate immune system. In parallel, other proteins appeared (for example, hemopexin and alpha(1)-microglobulin), which bound and mediated the removal of free heme groups. Remarkably, Hp later disappeared in some vertebrate lineages, suggesting that it could also be disadvantageous. In the avian lineage, a soluble protein evolved, possibly from a scavenger receptor, which in some birds seems to have replaced Hp. Among mammals, multimeric forms of Hp appeared independently at two discrete times, suggesting that this form of the protein confers an advantage on the bearer, possibly by improving resistance to infection.

Place, publisher, year, edition, pages
2010. Vol. 12, no 2, 249-259 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-138203DOI: 10.1089/ars.2009.2760ISI: 000273181600007PubMedID: 19650711OAI: oai:DiVA.org:uu-138203DiVA: diva2:378886
Available from: 2010-12-16 Created: 2010-12-16 Last updated: 2011-06-28Bibliographically approved

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