title: Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.
abstract: It is now well documented that peptides with enhanced or alternative functionality (termed cryptides) can be liberated from larger, and sometimes inactive, proteins. A primary example of this phenomenon is the oxygen-transport protein hemoglobin. Aside from respiration, hemoglobin and hemoglobin-derived peptides have been associated with immune modulation, hematopoiesis, signal transduction and microbicidal activities in metazoans. Likewise, the functional equivalents to hemoglobin in invertebrates, namely hemocyanin and hemerythrin, act as potent immune effectors under certain physiological conditions. The purpose of this review is to evaluate the true extent of oxygen-transport protein dynamics in innate immunity, and to impress upon the reader the multi-functionality of these ancient proteins on the basis of their structures. In this context, erythrocyte-pathogen antibiosis and the immune competences of various erythroid cells are compared across diverse taxa.
authors: Department of Biosciences, College of Science, Swansea University, Singleton Park, Swansea, Wales, SA2 8PP, UK. c.j.coates@swansea.ac.uk.
authors: Christopher J
authors: CJ
authors: Coates
authors: Institut für Molekulare Biophysik, Johannes Gutenberg-Universität Mainz, Jakob Welder-Weg 28, 55128, Mainz, Germany.
authors: Heinz
authors: H
authors: Decker
mesh_terms: D000818:Animals; D001692:Biological Transport; D006422:Hemerythrin / Q000276:immunology*; D006433:Hemocyanins / Q000276:immunology*; D006454:Hemoglobins / Q000276:immunology*; D006801:Humans; D007113:Immunity, Innate; D010100:Oxygen / Q000378:metabolism*
chemical_list: D006422:Hemerythrin; D006454:Hemoglobins; D006433:Hemocyanins; D010100:Oxygen
keywords: Antimicrobial peptides; Enzyme promiscuity; Erythrocytes; Innate immunity; Metabolism; Myoglobin; Phenoloxidase; Redox