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The Primary Role of Fibrinogen-Related Proteins in Invertebrates Is Defense, Not CoagulationHanington P.C. · Zhang S.-M.
Center for Evolutionary and Theoretical Immunology, Department of Biology, University of New Mexico, Albuquerque, N. Mex., USA Corresponding Author
Dr. Si-Ming Zhang
Center for Evolutionary and Theoretical Immunology
Department of Biology, MSC03 2020, University of New Mexico
Albuquerque, NM 87131 (USA)
Tel. +1 505 277 4589, Fax +1 505 277 0304, E-Mail email@example.com
In vertebrates, the conversion of fibrinogen into fibrin is an essential process that underlies the establishment of the supporting protein framework required for coagulation. In invertebrates, fibrinogen-domain-containing proteins play a role in the defense response generated against pathogens; however, they do not function in coagulation, suggesting that this role has been recently acquired. Molecules containing fibrinogen motifs have been identified in numerous invertebrate organisms, and most of these molecules known to date have been linked to defense. Moreover, recent genome projects of invertebrate animals have revealed surprisingly high numbers of fibrinogen-like loci in their genomes, suggesting important and perhaps diverse functions of fibrinogen-like proteins in invertebrates. The ancestral role of molecules containing fibrinogen-related domains (FReDs) with immunity is the focus of this review, with emphasis on specific FReDs called fibrinogen-related proteins (FREPs) identified from the schistosome-transmitting mollusc Biomphalaria glabrata. Herein, we outline the range of invertebrate organisms FREPs can be found in, and detail the roles these molecules play in defense and protection against infection.
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