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Integrative and Comparative Biology Advance Access originally published online on June 6, 2007
Integrative and Comparative Biology 2007 47(4):662-665; doi:10.1093/icb/icm039
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© The Author 2007. Published by Oxford University Press on behalf of the Society for Integrative and Comparative Biology. All rights reserved. For permissions please email: journals.permissions@oxfordjournals.org.

Hemocyanins and the immune response: defense against the dark arts

Nora B. Terwilliger1
Oregon Institute of Marine Biology and Department of Biology, University of Oregon, Charleston, OR 97420 USA

Correspondence: 1E-mail: nterwill{at}uoregon.edu

The innate immune response is a conserved trait shared by invertebrates and vertebrates. In crustaceans, circulating hemocytes play significant roles in the immune response, including the release of prophenoloxidases. Activated phenoloxidase (tyrosinase) participates in encapsulation and melanization of foreign organisms as well as sclerotization of the new exoskeleton after wound-repair or molting. Hemocyanin functions as a phenoloxidase under certain conditions and thus also participates in the immune response and molting. The relative contributions of hemocyte phenoloxidase and hemocyanin in the physiological ratio at which they occur in hemolymph have been investigated in the crab Cancer magister. Differences in activity, substrate affinity, and catalytic ability between the two enzymes indicate that hemocytes are the predominant source of phenoloxidase activity in crabs. In contrast, hemocyanin is the primary source of phenoloxidase activity in isopods and chelicerates whose hemocytes show no phenoloxidase activity. Quantitative PCR studies on the distribution of prophenoloxidase mRNA in the tissues of Carcinus maenas showed little effect relative to salinity stress. Phylogenetic analysis of hemocyanin, phenoloxidase, and other members of this arthropod gene family are consistent with the possibility that a common ancestral molecule had both phenoloxidase and oxygen-binding capabilities.


From the symposium "Integrative and Evolutionary Physiology of Copper Proteins: From Molecules to Organisms in their Environment" presented at the First International Congress of Respiratory Biology, August 14–16, 2006, at Bad Honnef/Bonn, Germany.


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