Abstract
The copper-containing hemocyanins are proteins responsible for the binding, transportation and storage of dioxygen within the blood (hemolymph) of many invertebrates. Several additional functions have been attributed to both arthropod and molluscan hemocyanins, including (but not limited to) enzymatic activity (namely phenoloxidase), hormone transport, homeostasis (ecdysis) and hemostasis (clot formation). An important secondary function of hemocyanin involves aspects of innate immunity—such as acting as a precursor of broad-spectrum antimicrobial peptides and microbial/viral agglutination. In this chapter, we present the reader with an up-to-date synthesis of the known functions of hemocyanins and the structural features that facilitate such activities.
This chapter is dedicated to the work and fond memory of the late Professor Heinz Decker (1950–2018).
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Acknowledgements
We should like to thank Prof Andrew Rowley (Swansea University) for providing comments on the text. No direct funding was provided to undertake this review; however, the content was presented and discussed at the SafeAqua workshop on Invertebrate Immunology held in Thailand, July 2019. The SafeAqua project has received funding from the European Union’s Horizon 2020 research and innovation programme under the grant agreement No. 734486 (CJC is the PI for Swansea University).
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Coates, C.J., Costa-Paiva, E.M. (2020). Multifunctional Roles of Hemocyanins. In: Hoeger, U., Harris, J. (eds) Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins. Subcellular Biochemistry, vol 94. Springer, Cham. https://doi.org/10.1007/978-3-030-41769-7_9
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