Abstract
Hemocyanin (Hc), a copper-containing extracellular multimeric protein, is the major protein component of hemolymph in different arachnid groups. Hc possesses 7 or 8 very well-characterized types of monomers with molecular weights ranging from 70 to 85 kDa, organized in hexamers or multiple of hexamers. The present chapter compiles the existing data with relation to the function of this protein in the arachnids. Hc has as main function the reversible transport of O2, but it shows many secondary though not less important functions. With reference to this, it has been described that Hc can transport hydrophobic molecules (lipid-derived hormones and lipids) to the different organs, having a key role in the lipid transport system. In arachnids, like in other arthropods and invertebrates, Hc has phenoloxidase function which is related to different metabolic processes such as melanin formation and defense against pathogens. In addition, Hc has additional defensive functions since it can serve as precursor for the production of antimicrobial peptides. In short, the evolution of this protein has led to the development of multiple functions essential for organisms possessing this protein.
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Acknowledgements
This work was supported by grants from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET-PIP no. 515), UNLP and Agencia Nacional de Promoción Científica y Tecnológica (PICT no. 2017-0684), Argentina. A.L., F.G. and M.C. are researchers of CONICET, Argentina. S.R. is a CONICET scholarship holder. We are very grateful to Rosana del Cid for the review of the manuscript, Mario Ramos for the figure design, and Francisco Giambelluca for the photograph of the spider Latrodectus mirabilis.
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Cunningham, M., Laino, A., Romero, S., Fernando Garcia, C. (2020). Arachnid 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_8
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