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Walters Mouridsen posted an update 6 months, 3 weeks ago
There are three broad groups of oxygen-transport proteins found in the haemolymph (blood) of invertebrates, namely the hemocyanins, the hemerythrins and the globins. Both hemerythrins and extracellular globins are iron-based proteins that are understudied when compared to the copper-containing hemocyanins. Recent evidence suggests that hemerythrins and (giant) extracellular globins (and their linker chains) are more widely distributed than previously thought and may have biological functions beyond oxygen transport and storage. Herein, we review contemporary literature of these often-neglected proteins with respect to their structural configurations on formation and ancestral states.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.Hemocyanin (Hc), a copper-containing extracellular multimeric protein, is the major protein component of hemolymph in different arachnid groups. https://www.selleckchem.com/products/Elesclomol.html 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.Instead of the red blood of vertebrates, most molluscs have blue hemolymph containing hemocyanin, a type-3 copper-containing protein. The hemoglobin of vertebrate blood is replaced in most molluscs with hemocyanin, which plays the role of an oxygen transporter. Oxygen-binding in hemocyanin changes its hue from colorless deoxygenated hemocyanin into blue oxygenated hemocyanin. Molecules of molluscan hemocyanin are huge, cylindrical multimeric proteins-one of the largest protein molecules in the natural world. Their huge molecular weight (from 3.3 MDa to more than 10 MDa) are the defining characteristic of molluscan hemocyanin, a property that has complicated structural analysis of the molecules for a long time. Recently, the structural analysis of a cephalopod (squid) hemocyanin has succeeded using a hybrid method employing both X-ray crystallography and cryo-EM. In a biochemical breakthrough for molluscan hemocyanin, the first quaternary structure with atomic resolution is on the verge of solving the mystery of molluscan hemocyanin. Here we describe the latest information about the molecular structure, classification and evolution of the molecule, and the physiology of molluscan hemocyanin.Hemoglobin is the respiratory protein of many arthropods, enhancing the oxygen transport capacity of the hemolymph. One example, that has been subject of extensive studies, is the hemoglobin of the crustacean genus Daphnia. Here the characteristics of this oxygen binding protein are reviewed. The genetic structure is the result of repeated duplication events in the evolution, leading to a variety of di-domain isoforms. Adjustments to environmental changes thus result from differential expression of these paralogs. The biochemical properties, including spectral characteristics, concentration ranges, molecular mass of monomers and native oligomers, are compared. Structural differences between isoforms can be correlated to functional properties of oxygen binding characteristics. The mechanism of hemoglobin induction via hypoxia-inducible factor 1 allows the response to altered oxygen and temperature conditions. Changes of the hemoglobin suite in quantity and functional quality can be linked to their benefits for the animals’ physiological performance. However, there is a large inter- and intra-specific variability of this induction potential. The consequences of altered hemoglobin characteristics for the animals’ success within their habitat are discussed.Insects possess powerful immune systems that have evolved to defend against wounding and environmental pathogens such as bacteria, fungi, protozoans, and parasitoids. This surprising sophistication is accomplished through the activation of multiple immune pathways comprised of a large array of components, many of which have been identified and studied in detail using both genetic manipulations and traditional biochemical techniques. Recent advances indicate that certain pathways activate arrays of proteins that interact to form large functional complexes. Here we discuss three examples from multiple insects that exemplify such processes, including pathogen recognition, melanization, and coagulation. The functionality of each depends on integrating recognition with the recruitment of immune effectors capable of healing wounds and destroying pathogens. In both melanization and coagulation, protein interactions also appear to be essential for enzymatic activities tied to the formation of melanin and for the recruitment of hemocytes.