The spider hemolymph clot proteome reveals high concentrations of hemocyanin and von Willebrand factor-like proteins
Autor: | Tobias Wang, Carsten Scavenius, Jesper Bechsgaard, Kristian W. Sanggaard, Trine Bilde, Jan J. Enghild, Thomas F. Dyrlund |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
animal structures Proteome medicine.medical_treatment Biophysics Biology Proteomics Biochemistry Analytical Chemistry 03 medical and health sciences Vitellogenin Hemolymph von Willebrand Factor medicine Animals Blood Coagulation Molecular Biology Innate immune system 030102 biochemistry & molecular biology Spiders Hemocyanin biology.organism_classification Crustacean Horseshoe crab 030104 developmental biology Hemocyanins Immunology biology.protein Brazil |
Zdroj: | Sanggaard, K W, Dyrlund, T F, Bechsgaard, J S, Scavenius, C, Wang, T, Bilde, T & Enghild, J J 2016, ' The spider hemolymph clot proteome reveals high concentrations of hemocyanin and von Willebrand factor-like proteins ', B B A-Proteins and Proteomics, vol. 1864, no. 2, pp. 233-241 . https://doi.org/10.1016/j.bbapap.2015.11.004 |
ISSN: | 1570-9639 |
DOI: | 10.1016/j.bbapap.2015.11.004 |
Popis: | Arthropods include chelicerates, crustaceans, and insects that all have open circulation systems and thus require different properties of their coagulation system than vertebrates. Although the clotting reaction in the chelicerate horseshoe crab (Family: Limulidae) has been described in details, the overall protein composition of the resulting clot has not been analyzed for any of the chelicerates. The largest class among the chelicerates is the arachnids, which includes spiders, ticks, mites, and scorpions. Here, we use a mass spectrometry-based approach to characterize the spider hemolymph clot proteome from the Brazilian whiteknee tarantula, Acanthoscurriageniculata. We focused on the insoluble part of the clot and demonstrated high concentrations of proteins homologous to the hemostasis-related and multimerization-prone von Willebrand factor. These proteins, which include hemolectins and vitellogenin homologous, were previously identified as essential components of the hemolymph clot in crustaceans and insects. Their presence in the spider hemolymph clot suggests that the origin of these proteins' function in coagulation predates the split between chelicerates and mandibulata. The clot proteome reveals that the major proteinaceous component is the oxygen-transporting and phenoloxidase-displaying abundant hemolymph protein hemocyanin, suggesting that this protein also plays a role in clot biology. Furthermore, quantification of the peptidome after coagulation revealed the simultaneous activation of both the innate immune system and the coagulation system. In general, many of the identified clot-proteins are related to the innate immune system, and our results support the previously suggested crosstalk between immunity and coagulation in arthropods. |
Databáze: | OpenAIRE |
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