Although it is unclear how C3a exerts these contradictory Tulathromycin B functions at this stage, it is possible that the function of C3a depends on or the duration of inflammation. In this aspect, it is notable that prostaglandin E2 can suppress IL-17 production during early Th17 differentiation, but enhance IL-17 production by mature Th17 cells. Since C3a have been shown to induce the production of prostaglandin E2 by macrophage, it is feasible to surmise that C3a-prostaglandin E2 pathway differently affects Th17 cells depending on their differentiation stages. Further studies are needed to clearly define the role of C3a in regulating pulmonary Th17 responses. It is also possible that the discrepancy between the two studies is due to different nature of allergen used. We used the mixture of Aspergillus proteinase and OVA as our model allergen whereas the prior study by Lajoie et al used house dust mite extract containing containing about 20 % weight of protein including Der p1 as well as non-protein components such as endotoxin. Therefore, we speculate that the mechanism of C3a induction by these two allergens might be different. For instance, while proteinase activity seems crucial for C3a production by allergen challenge in the present study, it is less clear how house dust mite extract induced C3a in vivo. Another possible explanation is that, in addition to C3a, these two allergens might induce different innate cytokines which overall could lead to different outcome in helper T cell responses in vivo. Whereas a large number of vertebrate FABPs have been extensively studied phylogenetically and for ligand-binding specificities, relatively less information is available regarding invertebrate FABPs. Mepiroxol Recently, molecular biology, gene expression profile and structural studies have substantially increased the information related to the evolutionary and the cellular diversity of invertebrate FABPs. Invertebrate FABPs display low sequence identities with vertebrate FABPs, even though a rather modest but significantly higher sequence identity exists with the H-FABP type. Taking into account that the vertebrate HFABP group has a wide distribution and multiple functions, one can reasonably assume that invertebrate FABPs may also ensure a wide spectrum of biological functions. Although its precise physiological function is still unclear, this protein is supposed to play an important role in the intracellular transport of long chain fatty acids and, putatively, is involved in signal transduction in the hepatopancreas of C. quadricarinatus. The binding of several fatty acids playing differential effects on the growth and gonad maturation of female C. quadricarinatus was then characterized by using four different procedures. Although all these procedures are based on the use of fluorescence and lead to similar results, they are not equivalent in terms of analysis and interpretation. Their advantages and/or limitations are discussed below. We report on assays for the ligand-binding affinity of Cq-FABP, three of these procedures are based on competitive experiments using the steady-state fluorescence intensity of ANS or cisparinaric acid while the last one is based on competitive experiments using the steady-state fluorescence anisotropy of the fluorescent fatty acid analog BODIPY-C16. ANS was extensively used in the past for characterizing FABP/ligand interactions because most of the fatty acids commonly used are not fluorescent.