Both antibodies recognize DYNLL1/LC8 in honey bee, which reinforces that it is a conserved protein ( Espindola et al., 2000, Jaffrey and Snyder, 1996 and Odronitz et al., 2009). In the present study, after fractionation of the soluble honey bee brain fraction by gel filtration, Western blot indicated the presence of DYNLL1/LC8 throughout the eluted fractions, which suggested the co-elution of this protein with high molecular weight proteins, such as dynein and myosin-Va. The biochemical and physicochemical properties of myosin-Va have been described, including the interaction of its head

domain with actin, which is influenced selleck kinase inhibitor by ATP and ADP (Nascimento et al., 1996). The effect of ATP was also observed for myosin-Va from honey bee brain protein fractions. In fact, ATP induces the release of myosin-Va from F-actin, which allows it to remain in the supernatant, and the F-actin cytoskeleton is pelleted by centrifugation (Espindola et al., 1992 and Tauhata et al., 2001). We also noted that the solubility of DYNLL1/LC8 increases similarly to myosin-Va in the presence of ATP. Future studies will determine if a physical interaction between these two proteins

exist. The buy BYL719 distributions of CaMKII, DYNLL1/LC8, and myosins -Va and -VI in the honey bee brain indicated that these proteins are expressed in specific regions of the four dissected neuropils. In regard to CaMKII immunodetection, we found higher expression levels in the antennal lobe than in the other regions. The differentiation of the honey bee brain regions is reflected in the distribution of important kinases of the signal

transduction system. Protein kinases A and C, CaMKII and inositol 1,4,5-trisphosphate receptor were expressed preferentially in the mushroom bodies (Kamikouchi et al., 2000, Kamikouchi et al., 1998 and Muller, 1999). It is possible that the distribution patterns of myosins, DYNLL1/LC8 and Doxorubicin clinical trial synaptophysin are associated with the functions of these proteins in these regions of the honey bee brain. Through immunolocalization analyses, myosin-Va was found in the optical and antennal lobes, and in the mushroom bodies. In the neuropils, myosin-Va was expressed in neurons and fibers in all of the honey bee brain regions evaluated. Myosin-Va studies in the vertebrate brain have also reported that it is localized in neurons and glial cells (Espindola et al., 1992, Martins et al., 1999 and Tilelli et al., 2003). In mushroom bodies, we also demonstrated that the localization of synaptophysin was restricted to the membrane space of Kenyon cells. This protein is an integral synaptic vesicle glycoprotein (Leube et al., 1987) and is widely used as a marker for synapses because it is distributed in presynaptic terminals (Li et al., 2010). In addition, myosin-Va was immunolocalized in the fibers of the mushroom bodies in a manner similar to the distribution of zinc in this honey bee brain region.