Fifteen local spiking interneurons (LSIs) andtwenty-one local nonspiking interneurons (LNIs) were identified in the terminal abdominal ganglion (TAG) of the cricket Gryllus bimaculatus on the basis of intracellular recording and staining (Figs. 1, 5, 6). Although the majority of LNIs showed sharp directionalities (Fig. 7) the LSIs did not (Fig. 3). The directionality of LNIs varied with the recording sites within a single cell (Fig. 8). Electrical stimulations of the cercal sensory nerve suggested that the LNIs are connected monosynaptically with the sensory afferents of both the cerci, and that LSIs may possess a variety of bilateral combinations of polysynaptic connections with the sensory afferents. We found that the spiking and the nonspiking local interneurons in the cercal sensory system differ not only in their membrane properties, but also in their afferent connections, and concluded that their differing connectivity to the sensory afferents will associate them with different roles in signal processing.

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BackgroundFas ligand plays a key role in the human immune system as a major cell death inducing protein. The extracellular domain of human Fas ligand (hFasLECD) triggers apoptosis of malignant cells, and therefore is expected to have substantial potentials in medical biotechnology. However, the current application of this protein to clinical medicine is hampered by a shortage of the benefits relative to the drawbacks including the side-effects in systemic administration. Effective procedures for the engineering of the protein by attaching useful additional functions are required to overcome the problem.ResultsA procedure for the site-specific chemical conjugation of hFasLECD with a fluorochrome and functional proteins was devised using an inverse-electron-demand Diels-Alder reaction between trans-cyclooctene group and methyltetrazine group. The conjugations in the present study were attained by using much less molar excess amounts of the compounds to be attached as compared with the conventional chemical modification reactions using maleimide derivatives in the previous study. The isolated conjugates of hFasLECD with sulfo-Cy3, avidin and rabbit IgG Fab’ domain presented the functional and the structural integrities of the attached molecules without impairing the specific binding activity toward human Fas receptor extracellular domain.ConclusionsThe present study provided a new fundamental strategy for the production of the engineered hFasLECDs with additional beneficial functions, which will lead to the developments of the improved diagnostic systems and the effective treatment methods of serious diseases by using this protein as a component of novel molecular tools.Electronic supplementary materialThe online version of this article (doi:10.1186/s12896-017-0381-2) contains supplementary material, which is available to authorized users.

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