Function of snail shell hairs in anti-predator defense.

The function and evolutionary background of the hairs on the shells of terrestrial gastropods is largely unknown. Many hypotheses proposed by malacologists have never been proven, and the long-held hypothesis of mechanical stability in wet environments has been rejected by recent studies. It would therefore be worthwhile to reexamine other hypotheses regarding the adaptive significance of shell hairs. We investigated the defense function of shell hairs against a specialist predator, the snail-eating firefly, in the long-haired snail Moellendorffia diminuta. The firefly larvae, which hunt snails using abdominal suckers, were unable to attach to the shell because of the shell hairs but were able to attach to the shells that had lost their hairs. About half of the hairy snails successfully defended themselves by swinging their shells and dropping firefly larvae, but most of the snails without hair failed to defend. The hairs reduce the ability of the larva to attach to the shell and increase the effectiveness of the shell-swinging defense behavior in removing the larva from the shell. As shell hairs grow longer with shell development, they may confer an advantage based on the predator's growth stage. Our findings highlight the anti-predator defense role of shell hairs in land snails, introducing a hypothesis previously overlooked in the evolutionary context of hairy snails.

Carcinoecium-Forming Sea Anemone Stylobates calcifer sp. nov. (Cnidaria, Actiniaria, Actiniidae) from the Japanese Deep-Sea Floor: A Taxonomical Description with Its Ecological Observations.

Here we describe Stylobates calcifer sp. nov. (Cnidaria, Actiniaria, Actiniidae), a new carcinoecium-forming sea anemone from the deep-sea floor of Japan. Stylobates produces a carcinoecium that thinly covers the snail shells inhabited by host hermit crabs Pagurodofleinia doederleini. The new species is distinct from other species by the shape of the marginal sphincter muscle, the distribution of cnidae, the direction of the oral disk, and host association. The species' novelty is supported by the data of its mitochondrial genes 12S, 16S, and COIII and nuclear genes 18S and 28S. Also, we conducted behavioral observation of this new species, focusing on the feeding behavior and interaction with the specific host hermit crab. Our observations suggest that this sea anemone potentially feeds on the suspended particulate organic matter from the water column or the food residuals of hermit crabs. When the host's shell changed, intensive manipulation for transference of S. calcifer sp. nov. was recorded. However, although the hermit crab detached and transferred the sea anemone to the new shell after shell change, the sea anemone did not exhibit active or cooperative participation. Our data suggest that the sea anemone may not produce a carcinoecium synchronously to its host's growth, contrary to the anecdotal assumption about carcinoecium-forming sea anemones. Conversely, the host hermit crab's growth may not depend entirely on the carcinoecium produced by the sea anemone. This study is perhaps the first observation of the behavioral interaction of the rarely studied carcinoecium-forming mutualism in the deep sea.

A Brief Description of Surface Structure and Composition of the Pseudo-Snail Shell Formed by a Sea Anemone Stylobates sp. Symbiotic with Hermit Crabs from the Deep-Sea Floor.

Sea anemones belonging to the genera Adamsia and Stylobates have a remarkable symbiotic relationship with hermit crabs. These symbiotic sea anemones produce a shell-like structure, called a "carcinoecium," that covers and extends over the gastropod shell of the host hermit crab as hermit crabs grow. This structure has been described as "chitinous carcinoecium" or "chitinous coating." A previous study investigated carcinoecia of Stylobates aeneus, the results of which indicated that it contained at least 1.7% chitin, while the remaining components were unidentified. Moreover, the microscopic structure of a carcinoecium still remains to be detailed. We, therefore, conducted detailed observations using a stereoscopic microscope and scanning electron microscope (SEM) and the analyses of the chemical composition of carcinoecia produced by Stylobates sp. (apparently conspecific with Isadamsia sp. "J" reported in Uchida and Soyama, 2001) associated with a pagurid hermit crab Pagurodofleinia doederleini collected in the south of the Shima Peninsula, Mie, Honshu Island, Japan at a depth of 294-306 m. Our results indicate that carcinoecia of Stylobates sp. contain HCl-soluble components (13%), NaOH-soluble components (38%), chitin (11%) and unidentified remnants (39%). Additionally, our observations show that Stylobates sp. incorporates dark- and white-colored particles that could be sand and/or mud into the carcinoecium.

Morphology and Habitats of the Hermit-Crab-Associated Calyptraeid Gastropod Ergaea walshi.

Ergaea walshi, a gastropod with a markedly flat shell, often lives inside empty snail shells occupied by hermit crabs. We investigated its lifestyle, shell growth pattern, and habitat preference for host hermit crabs and host snail shells. Four hundred sixteen snail shells, including 363 shells with hermit crabs and 53 empty shells, were collected from intertidal zones of sandy and muddy flats around Kii Peninsula, Japan. The specimens comprised seven hermit crab species occupying 24 shell species; E. walshi was harbored in 13.2% of snail shells with hermit crabs and 17.0% of those without hermit crabs. Although no preference was detected for particular species of hermit crab or snail shell, E. walshi preferred to live inside of snail shells with wider apertures used by comparatively bigger hermit crabs. This suggests that the occurrence of E. walshi was influenced by host size rather than host species. When looking at growth patterns, we found that the attached shell portion of E. walshi continued to be enlarged horizontally, while growth in shell height slowed at approximately 5.0 mm. The conspicuously flattened shell of E. walshi is considered as a growth pattern for adapting to the narrow space within the snail shell occupied by hermit crabs. Consistent with this idea, our comparison of shell growth patterns in 23 calyptraeid species showed that shell of E. walshi is the flattest in this family.

Rubimetide, humanin, and MMK1 exert anxiolytic-like activities via the formyl peptide receptor 2 in mice followed by the successive activation of DP1, A2A, and GABAA receptors.

Rubimetide (Met-Arg-Trp), which had been isolated as an antihypertensive peptide from an enzymatic digest of spinach ribulose-bisphosphate carboxylase/oxygenase (Rubisco), showed anxiolytic-like activity prostaglandin (PG) D2-dependent manner in the elevated plus-maze test after administration at a dose of 0.1mg/kg (ip.) or 1mg/kg (p.o.) in male mice of ddY strain. In this study, we found that rubimetide has weak affinities for the FPR1 and FPR2, subtypes of formyl peptide receptor (FPR). The anxiolytic-like activity of rubimetide (0.1mg/kg, ip.) was blocked by WRW4, an antagonist of FPR2, but not by Boc-FLFLF, an antagonist of FPR1, suggesting that the anxiolytic-like activity was mediated by the FPR2. Humanin, an endogenous agonist peptide of the FPR2, exerted an anxiolytic-like activity after intracerebroventricular (icv) administration, which was also blocked by WRW4. MMK1, a synthetic agonist peptide of the FPR2, also exerted anxiolytic-like activity. Thus, FPR2 proved to mediate anxiolytic-like effect as the first example of central effect exerted by FPR agonists. As well as the anxiolytic-like activity of rubimetide, that of MMK1 was blocked by BW A868C, an antagonist of the DP1-receptor. Furthermore, anxiolytic-like activity of rubimetide was blocked by SCH58251 and bicuculline, antagonists for adenosine A2A and GABAA receptors, respectively. From these results, it is concluded that the anxiolytic-like activities of rubimetide and typical agonist peptides of the FPR2 were mediated successively by the PGD2-DP1 receptor, adenosine-A2A receptor, and GABA-GABAA receptor systems downstream of the FPR2.