Two halogenated C15 acetogenins, named lembyne-A and lembyne-B, have been isolated from an unrecorded Laurencia species collected off the Malaysian waters. Their structures were deduced on the basis of spectroscopic evidence. Previously known elatol and iso-obtusol showed potent antibacterial activity against some marine bacteria.

A novel brominated diterpene based on the rare neoirieane skeleton, named neoirietetraol (1), has been isolated along with a halogenated C15 acetogenin, (3Z)-laurenyne (2), from a new Laurencia species, L.yonaguniensis Masuda et Abe, species inedita, collected at Yonaguni Island, Okinawa Prefecture, Japan. The structures of these metabolites were elucidated by spectroscopic data (IR, 1H NMR, 13C NMR, 2D NMR, and MS). Neoirietetraol (1) was toxic to the brine shrimp (Altemia salina; LC50, 40.1 microM) and also showed weak antibacterial activities against two marine bacteria, Alcaligenes aquamarinus and Escherichia coli.

In connection with our chemotaxonomic studies of Malaysian species of the red algal genus Laurencia, the chemical composition of Laurencia pannosa Zanardini was examined. Two halogenated sesquiterpenoids, named pannosanol (1) and pannosane (2), have been isolated along with a halogenated C15-acetogenin, (3Z)-chlorofucin (3). The structures of these compounds were determined from their spectroscopic data (IR, 1H NMR, 13C NMR, 2D NMR, and MS). Pannosanol and pannosane are novel halometabolites with an unusual rearranged chamigrane framework. Antibacterial activities of these metabolites against marine bacteria are also described.

Heterotrimeric G proteins play crucial roles as mediators of signaling by many extracellular stimuli. The receptors that activate G proteins constitute the largest and most diverse family of cell surface molecules involved in signal transmission of metazoan cells. To investigate G protein signaling in the central nervous system (CNS) of chordates, we isolated cDNA fragments encoding five different G protein alpha subunits (CiGalpha(x), CiGalpha(q), CiGalpha(i1a), CiGalpha(i1b), and CiGalpha(i2)) from larvae of the ascidian, a simple chordate, Ciona intestinalis. In situ hybridization analysis revealed that each isoform had distinct patterns of spatial distribution in embryos. Among them, CiGalpha(i1a) and CiG alpha(i1b) mRNAs were specifically expressed in the CNS of the larva, whereas CiGalpha(q) transcripts were expressed in small parts of the trunk epidermis and the tip of the tail, but not in the CNS. The CiGalpha(x) expression was widely observed throughout the trunk and tail of the embryos, and the signals were stronger in the epidermis, mesenchyme, and tail muscle cells. Comparison of cDNA sequences and the exon-intron organization indicate that CiGalpha(i1a) and CiGalpha(i1b) are produced by alternative splicing of transcripts from a single gene, CiGalpha(i1). In the cleavage and gastrula stages, transcripts of CiGalpha(i1) were widely distributed in embryos, and the expression then became restricted to the CNS of tailbud embryos and larvae. An exhaustive search has failed to find transducin-type alpha subunits in C. intestinalis. Since CiGalpha(i1) is expressed in the ocellus, CiGalpha(i1) may mediate signals from Ci-opsin1, a visual pigment of the ocellus photoreceptor cells.

No abstract