Peroxiredoxin (Prx) is an antioxidant protein, which protects organisms against various oxidative stresses. In this study, we isolated Peroxiredoxin cDNA from the muscle tissues of American white shrimp, Litopenaeus vannamei, using reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE). The full-length cDNA consists of 962-bp, which includes a 49-bp 5′-untranslated region (UTR), a 316-bp 3′-untranslated region, and a 597-bp open reading frame (ORF) encoding 198 amino acids. The signal peptide sequence was not found in this cDNA. We aligned the deduced amino acid sequence with the known amino acid sequences of Fenneropenaeus indicus, Fenneropenaeus chinensis, Marsupenaeus japonicus, Scylla serrata, Drosophila melanogaster, Bos taurus, Branchiostoma belcheri, Anoplopoma fimbria, and Rattus norvegicus, and the sequence similarities scores were found to be 97%, 96%, 95%, 83%, 72%, 70%, 80%, 81%, and 75%, respectively. We also found 2-cysteine (Cys) residues in this peroxiredoxin sequence. The RT-PCR analysis revealed that the peroxiredoxin mRNA was expressed in the gills, hepatopancreas, muscles, intestine, and hemocytes. Studies using this newly cloned peroxiredoxin gene from Litopenaeus vannamei will add to the existing knowledge base on the physiological role of peroxiredoxin in shrimp species.

Mixed-valence copper(I/II) atoms have been introduced successfully into a Pb/I skeleton to obtain two heterometallic iodoplumbates, namely poly[bis(tetra-n-butylammonium) [bis(μ-dimethyldithiocarbamato)dodeca-μ-iodido-hexa-μ-iodido-tetracopper(I)copper(II)hexalead(II)]], {(CHN)[CuCuPb(CHNS)I]}, (I), and poly[[μ-iodido-tri-μ-iodido-iodido[bis(1,10-phenanthroline)copper(I)]copper(I)copper(II)lead(II)] hemiiodine], {[CuCuPbI(CHN)]·0.5I}, (II), under solution and solvothermal conditions, respectively. Compound (I) contains two-dimensional anionic layers, which are built upon the linkages of Cu(SCNMe) units and one-dimensional anionic Pb/I/Cu chains. Tetra-n-butylammonium cations are located between the anionic layers and connected to them via C-H...I hydrogen-bonding interactions. Compound (II) exhibits a one-dimensional neutral structure, which is composed of [PbI] square pyramids, [CuI] tetrahedra and [CuNI] trigonal bipyramids. Face-to-face aromatic π-π stacking interactions between adjacent 1,10-phenanthroline ligands stabilize the structure and assemble compound (II) into a three-dimensional supramolecular structure. I molecules lie in the voids of the structure.

Two shRNA sequences against porcine somatostatin (SST) were designed using software available on the NCBI website. The designed RNA sequences were chemically synthesized and cloned into lentiviral vectors (LV-siRNA1 and LV-siRNA2). Porcine somatostatin cDNA was amplified and cloned into pcDNA3.1 (pcDNA3.1-SST). LV-siRNA1 or LV-siRNA2 was cotransfected with pcDNA3.1-SST into NIH3T3 cells. Real-time RT-PCR for the detection of SST mRNA, revealed that LV-siRNA1 and LV-siRNA2 suppressed SST expression by 87.9% and 86.3% (P< 0.01), respectively. In addition, radioimmunoassay (RIA) for direct detection of SST indicated that the suppression ratios for LV-siRNA1 and LV-siRNA2 were 55.1% and 51.6% (P< 0.01), respectively. These data showed that the 2 shRNA sequences were effective in suppressing SST expression and may provide an approach to down-regulate bothin vitroandin vivoexpression of porcine SST.