Molecular characterization of an adiponectin receptor homolog in the white leg shrimp, Litopenaeus vannamei

Adiponectin (AdipoQ) and its receptors (AdipoRs) are strongly related to growth and development of skeletal muscle, as well as glucose and lipid metabolism in vertebrates. Herein we report the identification of the first full-length cDNA encoding an AdipoR homolog (Liv-AdipoR) from the decapod crustacean Litopenaeus vannamei using a combination of next generation sequencing (NGS) technology and bioinformatics analysis. The full-length Liv-AdipoR (1,245 bp) encoded a protein that exhibited the canonical seven transmembrane domains (7TMs) and the inversed topology that characterize members of the progestin and adipoQ receptor (PAQR) family. Based on the obtained sequence information, only a single orthologous AdipoR gene appears to exist in arthropods, whereas two paralogs, AdipoR1 and AdipoR2, have evolved in vertebrates. Transcriptional analysis suggested that the single Liv-AdipoR gene appears to serve the functions of two mammalian AdipoRs. At 72 h after injection of 50 pmol Liv-AdipoR dsRNA (340 bp) into L. vannamei thoracic muscle and deep abdominal muscle, transcription levels of Liv-AdipoR decreased by 93% and 97%, respectively. This confirmed optimal conditions for RNAi of Liv-AdipoR. Knockdown of Liv-AdipoR resulted in significant changes in the plasma levels of ammonia, 3-methylhistine, and ornithine, but not plasma glucose, suggesting that that Liv-AdipoR is important for maintaining muscle fibers. The chronic effect of Liv-AdipoR dsRNA injection was increased mortality. Transcriptomic analysis showed that 804 contigs were upregulated and 212 contigs were downregulated by the knockdown of Liv-AdipoR in deep abdominal muscle. The significantly upregulated genes were categorized as four main functional groups: RNA-editing and transcriptional regulators, molecular chaperones, metabolic regulators, and channel proteins

Aromatic Hybrid Foldamer with a Hydrophilic Helical Cavity Capable of Encapsulating Glucose

An indolocarbazole–naphthyridine hybrid oligomer capable of adopting a stable helical conformation was prepared, and its folding properties were thoroughly studied in the solid state and in solution. As a result of folding, a hydrophilic cavity was generated inside the helix wherein monosaccharides were able to be encapsulated in the order of glucose (9.6 × 10⁴ M^–1) > galactose (1.0 × 10⁴ M^–1) ≫ mannose (∼0) in 10% (v/v) DMSO/CH₂Cl₂

Helical Aromatic Foldamers Functioning as a Fluorescence Turn-on Probe for Anions

Indolocarbazole-pyridine hybrid foldamers are strongly fluorescent in an extended random conformation, but the fluorescence is completely quenched upon folding to a helical conformation due to the compact stacking between aryl planes in the backbone. Anion binding disturbs the helical conformation, thus regenerating the fluorescence of the foldamers. This unique property has been utilized to develop a fluorescence turn-on probe for anions such as sulfate and fluoride