Detection of human papillomavirus in anal specimens using the hybrid capture 2 assay.

The hc2 human papillomavirus DNA test (HC2) is effective when screening women for cervical dysplasia, and it might be effective in the screening for anal dysplasia. Differences between the anal and the cervical canals could affect the test performance. This prospective study (n=292) measured the HC2 signal and in agreement with a histologic endpoint of high-grade dysplasia for anal specimens collected in various ways.

The discriminative effects of the kappa-opioid hallucinogen salvinorin A in nonhuman primates: dissociation from classic hallucinogen effects.

Rationale: The widely available hallucinogen salvinorin A is a unique example of a plant-derived compound selective for kappa-opioid receptors and may produce effects distinct from those of other compounds with classic hallucinogenic or dissociative properties which are also abused in humans.

Objectives: The objective of this study is to characterize the salvinorin A discriminative cue in nonhuman primates with high kappa-receptor genetic homology to humans.

Methods: Adult rhesus monkeys (n = 3) were trained to discriminate salvinorin A (0.

Molecular, mass spectral, and physiological analyses of orcokinins and orcokinin precursor-related peptides in the lobster Homarus americanus and the crayfish Procambarus clarkii.

Recently, cDNAs encoding prepro-orcokinins were cloned from the crayfish Procambarus clarkii; these cDNAs encode multiple copies of four orcokinin isoforms as well as several other peptides. Using the translated open reading frames of the P. clarkii transcripts as queries, five ESTs encoding American lobster Homarus americanus orthologs were identified via BLAST analysis.

Unconditioned behavioral effects of the powerful kappa-opioid hallucinogen salvinorin A in nonhuman primates: fast onset and entry into cerebrospinal fluid.

Salvinorin A is the main active component of the widely available hallucinogenic plant, Salvia divinorum. Salvinorin A is a selective high-efficacy kappa-agonist in vitro, with some unique pharmacodynamic properties. Descriptive reports show that salvinorin A-containing products produce robust behavioral effects in humans.

The effects of herkinorin, the first mu-selective ligand from a salvinorin A-derived scaffold, in a neuroendocrine biomarker assay in nonhuman primates.

Herkinorin is the first mu-opioid receptor-selective ligand from the salvinorin A diterpenoid scaffold. Herkinorin has relative mu > kappa > delta binding selectivity, and it can act as an agonist at both mu- and kappa-receptors, in vitro. These studies were the first in vivo evaluation of the effects of herkinorin in nonhuman primates, using prolactin release, a neuroendocrine biomarker assay that is responsive to both mu- and kappa-agonists, as well as to compounds with limited ability to cross the blood-brain barrier.

Identification of A-type allatostatins possessing -YXFGI/Vamide carboxy-termini from the nervous system of the copepod crustacean Calanus finmarchicus.

The copepod crustacean Calanus finmarchicus plays a critical role in the ecology of the Gulf of Maine and other regions of the North Atlantic. To increase our understanding of the physiology of this species, a normalized, whole organism cDNA library was constructed, and expressed sequence tags (ESTs) of the clones were generated. Among these ESTs was one with homology to known cDNAs encoding prepro-A-type allatostatins (A-type ASTs), a well-known family of arthropod peptides that regulate juvenile hormone production in insects.

Identification and cardiotropic actions of sulfakinin peptides in the American lobster Homarus americanus.

In arthropods, a group of peptides possessing a -Y((SO3H))GHM/LRFamide carboxy-terminal motif have been collectively termed the sulfakinins. Sulfakinin isoforms have been identified from numerous insect species. In contrast, members of this peptide family have thus far been isolated from just two crustaceans, the penaeid shrimp Penaeus monodon and Litopenaeus vannamei.

Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus.

Pathogenic challenges in decapod crustaceans are combated by innate immune responses, including the production and secretion of soluble antibacterial proteins into the hemolymph. Among the antibacterials that have been identified in decapod species are the crustins, a group of four-disulfide core/whey-acidic-protein (WAP) domain-containing proteins, which target marine/salt tolerant Gram-positive bacteria. To begin to assess the possible role of crustins in combating bacterial invasion in the American lobster Homarus americanus, we identified and sequenced a 744 base pair cDNA that encodes a novel 96 amino acid crustin-like protein.