Factors affecting the Human Attribution of Emotions toward Animals

ABSTRACT

Attribution of emotions to animals can affect human–animal interactions and dictate animal welfare laws. However, little is known about the factors that influence these attributions. We investigated the effect of belief in animal mind, pet ownership, emotional intelligence, eating orientation, and gender on the attribution of different emotions to a variety of species, from different taxonomic classes, considered as Pet, Use (e.g., used for food, experimentation), or Pest animals. Three hundred and forty-seven participants, aged between 16 and 65 years, completed a questionnaire that measured their belief in the capacity for animals to experience seven primary and secondary emotions. The results showed that attribution of emotions to animals is inconsistent. The ambiguity appears to hinge, in part, upon an animal's functional category and their perceived place in the commonly supposed, though inaccurate, linear hierarchy of species. Nonetheless, the wide range of emotions that were attributed to all species highlights the complex and potentially disorganized thoughts that humans have concerning animals. Belief in animal mind was found to be the strongest and only predictor of emotion attribution to animals in general, but is probably because both are part of the same underlying construct. Ownership of some species—rabbits, horses, rodents and birds—mediated the emotions attributed to that particular species. We conclude that ambiguous attitudes influence the standards of welfare for animals used by humans and that the dichotomous attitudes permit exploitation and welfare violations against animals. Greater understanding of emotion attribution has the potential to improve humane education methods, and suggestions for future research are made.     

High-level expression of bovine rotavirus VP4 protein in Escherichia coli using a hepatitis B core antigen vector

Six regions of the VP4 protein of bovine rotavirus strain UKtc were expressed using hepatitis B core antigen (HBcAg) as a carrier. Following induction by IPTG, the six fusion proteins, AHBcAg through FHBcAg, were expressed in Escherichia coli to a level of 20–37% of total cellular protein. Soluble fusion proteins in a particulate form were partially purified with yields ranging from 0.5–6.4 mg l^–1 of culture.     

Hydrophobic, aza-glycine analogues of luteinizing hormone-releasing hormone

The effect of combination of the hydrophilic aza-Gly substitution (NHNHCO) at position 10 with hydrophobic, unnatural D-amino acids in position 6 on the potency of luteinizing hormone-releasing hormone (LH-RH) analogues has been investigated. Previously the aza-Gly residue was shown to provide protection from enzymatic cleavage and lead to potency increases in a less hydrophobic series. The compounds were prepared by coupling of the corresponding nonapeptide acids with semicarbazide hydrochloride by the N,N'-dicyclohexylcarbodiimide/1-hydroxybenzotriazole procedure. The required nonapeptide acids were prepared by the solid phase method on chloromethyl-polystyrene resin using HF/anisole deprotection. The products were purified by preparative reversed-phase high-performance liquid chromatography. The analogues were tested in a rat estrous cyclicity suppression assay designed to show the paradoxical antifertility effects of these compounds. The potencies of [6-(3-benzimidazol-2-yl)-D-alanine), 10-aza-glycine] LH-RH and [6-(3-(5,6-dimethylbenzimidazol-2-yl)-D-alanine), 10-aza-glycine] LH-RH are 40 and 190 times that of LH-RH respectively. The most active compound in this series is [6-(3-(2-naphthyl)-D-alanine), 10-aza-glycine] LH-RH with a potency 230 times that of LH-RH. This compound is 2.3 times as potent as the standard ([D-Trp6, Pro9-NHEt] LH-RH) and appears to be the most potent LH-RH agonist reported.     

Bunyamwera virus-induced polypeptide synthesis.

Bunyamwera virus-induced polypeptide synthesis in BSC-1 cell has been studied using polyacrylamide gel electrophoresis and autoradiography. Four virus-induced polypeptides were identified. Their molecular weights were 200 X 10(6) (L), 128 X 10(6) (G1), 31 X 10(6) (G2), and 23 X 10(6) (N). Pulse-chase experiments, short labeling experiments, and experiments using amino acid analogs failed to show evidence of polypeptides processing by proteolytic cleavage. Analysis of the kinetics of synthesis of these polypeptides showed that a clear division into early and late categories could be made, the onset of synthesis of polypeptide N and L rapidly reached a peak and then declined. Polypeptides G1 and G2 were made for several hours; their rate of synthesis then declined. All four polypeptides then continued to be made in relatively small amounts for many hours.     

EDC3 phosphorylation regulates growth and invasion through controlling P‐body formation and dynamics

Regulation of mRNA stability and translation plays a critical role in determining protein abundance within cells. Processing bodies (P‐bodies) are critical regulators of these processes. Here, we report that the Pim1 and 3 protein kinases bind to the P‐body protein enhancer of mRNA decapping 3 (EDC3) and phosphorylate EDC3 on serine (S)161, thereby modifying P‐body assembly. EDC3 phosphorylation is highly elevated in many tumor types, is reduced upon treatment of cells with kinase inhibitors, and blocks the localization of EDC3 to P‐bodies. Prostate cancer cells harboring an EDC3 S161A mutation show markedly decreased growth, migration, and invasion in tissue culture and in xenograft models. Consistent with these phenotypic changes, the expression of integrin β1 and α6 mRNA and protein is reduced in these mutated cells. These results demonstrate that EDC3 phosphorylation regulates multiple cancer‐relevant functions and suggest that modulation of P‐body activity may represent a new paradigm for cancer treatment.     

Selection of a screening panel of rhinoviral serotypes

A novel methodology for the selection of a representative primary and secondary screening panel of rhinoviral serotypes for the purposes of identifying potential antiviral agents is presented. This methodology focuses on the active-sites of the rhinoviral proteins but does not invoke historical SAR data, thereby avoiding compound bias.