De Boyer Des Roches, A., Richard-Yris, M. - A., Henry, S., Ezzaouia, M., & Hausberger, M. (2008). Laterality and emotions: visual laterality in the domestic horse (Equus caballus) differs with objects' emotional value. Physiol. Behav., 94(3), 487–490.
Abstract: Lateralization of emotions has received great attention in the last decades, both in humans and animals, but little interest has been given to side bias in perceptual processing. Here, we investigated the influence of the emotional valence of stimuli on visual and olfactory explorations by horses, a large mammalian species with two large monocular visual fields and almost complete decussation of optic fibres. We confronted 38 Arab mares to three objects with either a positive, negative or neutral emotional valence (novel object). The results revealed a gradient of exploration of the 3 objects according to their emotional value and a clear asymmetry in visual exploration. When exploring the novel object, mares used preferentially their right eyes, while they showed a slight tendency to use their left eyes for the negative object. No asymmetry was evidenced for the object with the positive valence. A trend for an asymmetry in olfactory investigation was also observed. Our data confirm the role of the left hemisphere in assessing novelty in horses like in many vertebrate species and the possible role of the right hemisphere in processing negative emotional responses. Our findings also suggest the importance of both hemispheres in the processing positive emotions. This study is, to our knowledge, the first to demonstrate clearly that the emotional valence of a stimulus induces a specific visual lateralization pattern.
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Hostikka, S. L., Eddy, R. L., Byers, M. G., Hoyhtya, M., Shows, T. B., & Tryggvason, K. (1990). Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome. Proc. Natl. Acad. Sci. U.S.A., 87(4), 1606–1610.
Abstract: We have identified and extensively characterized a type IV collagen alpha chain, referred to as alpha 5(IV). Four overlapping cDNA clones isolated contain an open reading frame for 543 amino acid residues of the carboxyl-terminal end of a collagenous domain, a 229-residue carboxyl-terminal noncollagenous domain, and 1201 base pairs coding for a 3' untranslated region. The collagenous Gly-Xaa-Yaa repeat sequence has five imperfections that coincide with those in the corresponding region of the alpha 1(IV) chain. The noncollagenous domain has 12 conserved cysteine residues and 83% and 63% sequence identity with the noncollagenous domains of the alpha 1(IV) and alpha 2(IV) chains, respectively. The alpha 5(IV) chain has less sequence identity with the putative bovine alpha 3(IV) and alpha 4(IV) chains. Antiserum against an alpha 5(IV) synthetic peptide stained a polypeptide chain of about 185 kDa by immunoblot analysis and immunolocalization of the chain in human kidney was almost completely restricted to the glomerulus. The gene was assigned to the Xq22 locus by somatic cell hybrids and in situ hybridization. This may be identical or close to the locus of the X chromosome-linked Alport syndrome that is believed to be a type IV collagen disease.
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