Network analysis of adhesion/growth-regulatorygalectins and their binding sites in adult chicken retinaand choroid

• Joachim C. Manning ^[1] ; Gabriel García Caballero ^[1] ; Clemens Knospe ^[1] ; Herbert Kaltner ^[1] ; Hans Joachim Gabius ^[1]
  1. [1] University Munich Institute of Anatomy Munich Germany
• Localización: Journal of Anatomy, ISSN 0021-8782, Vol. 231, Nº. 1, 2017, págs. 23-37
• Idioma: inglés
• Texto completo no disponible (Saber más ...)
• Resumen

  • The highly ordered multilayered organization of the adult chicken retina is a suitable test model for examiningzonal distribution of the members of a bioeffector family. Based on the concept of the sugar code, thefunctional pairing of glycan epitopes with cognate receptors (lectins) is emerging as a means to explain thecontrol of diverse physiological activities. Having recently completed the biochemical characterization of allseven adhesion/growth-regulatory galectins present in chicken, it was possible to establish how the individualcharacteristics of their expression profiles add up to shape the galectin network, which until now has not beendefined at this level of complexity. This information will also have relevance in explaining the region-specificpresence of glycan determinants in the retina, as illustrated in the first part of this study using a panel of nineplant/fungal agglutinins. The following systematic monitoring of the galectins yielded patterns for whichquantitative and qualitative differences were detected. Obviously, positivity in distinct layers is not confined toa single protein of this family, e.g. CG-1A, CG-3 or CG-8. These results underline the requirement for networkanalysis for these proteins that can functionally interact in additive or antagonistic modes. Labeling of thetissue galectins facilitated profiling of their accessible binding sites. It also revealed differences among thegalectin family members, highlighting the ability of this method to define binding properties on the level oftissue sections. Methodologically, the detection of endogenous lectins intimates that cognate glycans canbecome inaccessible, a notable caveat for lectin histochemical studies