SummaryTwenty-two stages of the prenatal development of the domestic cat are described for intraspecies comparison in embryological studies. These are assigned to the 15 embryonal periods based on the Nomina Embryologica Veterinaria to make the interspecies comparison possible.

Discoveries on involvement of glycan–protein recognition in many (patho)physiological processes are directing attention to exploring the significance of a fundamental structural aspect of sugar receptors beyond glycan specificity, i.e., occurrence of distinct types of modular architecture. In order to trace clues for defining design–functionality relationships in human lectins, a lectin's structural unit has been used as source material for engineering custom-made variants of the wild-type protein. Their availability facilitates comparative analysis toward the stated aim. With adhesion/growth-regulatory human galectin-1 as example, the strategy of evaluating how changes of its design (here, from the homodimer of non-covalently associated domains to (i) linker-connected di- and tetramers and (ii) a galectin-3-like protein) affect activity is illustrated by using three assay systems of increasing degree of glycan complexity. Whereas calorimetry with two cognate disaccharides and array testing with 647 (glyco)compounds disclosed no major changes, galectin histochemical staining profiles of tissue sections that present natural glycome complexity revealed differences between wild-type and linker-connected homo-oligomers as well as between the galectin-3-like variant and wild-type galectin-3 for cell-type positivity, level of intensity at the same site and susceptibility for inhibition by a bivalent glycocompound. These results underscore the strength of the documented approach. Moreover, they give direction to proceed to (i) extending its application to other members of this lectin family, especially galectin-3 and (ii) then analyzing impact of architectural alterations on cell surface lattice formation and ensuing biosignaling systematically, considering the variants’ potential for translational medicine.

Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides, which display diverse bioactivities (e.g., antifungal, antimicrobial, and antiviral). One characteristic of these lanthipeptides is the presence of thioether bonds, which are termed (methyl-) lanthionine rings. These modifications are installed by corresponding modification enzymes in a two-step modality. First, serine and threonine residues are dehydrated followed by a subsequent catalyzed cyclization reaction, in which the dehydrated serine and threonine residues are undergoing a Michael-type addition with cysteine residues. The dedicated enzymes are encoded by one or two genes and the classification of lanthipeptides is pending on this. The modification steps form the basis of distinguishing the different classes of lanthipeptides and furthermore reflect also important mechanistic differences. Here, we will summarize recent insights into the mechanisms and the structures of the participating enzymes, focusing on the two core modification steps-dehydration and cyclization.

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

Introducing tissue sections for testing glycocluster activity as inhibitors of lectin binding close to in vivo conditions.