A flashing light may not be that flashy: A systematic review on critical fusion frequencies.

BACKGROUND: Light pollution could represent one of the main drivers behind the current biodiversity erosion. While the effects of many light components on biodiversity have already been studied, the influence of flicker remains poorly understood. The determination of the threshold frequency at which a flickering light is perceived as continuous by a species, usually called the Critical Fusion Frequency (CFF), could thus help further identify the impacts of artificial lighting on animals. OBJECTIVE: This review aimed at answering the following questions: what is the distribution of CFF between species? Are there differences in how flicker is perceived between taxonomic classes? Which species are more at risk of being impacted by artificial lighting flicker? METHODS: Citations were extracted from three literature databases and were then screened successively on their titles, abstracts and full-texts. Included studies were critically appraised to assess their validity. All relevant data were extracted and analysed to determine the distribution of CFF in the animal kingdom and the influence of experimental designs and species traits on CFF. RESULTS: At first, 4881 citations were found. Screening and critical appraisal provided 200 CFF values for 156 species. Reported values of CFF varied from a maximum of between 300 Hz and 500 Hz for the beetle Melanophila acuminata D. to a mean of 0.57 (± 0.08) Hz for the snail Lissachatina fulica B. Insects and birds had higher CFF than all other studied taxa. Irrespective of taxon, nocturnal species had lower CFF than diurnal and crepuscular ones. CONCLUSIONS: We identified nine crepuscular and nocturnal species that could be impacted by the potential adverse effects of anthropogenic light flicker. We emphasize that there remains a huge gap in our knowledge of flicker perception by animals, which could potentially be hampering our understanding of its impacts on biodiversity, especially in key taxa like bats, nocturnal birds and insects.

Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation.

Several studies suggest that the Rh complex represents a major interaction site between the membrane lipid bilayer and the red cell skeleton, but little is known about the molecular basis of this interaction. We report here that ankyrin-R is capable of interacting directly with the C-terminal cytoplasmic domain of Rh and RhAG polypeptides. We first show that the primary defect of ankyrin-R in normoblastosis (nb/nb) spherocytosis mutant mice is associated with a sharp reduction of RhAG and Rh polypeptides. Secondly, our flow cytometric analysis of the Triton X-100 extractability of recombinant fusion proteins expressed in erythroleukemic cell lines suggests that the C-terminal cytoplasmic domains of Rh and RhAG are sufficient to mediate interaction with the erythroid membrane skeleton. Using the yeast two-hybrid system, we demonstrate a direct interaction between the cytoplasmic tails of Rh and RhAG and the second repeat domain (D2) of ankyrin-R. This finding is supported by the demonstration that the substitution of Asp-399 in the cytoplasmic tail of RhAG, a mutation associated with the deficiency of the Rh complex in one Rhnull patient, totally impaired interaction with domain D2 of ankyrin-R. These results identify the Rh/RhAG-ankyrin complex as a new interaction site between the red cell membrane and the spectrin-based skeleton, the disruption of which might result in the stomato-spherocytosis typical of Rhnull red cells.

Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47.

Rh(null) red cells are characteristically stomato-spherocytic. This and other evidence suggest that the Rh complex represents a major attachment site between the membrane lipid bilayer and the erythroid skeleton. As an attempt to identify the linking protein(s) between the red cell skeleton and the Rh complex, we analyzed the expression of Rh, RhAG, CD47, LW, and glycophorin B proteins in red cells from patients with hereditary spherocytosis associated with complete protein 4.2 deficiency but normal band 3 (4.2(-)HS). Flow cytometric and immunoblotting analysis revealed a severe reduction of CD47 (up to 80%) and a slower mobility of RhAG on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, possibly reflecting an overglycosylation state. Unexpectedly, 4.2(-/-) mice, which are anemic, displayed a normal red cell expression of CD47 and RhAG. These results suggest that human protein 4.2, through interaction with CD47, is involved in the skeleton linkage and/or membrane translocation of the Rh complex. However, these potential role(s) of protein 4.2 might be not conserved across species. Finally, the absence or low expression of red cell CD47 in CD47(-/-) mice and in some humans carrying RHCE gene variants (D--, D., and R(N)), respectively, had no detectable effect on protein 4.2 and RhAG expression. Since these cells are morphologically normal with no sign of hemolysis, it is assumed that CD47 deficiency per se is not responsible for the cell shape abnormalities and for the compensated hemolytic anemia typical of 4.2(-) and Rh(null) red cells.