Axoplasmic asymmetry at the node of Ranvier

Brain Cell Biology - The previously described unilateral condensation of axoplasmic organelles at the node of Ranvier of large diameter fibres in spinal nerve roots has been confirmed in a single...     

Recording of DNA-binding events reveals the importance of a repurposed Candida albicans regulatory network for gut commensalism

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Success in the demographic expansion of Fraxinus excelsior L.

This review examines the ecological traits and ecophysiological characteristics of the common ash (Fraxinus excelsior L.) that help to explain the current spread of ash communities in Europe. As a consequence of anthropogenic disturbance, the common ash has experienced new environmental conditions and the frequency of the species has fluctuated over space and time. Owing to its ubiquity, over the last few decades the common ash has been greatly favoured in areas abandoned by agriculture and also along impounded rivers. F. excelsior is a mesophilic species that usually thrives on alluvial soils and can also survive the strong water deficit on hillslopes. Drought tolerance in ash trees is related to stomatal regulation, a decrease in osmotic potential and also an increase in the elastic modulus ). Malic acid plays a central role in drought tolerance, first as one of the major solutes involved in osmotic adjustment, and second as an effector for stomatal regulation through a drought-induced increase in its xylem concentration.     

Prion Protein Paralog Doppel Protein Interacts with Alpha-2-Macroglobulin: A Plausible Mechanism for Doppel-Mediated Neurodegeneration

Doppel protein (Dpl) is a paralog of the cellular form of the prion protein (PrP^C), together sharing common structural and biochemical properties. Unlike PrP^C, which is abundantly expressed throughout the central nervous system (CNS), Dpl protein expression is not detectable in the CNS. Interestingly, its ectopic expression in the brain elicits neurodegeneration in transgenic mice. Here, by combining native isoelectric focusing plus non-denaturing polyacrylamide gel electrophoresis and mass spectrometry analysis, we identified two Dpl binding partners: rat alpha-1-inhibitor-3 (α₁I₃) and, by sequence homology, alpha-2-macroglobulin (α₂M), two known plasma metalloproteinase inhibitors. Biochemical investigations excluded the direct interaction of PrP^C with either α₁I₃ or α₂M. Nevertheless, enzyme-linked immunosorbent assays and surface plasmon resonance experiments revealed a high affinity binding occurring between PrP^C and Dpl. In light of these findings, we suggest a mechanism for Dpl-induced neurodegeneration in mice expressing Dpl ectopically in the brain, linked to a withdrawal of natural inhibitors of metalloproteinase such as α₂M. Interestingly, α₂M has been proven to be a susceptibility factor in Alzheimer''s disease, and as our findings imply, it may also play a relevant role in other neurodegenerative disorders, including prion diseases.