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Over 30 different amyloid proteins and a number of corresponding protein-misfolding diseases have been identified. Among these is Alzheimer's disease, the most common neurodegenerative disorder. The treatment of these diseases is still a goal to reach and many molecules have been studied in this context. Among these, the cyclodextrins have shown interesting potential as agents against protein aggregation (antiaggregants). On the basis of this interest, we investigated the effect on protein aggregation of some oligomers of β-cyclodextrins. In particular, it was found that amino oligomers show good inhibition of β-amyloid aggregation in the micromolar concentration range. The presence of both a multicavity system and amino groups seems to be essential for preventing protein aggregation.

l-Carnosine is an endogenously synthesized dipeptide composed of beta-alanine and l-histidine. It acts as a free radical scavenger and possesses antioxidant properties. l-Carnosine reduces proinflammatory and profibrotic cytokines such as transforming growth factor-beta (TGF-beta), interleukin (IL)-1, and tumor necrosis factor (TNF)-alpha in different experimental settings. In the present study, we investigated the efficacy of l and d-carnosine on the animal model of spinal cord injury (SCI). The spinal cord was exposed via a four-level T5-T8 laminectomy and SCI was produced by extradural compression of the spinal cord at level T6-T7 using an aneurysm clip with a closing force of 24 g. Treatment with d-carnosine (150 mg/kg administered i.p., 1 h and 6 h, after SCI), but not l-carnosine significantly decreased (a) the degree of spinal cord inflammation and tissue injury (histological score), (b) neutrophil infiltration (myeloperoxidase activity), (c) nitrotyrosine formation, inducible NO synthase (iNOS) and Hsp70 expression, (d) proinflammatory cytokines, and (e) apoptosis (TUNEL staining, Fas ligand, Bax, and Bcl-2 expression). Furthermore, d-carnosine (150 mg/kg administered i.p., 1 h and 6 h, after SCI) significantly ameliorated the loss of limb function (evaluated by motor recovery score). Taken together, our results demonstrate the strong difference between l-carnosine and d-carnosine. The result strongly suggests that d-carnosine treatment reduces the development of inflammation and tissue injury associated with spinal cord trauma. © 2011 Elsevier Inc. All rights reserved.

VDACs (voltage-dependent anion-selective channels) or mitochondrial PORINS are transmembrane proteins forming pores in the outer membrane. In eukaryotic genomes multiple genes coding for VDAC homologues have been discovered, but the functional meaning of this gene redundancy is unknown. In Drosophila melanogasterthree additional genes homologous to the gene porin (CG6647) have been found. As in other occurences, the presence of a gene revealed by genome analysis raises the questions: are these genes really expressed? What are the molecular features of the putative proteins, if they are expressed? Where and when in the organism are they expressed? Consequently have they any specific activity justifying the presence of more isoforms in the organism? To answer to these questions we have produced antibodies against the recombinant proteins corresponding to the whole (VDAC1 and 2) or to substantial portions (VDAC3 and 4) of the known or predicted proteins. Immunohistological and transcriptional analysis has been performed, showing that VDAC2 and 3 are expressed, while VDAC4 was not detected. Structural predictions of VDAC3 are consistent with the presence of additional alpha-helices at the N-terminus of the protein.