Publications by authors named "S Poggioli"

The integrated diagnosis of anaplastic oligodendroglioma, IDH mutant and 1p/19q co-deleted, grade III (O3 ) is a histomolecular entity that WHO 2016 classification distinguished from other diffuse gliomas by specific molecular alterations. In contrast, its cell portrait is less well known. The present study is focused on intertumor and intratumor, cell lineage-oriented, heterogeneity in O3 .

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Modification of proteins by reactive oxygen species is implicated in different disorders. The proteasome is a multicatalytic proteinase in charge of intracellular protein turnover and of oxidized proteins degradation. Consequently, proteasome function is very important in controlling the level of altered proteins in eukaryotic cells.

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Oxidatively modified proteins have been analyzed in aging human peripheral blood lymphocytes since protein modification by oxidation and other related pathways are believed to contribute to the intracellular age-related accumulation of damaged proteins, a process that has been associated with the cellular functional deficits that occur with age. Advanced glycation end products (AGE) were quantified and the pattern of glycated proteins analyzed by two-dimensional gel electrophoresis followed by Western blotting using an anti-AGE antibody raised against glycated RNAse. The protein silver stain and the immunoblot patterns were not superimposable, indicating that glycoxidative modifications are targeting only a restricted set of proteins.

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Advanced glycation end products (AGE) have been analyzed in aging human peripheral blood lymphocytes since protein glycation and glycoxidation are believed to contribute to the intracellular age-related accumulation of damaged proteins, a process that has been associated with the cellular functional deficits that occur with age. The appearance of AGE in cell lysates was monitored with an enzyme-linked immunosorbent assay using an anti-AGE antibody raised against glycated RNAse. When lymphocyte cytosolic extracts from old donors (86-91 years old) were compared with those from young donors (20-25 years old), a small but significant 40% increase of protein glycation was observed.

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The present study analyses differential polypeptide expression of seminal plasma from fertile and infertile men by two-dimensional gel electrophoresis. Optimization of solubilization of seminal plasma was obtained by using [3-(3-(cholamidopropyl) dimethyl-ammonio)-1-propane sulphonate] and chaotropic agent mixture in lysis buffer before separation in immobilized pH gradient for isoelectric focusing. A two-dimensional map of seminal plasma from a fertile man allowed the detection of about 750 spots.

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