Domanda di istruzione universitaria in Sardegna da parte degli studenti delle scuole secondarie

Col presente lavoro si cercherà di offrire alcuni spunti di riflessione sui problemi dell’efficienza e dell’efficacia del sistema universitario principalmente attraverso uno studio sull’intenzione di accedere all’istruzione universitaria espressa da un insieme di studenti dell’ultimo anno delle scuole medie superiori. Si farà, cioè, riferimento a quella che comunemente viene indicata come la domanda potenziale di istruzione universitaria. Il lavoro è articolato in due parti, nella prima vengono illustrate le dinamiche evolutive, a partire dagli anni Cinquanta, della citata domanda di istruzione con riferimento all’università italiana in generale ed agli atenei sardi in particolare. Nella seconda, la domanda di istruzione universitaria viene analizzata attraverso un’indagine condotta sugli studenti delle scuole medie superiori di tre province sarde: viene descritto l’insieme dei rispondenti utilizzato per l’analisi della stessa e viene presentato un modello logit a risposta politomica attraverso il quale, considerando alcuni predittori quali il sesso e la scuola di provenienza, è stata modellata la variabile dipendente a tre modalità (Sì, Non so, No), relativa al quesito posto agli studenti delle scuole medie “Intendi proseguire gli studi dopo il diploma di maturità?”

Patient-reported outcome measures (PROMs) after elective hip, knee and shoulder arthroplasty: protocol for a prospective cohort study

Background The number of hip, knee and shoulder arthroplasties continues to rise worldwide. The Organization for Economic Cooperation and Development has launched an initiative (called PaRIS Initiative) for the systematic collection of Patient Reported Outcome Measures (PROMs) in patients undergoing elective hip and knee arthroplasty. The Rizzoli Orthopedic Institute (IOR) was selected as a pilot center for the launch of the Initiative in Italy given that IOR hosts the Registry of Orthopedic Prosthetic Implants (RIPO), a region-wide registry which collects joint implant data from all the hospitals in the Emilia-Romagna Region. In this specific geographic area information related to PROMs after joint replacement is unknown. This paper describes the protocol of a study (PaRIS-IOR) that aims to implement the collection of a set of PROMs within an existing implant registry in Italy. The study will also investigate the temporal trend of PROMs in relation to the type of prosthesis and the type of surgical intervention. Methods The PaRIS-IOR study is a prospective, single site, cohort study that consists of the administration of PROMs questionnaires to patients on the list for elective arthroplasty. The questionnaires will be administered to the study population within 30 days before surgery, and then at 6 and 12 months following surgery. The study population will consist of consecutive adult patients undergoing either hip, knee or shoulder arthroplasty. The collected data will be linked with those routinely collected by the RIPO in order to assess the temporal trend of PROMs in relation to the type of prosthesis and the type of surgical intervention. Discussion The PaRIS-IOR study could have important implications in targeting the factors influencing functional outcomes and quality of life reported by patients after hip, knee and shoulder arthroplasty, and will also represent the first systematic collection of PROMs related to arthroplasty in Italy

Detection and exploitation of white lupin (Lupinus albus L.) genetic variation for seed γ-conglutin content

The seed γ-conglutin protein fraction of white lupin has particular pharmacological interest, but its industrial production is hindered by low content in the seed. This study provides an unprecedented assessment of genotypic and environmental variation for seed content and production of γ-conglutin, exploring also the ability of Near-Infrared Spectroscopy (NIRS) to predict seed γ-conglutin content. Significant (P < 0.01) genetic variation for seed γ-conglutin content emerged among ten genotypes (cultivars or breeding lines) across three environments (range: 1.59-2.02 %) and five genotypes in other two environments (range: 1.47-1.80 %). Genotype variation was found also for seed protein content and γ-conglutin proportion on total protein, the latter trait having higher impact than the former on genotype variation for seed γ-conglutin content. The production of γ-conglutin per unit area was affected also by genotype yielding ability beside genotype seed γ-conglutin content. No genotype × environment interaction was detected for any γ-conglutin trait. NIRS-based prediction based on cross-validations was only moderately accurate for seed γ-conglutin content (R2 = 0.66), while being accurate for seed protein content (R2 = 0.95). In conclusion, breeding for higher seed γ-conglutin content is feasible using data from very few test sites and, to some extent, NIRS-based predictions

Patient reported outcomes measures (PROMs) trajectories after elective hip arthroplasty: a latent class and growth mixture analysis

Patient-reported outcome measures (PROMs) are an extensively used tool to assess and improve the quality of healthcare services. PROMs can be related to individual demographic and clinical characteristics in patients undergoing hip arthroplasty (HA). The aim of this study is to identify distinct subgroups of patients with unique trajectories of PROMS scores and to determine patients' features associated with these subgroups

A Crucial Role for the Protein Quality Control System in Motor Neuron Diseases.

Motor neuron diseases (MNDs) are fatal diseases characterized by loss of motor neurons in the brain cortex, in the bulbar region, and/or in the anterior horns of the spinal cord. While generally sporadic, inherited forms linked to mutant genes encoding altered RNA/protein products have also been described. Several different mechanisms have been found altered or dysfunctional in MNDs, like the protein quality control (PQC) system. In this review, we will discuss how the PQC system is affected in two MNDs-spinal and bulbar muscular atrophy (SBMA) and amyotrophic lateral sclerosis (ALS)-and how this affects the clearance of aberrantly folded proteins, which accumulate in motor neurons, inducing dysfunctions and their death. In addition, we will discuss how the PQC system can be targeted to restore proper cell function, enhancing the survival of affected cells in MNDs

The Regulation of the Small Heat Shock Protein B8 in Misfolding Protein Diseases Causing Motoneuronal and Muscle Cell Death

Misfolding protein diseases are a wide class of disorders in which the aberrantly folded protein aggregates accumulate in affected cells. In the brain and in the skeletal muscle, misfolded protein accumulation induces a variety of cell dysfunctions that frequently lead to cell death. In motoneuron diseases (MNDs), misfolded proteins accumulate primarily in motoneurons, glial cells and/or skeletal muscle cells, altering motor function. The deleterious effects of misfolded proteins can be counteracted by the activity of the protein quality control (PQC) system, composed of chaperone proteins and degradative systems. Here, we focus on a PQC system component: heat shock protein family B (small) member 8 (HSPB8), a chaperone induced by harmful stressful events, including proteotoxicity. In motoneuron and muscle cells, misfolded proteins activate HSPB8 transcription and enhance HSPB8 levels, which contributes to prevent aggregate formation and their harmful effects. HSPB8 acts not only as a chaperone, but also facilitates the autophagy process, to enable the efficient clearance of the misfolded proteins. HSPB8 acts as a dimer bound to the HSP70 co-chaperone BAG3, a scaffold protein that is also capable of binding to HSP70 (associated with the E3-ligase CHIP) and dynein. When this complex is formed, it is transported by dynein to the microtubule organization center (MTOC), where aggresomes are formed. Here, misfolded proteins are engulfed into nascent autophagosomes to be degraded via the chaperone-assisted selective autophagy (CASA). When CASA is insufficient or impaired, HSP70 and CHIP associate with an alternative co-chaperone, BAG1, which routes misfolded proteins to the proteasome for degradation. The finely tuned equilibrium between proteasome and CASA activity is thought to be crucial for maintaining the functional cell homeostasis during proteotoxic stresses, which in turn is essential for cell survival. This fine equilibrium seems to be altered in MNDs, like Amyotrophic lateral sclerosis (ALS) and spinal and bulbar muscular atrophy (SBMA), contributing to the onset and the progression of disease. Here, we will review how misfolded proteins may affect the PQC system and how the proper activity of this system can be restored by boosting or regulating HSPB8 activity, with the aim to ameliorate disease progression in these two fatal MNDs

The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are two neurodegenerative diseases in which similar pathogenic mechanisms are involved. Both diseases associate to the high propensity of specific misfolded proteins, like TDP-43 or FUS, to mislocalize and aggregate. This is partly due to their intrinsic biophysical properties and partly as a consequence of failure of the neuronal protein quality control (PQC) system. Several familial ALS/FTD cases are linked to an expansion of a repeated G4C2 hexanucleotide sequence present in the C9ORF72 gene. The G4C2, which localizes in an untranslated region of the C9ORF72 transcript, drives an unconventional repeat-associated ATG-independent translation. This leads to the synthesis of five different dipeptide repeat proteins (DPRs), which are not âclassicalâ misfolded proteins, but generate aberrant aggregation-prone unfolded conformations poorly removed by the PQC system. The DPRs accumulate into p62/SQSTM1 and ubiquitin positive inclusions. Here, we analyzed the biochemical behavior of the five DPRs in immortalized motoneurons. Our data suggest that while the DPRs are mainly processed via autophagy, this system is unable to fully clear their aggregated forms, and thus they tend to accumulate in basal conditions. Overexpression of the small heat shock protein B8 (HSPB8), which facilitates the autophagy-mediated disposal of a large variety of classical misfolded aggregation-prone proteins, significantly decreased the accumulation of most DPR insoluble species. Thus, the induction of HSPB8 might represent a valid approach to decrease DPR-mediated toxicity and maintain motoneuron viability

Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target Cells

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that primarily affects motoneurons, while non-neuronal cells may contribute to disease onset and progression. Most ALS cases are characterized by the mislocalization and aggregation of the TAR DNA binding protein 43 (TDP-43) in affected cells. TDP-43 aggregates contain C-terminal TDP-43 fragments of 35 kDa (TDP-35) and 25 kDa (TDP-25) and have been mainly studied in motoneurons, while little is currently known about their rate of accumulation and clearance in myoblasts. Here, we performed a comparative study in immortalized motoneuronal like (NSC34; i-motoneurons) cells and stabilized myoblasts (C2C12; s-myoblasts) to evaluate if these two cell types differentially accumulate and clear TDP forms. The most aggregating specie in i-motoneurons is the TDP-25 fragment, mainly constituted by the \u201cprion-like\u201d domain of TDP-43. To a lower extent, TDP-25 also aggregates in s-myoblasts. In both cell types, all TDP species are cleared by proteasome, but TDP-25 impairs autophagy. Interestingly, the routing of TDP-25 fragment to proteasome, by overexpressing BAG1, or to autophagy, by overexpressing HSPB8 or BAG3 decreased its accumulation in both cell types. These results demonstrate that promoting the chaperone-assisted clearance of ALS-linked proteins is beneficial not only in motoneurons but also in myoblasts