Objectives: propofol is a short-acting, hypnotic agent that is increasingly being used for gastrointestinal endoscopic sedation. There are concerns about the use of propofol by non anesthesiologists due to its potential for respiratory and cardiovascular depression. This report describes our experience concerning effectiveness and safety of propofol administered in endoscopic procedures by the endoscopist and the assistant nurse.Methods: in this prospective study, a total of 102 consecutive endoscopies (60 colonoscopies and 42 upper endoscopies) performed under sedation with propofol were included. In 27 (26.47%) endoscopies propofol was administered alone and in 75 endoscopies (73.53%) it was combined with benzodiazepines and/or opioids. Seventy-six (74.51%) endoscopies were performed in patients under 65 years of age and 26 (25.49%) in patients over 65 years of age. Ninety-one (89.22%) endoscopies were performed in patients with low surgical risk (ASA I-II) and 11 (10.78%) in patients with high surgical risk. The medication was administered by the endoscopist that performed the procedure and the assistant nurse.Results: the mean dose of propofol used was 72.14 mg for gastroscopies and 71.33 for colonoscopies (p = 0.92). The mean dose of propofol when infused alone was 84.81 mg whereas in combination with benzodiazepines/opioids was 66.93 mg (p = 0.06). The doses of propofol required were lower for those colonoscopies in which midazolam and/or meperidine was combined and in patients over 65 years of age (p = 0.006 y p = 0.001, respectively). Eleven (10.8%) minor complications were reported, and managed by the own endoscopist. Patients had no memories of the procedure. The tolerance rated by the endoscopist was excellent-good, fair, bad-very bad in 83, 5 and 12% of the gastroscopies and in 79, 8 and 13% of the colonoscopies respectively. Nevertheless bad tolerance did not hinder the completion of the procedure in any case.Conclusions: the administration of propofol by the endoscopist and the assistant nurse, is an effective and safe method of sedation in patients of low and high-risk as well as in elderly patients. The doses of propofol required for an adequate sedation were lower in patients over 65 years of age and for colonoscopies in which medication was combined.

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Background “It's not what we do, it's the way that we do it”. Never has this maxim been truer in proteomics than now. Mass Spectrometry‐based proteomics/phosphoproteomics tools are critical to understand the structure and dynamics (spatial and temporal) of signalling that engages and migrates through the entire proteome. Approaches such as affinity purification followed by Mass Spectrometry (MS) have been used to elucidate relevant biological questions disease vs. health. Thousands of proteins interact via physical and chemical association. Moreover, certain proteins can covalently modify other proteins post‐translationally. These post‐translational modifications (PTMs) ultimately give rise to the emergent functions of cells in sequence, space and time. Findings Understanding the functions of phosphorylated proteins thus requires one to study proteomes as linked‐systems rather than collections of individual protein molecules. Indeed, the interacting proteome or protein‐network knowledge has recently received much attention, as network‐systems (signalling pathways) are effective snapshots in time, of the proteome as a whole. MS approaches are clearly essential, in spite of the difficulties of some low abundance proteins for future clinical advances. Conclusion Clinical proteomics‐MS has come a long way in the past decade in terms of technology/platform development, protein chemistry, and together with bioinformatics and other OMICS tools to identify molecular signatures of diseases based on protein pathways and signalling cascades. Hence, there is great promise for disease diagnosis, prognosis, and prediction of therapeutic outcome on an individualized basis. However, and as a general rule, without correct study design, strategy and implementation of robust analytical methodologies, the efforts, efficiency and expectations to make biomarkers (especially phosphorylated kinases) a useful reality in the near future, can easily be hampered.

Reversible protein phosphorylation is one of the most important forms of cellular regulation. Thus, phosphoproteomic analysis of protein phosphorylation in cells is a powerful tool to evaluate cell functional status. The importance of protein kinase-regulated signal transduction pathways in human cancer has led to the development of drugs that inhibit protein kinases at the apex or intermediary levels of these pathways. Phosphoproteomic analysis of these signalling pathways will provide important insights for operation and connectivity of these pathways to facilitate identification of the best targets for cancer therapies. Enrichment of phosphorylated proteins or peptides from tissue or bodily fluid samples is required. The application of technologies such as phosphoenrichments, mass spectrometry (MS) coupled to bioinformatics tools is crucial for the identification and quantification of protein phosphorylation sites for advancing in such relevant clinical research. A combination of different phosphopeptide enrichments, quantitative techniques and bioinformatic tools is necessary to achieve good phospho-regulation data and good structural analysis of protein studies. The current and most useful proteomics and bioinformatics techniques will be explained with research examples. Our aim in this article is to be helpful for cancer research via detailing proteomics and bioinformatic tools.

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