Listening to people to cure people: the LpCp - tool, an instrument to evaluate hospital humanization.

BACKGROUND: In the healthcare environment, nowadays, only a few among the available evaluation systems pay enough attention to certain social sustainability aspects. Among these, humanization plays a key role in an environment, like hospitals, where the mental and physical well-being of patients and healthcare operators is crucial. Our research project, known as 'SustHealth', is focused on the deficiencies of the evaluation methodology and aims at developing an assessment system related to a questionnaire-based investigation capable of revealing the most influential conditions and dynamics in people's hospital experience, while also recommending areas in hospitals where efforts can be made to sustain improvement strategies. METHODS: The humanization of healthcare structures began with a significant investigation to assess all the major evaluation tools in both hospitals - to better understand the physical and emotional interactions in the structure-user ratio - and other areas. This helped understand the strengths and criticalities of the systems that were examined. This first step also allowed to shed light on the most important aspects to keep in mind when developing an evaluation system. During the operational steps an all-new LpCp - tool (Listening to people to Cure people) was created, which includes a questionnaire-based investigation and processing software, and its application for beta-testing in a 600-bed hospital in Milan. RESULTS: The LpCp - tool proved to be effective and capable of finding the deficiencies and potential in the examined hospital. Considering different themes through alternative viewpoints (staff, patients/visitors, technicians, etc.), the tool has allowed underlining different perceptions of the same place and also provided sound information to guide healthcare management in taking informed decisions about specific problems or users. Former interesting results show an inadequate appraisal about e.g. on-site facilities or recreational activities and a lack of perception on existing services by users (e.g. translation, P.R.). CONCLUSIONS: The LpCp - tool was presented to other healthcare centres in Milan for wider-scale testing. Therefore, the LpCp - tool will hopefully increase healthcare companies' responsiveness towards improving comfort and humanization levels in hospitals. Sometimes all that is needed are small and inexpensive actions that often improve a hospital user's experience, and often important services are not used due to a lack of communication and information.

Identification of the human mitochondrial S-adenosylmethionine transporter: bacterial expression, reconstitution, functional characterization and tissue distribution.

The mitochondrial carriers are a family of transport proteins that, with a few exceptions, are found in the inner membranes of mitochondria. They shuttle metabolites and cofactors through this membrane, and connect cytoplasmic functions with others in the matrix. SAM (S-adenosylmethionine) has to be transported into the mitochondria where it is converted into S-adenosylhomocysteine in methylation reactions of DNA, RNA and proteins. The transport of SAM has been investigated in rat liver mitochondria, but no protein has ever been associated with this activity. By using information derived from the phylogenetically distant yeast mitochondrial carrier for SAM and from related human expressed sequence tags, a human cDNA sequence was completed. This sequence was overexpressed in bacteria, and its product was purified, reconstituted into phospholipid vesicles and identified from its transport properties as the human mitochondrial SAM carrier (SAMC). Unlike the yeast orthologue, SAMC catalysed virtually only countertransport, exhibited a higher transport affinity for SAM and was strongly inhibited by tannic acid and Bromocresol Purple. SAMC was found to be expressed in all human tissues examined and was localized to the mitochondria. The physiological role of SAMC is probably to exchange cytosolic SAM for mitochondrial S-adenosylhomocysteine. This is the first report describing the identification and characterization of the human SAMC and its gene.