How appropriate is the use of rehabilitation facilities? Assessment by an evaluation tool based on the AEP protocol.

BACKGROUND: During the last few decades, an increasing attention has been drawn to public health expenditure and resource use. The increasing aging population has highlighted the need to deliver post-acute care and to assess its appropriateness. The "PRUO rehab" (Protocollo di Revisione dell'Utilizzo dell'Ospedale riabilitativo) protocol was realized and validated to assess the appropriateness of use of rehabilitation units. The aims of this study were to test the validity of the PRUO-rehab tool and to analyse the causes for Inappropriate Hospital Stay (IPS) in rehabilitation units. METHODS: The PRUO rehab tool was retrospectively applied to the medical records of 502 patients who stayed at least overnight in one of ten different rehabilitation units set in Northern Italy, during 2007. RESULTS: The tool was valid and the inappropriate patient stay (IPS) score was 25.0%. CONCLUSION: Although reasonably low, the IPS indicates that the rehabilitation structures analysed could be used more efficiently.

A telephone survey on the reasons for non-attendance in a dermatological clinic.

AIM: Long waiting time before obtain medical attention is a significant problem that affects all specialties and especially dermatology, where a quick observation is required because of the rapid mutation of skin lesions pattern. Non-attendance (NA) is one of the aspects that is most involved in the length of waiting lists. The aim of this study was to investigate the different reasons for NA in the dermatological clinic as to improve the booking system and allow patients to be visited in a shorter time. METHODS: All the patients who failed to attend a visit, booked in the dermatological service during a two months period, were contacted by telephone to determine the reasons for having missed the appointment. For each patient details as age, sex, kind of visit (initial visit, follow-up visit or visit with priority level) and type of clinic (general dermatology, second level dermatology or paediatric dermatology) were collected and analyzed. RESULTS: The overall NA rate was 11.19% and different reasons for NA were found, namely forgetfulness of the appointment, work-related problems and concomitant illness. CONCLUSION: The most frequent reason for NA is forgetfulness of the appointment and it could be explained by the long time elapsing between booking and visit. Different techniques to reduce forgetfulness have been suggested; in our case the use of a unique call centre that coordinates booking for all the health structures in Milan and the sending of a reminder mobile message have led to good results with a NA rate lower than in other studies.

Purification of human recombinant interleukin 1 receptor antagonist proteins upon Bacillus subtilis sporulation.

Human interleukin 1 receptor antagonist (IL-1ra) and IL-1ra mutants were constitutively expressed in recombinant Bacillus subtilis in endocellular and active form. In order to optimize the purification of the recombinant proteins, a new method has been developed. After bacterial growth in fermenter, release of recombinant protein was achieved by starvation-induced sporulation. The sporulation supernatant was recovered by centrifugation, filtered, and subjected sequentially to cation- and anion-exchange chromatography. Alternatively, the fermenter's contents were directly subjected to expanded bed adsorption on a Streamline cation-exchange column, thus avoiding the centrifugation and filtration steps. Up to 88 mg of biological active purified recombinant protein per liter of culture was obtained, with a 72-79% recovery and 98% purity, depending on the molecule. By using the method described here, it is possible to achieve a spontaneous release of recombinant proteins expressed endocellularly at high levels in B. subtilis without need of a cell breakage step. Thus, this method could allow purification of the endocellular recombinant protein as if it were secreted. Furthermore, when using the expanded bed adsorption, highly purified protein was obtained in only two steps after sporulation. Among the advantages of the method, one of the most relevant is the possibility of keeping the system closed up to completion of the first purification step.

Transfected type II interleukin-1 receptor impairs responsiveness of human keratinocytes to interleukin-1.

Of the two known types of specific receptors for interleukin (IL)-1, the function of the type II IL-1 receptor (IL-1RII) is still elusive. IL-1RII is allegedly devoid of signaling capacity and is therefore thought to act by trapping and inhibiting IL-1. To directly assess the functional role of IL-1RII, a human keratinocyte cell line has been stably transfected with a cDNA coding for IL-1RII, and its responsiveness to IL-1 has been compared with that of nontransfected cells. Parental cells express IL-1RI and are responsive to low doses of IL-1, whereas transfected cells overexpress IL-1RII, both in its membrane and soluble form, and show a dramatically impaired response to IL-1. Selective block of IL-1RII restores the ability of transfected keratinocytes to respond to IL-1, indicating that the overexpressed IL-1RII is in fact uniquely responsible for their refractoriness to IL-1. The main mechanism of unresponsiveness in transfected keratinocytes appears to be the capture and neutralization of IL-1 by the soluble form of IL-1RII.

Mapping of receptor binding sites on IL-1 beta by reconstruction of IL-1ra-like domains.

Upon structure comparison between IL-1 beta and its antagonist IL-1ra, single or multiple residues along the IL-1 beta sequence were replaced with the corresponding amino acids present in the IL-1ra protein, in the attempt to identify sites important for receptor binding and for biologic activity on the two molecules. Ten of fifteen mutant proteins had activity comparable to that of wild-type IL-1 beta in three different biologic assays and in receptor binding, indicating that the introduced changes did not influence the functional structure of the protein. Conversely, three mutants (SMIL-9: 127/263 R/T-->W/Y; SMIL-10: 125/127/263/265 T/R/T/Q-->R/W/Y/E; SMIL-15:222/227 I/E-->S/S) showed an increased binding capacity for IL-1RI, not paralleled by increased agonist activity, indicating that the introduced IL-1ra residues could be involved in the nonagonist IL-1RI binding site. On the other hand, two mutants showed diminished binding capacity with concomitant decrease in biologic activity. Both mutants (SMIL-1, five substitutions in the loop 202-214; and SMIL-3, total replacement of the loop 164-173 with the IL-1ra stretch 52-55) included substitutions of residues allegedly important for agonist binding to IL-1RI. Mutant SMIL-3 showed the most profound reduction in binding capacity for IL-1RI (CDw121a) and a more than 1,000-fold reduced biologic activity both in vitro and in vivo, but it retained full capacity of binding to IL-1RII (CDw121b) and acted as a selective antagonist of IL-1RII. From these results the following conclusions can be drawn. IL-1 beta binds to IL-1RI and to IL-1RII through different sites, and the loop 164-173 appears as one of the areas involved in the selective interaction with IL-1RI. Agonist (IL-1 beta) and nonagonist (IL-1ra) binding to IL-1RI occur through distinct sites, with loops 164-173 and 202-214 of IL-1 beta identified as two of the sites selectively involved in agonist binding to the activating receptor.