Revision of hospital work organization using nurse and healthcare assistant workload indicators as decision aid tools.

BACKGROUND: Historically, governmental hospital organisation consisted in a heterogeneous distribution of staff and a fragmented logistical organisation without cross-functionality or sharing of resources between departments. This organisation could not last in a context of an evolving healthcare environment, changing patient profiles and hospital expenditure constraints. Cost-effective workforce regulation for optimal patient quality of care was urgently needed. The purpose of the study was to describe the reorganization that led to resource management no longer based on what has been achieved but based on a daily measured workload. METHODS: This prospective study used nursing intensity indicator, mirroring patient care needs, which was reported daily using VALPAReSO® software. Indirect care activities were recorded in departments of medicine, surgery and obstetrics. Based on data collected in 2012, a new organisation strategy was implemented and evaluated in 2015. RESULTS: Nursing intensity indicator analysis led to a reallocation of workforce per department, and the reinforcement unit (float pool) was managed based on this decision-aid tool for replacement and daily adequate staffing. The healthcare workflow audit resulted in the revision of five working tasks: time spent on handover, working time management, connections between services and the pharmacy, housekeeping, and food management. The reorganization took place at the same time as the transition to the development of very short-term care, resulting in a decrease in the number of full inpatient beds, which were therefore mainly occupied by heavier care profile patients. With the integrated strategy, this transition was achieved with constant staffing, and good overall patient satisfaction and working conditions were maintained. CONCLUSION: The reorganisation strategy was managed in a context of institutional commitment, coaching leadership built on close manager-employee interaction, a defragmented management between healthcare and all service providers, and a seamlessly dissemination and sharing of indicator information between healthcare managers, nurses and healthcare assistants. The process optimization allowed a better allocation of tasks and enabled nurses to refocus on patient care. Nursing intensity and indirect care indicators, when widely accepted, can be used as decision support tools for daily adequate staffing.

A novel human complement-related protein, C1r-like protease (C1r-LP), specifically cleaves pro-C1s.

The availability of the human genome sequence allowed us to identify a human complement-related, C1r-like protease gene (c1r-LP) located 2 kb centromeric of the C1r gene (c1r). Compared with c1r, c1r-LP carries a large deletion corresponding to exons 4-8 of c1r. The open reading frame of the C1r-LP cDNA predicts a 50 kDa modular protein displaying 52% amino acid residue identity with the corresponding regions of C1r and 75% identity with a previously described murine C1r-LP. The serine protease domain of C1r-LP, despite an overall similarity with the AGY group of complement serine proteases, has certain structural features characteristic of C2 and factor B, thus raising interesting evolutionary questions. Northern blotting demonstrated the expression of C1r-LP mRNA mainly in the liver and ELISA demonstrated the presence of the protein in human serum at a concentration of 5.5+/-0.9 microg/ml. Immunoprecipitation experiments failed to demonstrate an association of C1r-LP with the C1 complex in serum. Recombinant C1r-LP exhibits esterolytic activity against peptide thioesters with arginine at the P1 position, but its catalytic efficiency (kcat/K(m)) is lower than that of C1r and C1s. The enzymic activity of C1r-LP is inhibited by di-isopropyl fluorophosphate and also by C1 inhibitor, which forms stable complexes with the protease. Most importantly, C1r-LP also expresses proteolytic activity, cleaving pro-C1s into two fragments of sizes identical with those of the two chains of active C1s. Thus C1r-LP may provide a novel means for the formation of the classical pathway C3/C5 convertase.

A novel murine complement-related gene encoding a C1r-like serum protein.

C1r and C1s are highly specific serine proteases that initiate the classical pathway of complement activation. We recently demonstrated that, in the mouse, the genes encoding these proteins are duplicated. Analysis of the 5'-flanking region of the murine C1rA gene, the homologue of human C1r, revealed the presence of a novel gene encoding a C1r-like protein (c1r-LP). Although this gene carries a large deletion, it shows an overall structure similar to that of c1rA, suggesting that it may have arisen from a duplication of the C1r gene. The c1r-LP gene is expressed primarily in the liver, and is not regulated by lipopolysaccharide. The open reading frame of full-length cDNA clones encodes a pre-protein with a calculated molecular mass of 50.6 kDa which, except for an internal deletion of several modules, has a modular organization similar to that of C1r and shows 51% overall amino acid identity to corresponding regions of C1rA. Western blot analysis demonstrates the presence of C1r-LP in mouse serum. The serine protease domain of C1r-LP displays 60% amino acid residue identity to that of C1rA, however, certain atypical features of the active center, and primarily the absence of the activation/cleavage site, suggest that C1r-LP is either an atypical enzyme, or it lacks proteolytic activity, perhaps serving a regulatory function in the classical pathway.

Structure, function and molecular genetics of human and murine C1r.

C1r, the enzyme responsible for intrinsic activation of the C1 complex of complement, is a modular serine protease featuring an overall structural organization homologous to those of C1s and the mannan-binding lectin-associated serine proteases (MASPs). This review will initially summarize current information on the structure and function of C1r, with particular emphasis on the three-dimensional structure of its catalytic domain, which provides new insights into the activation mechanism of C1. The second part of this review will focus on recent discoveries dealing with a truncated, C1r-related protein, and the occurrence in the mouse of two isoforms, C1rA and C1rB, exhibiting tissue-specific expression patterns.

Complement C1r and C1s genes are duplicated in the mouse: differential expression generates alternative isomorphs in the liver and in the male reproductive system.

C1r and C1s are the serine proteases that form the catalytic unit of the C1 complex, the first component of complement. In the present study, we found that the genes encoding murine C1r and C1s are duplicated. One set of these genes, referred to as c1rA and c1sA, are primarily expressed in the liver and are therefore the homologues of the human C1r and C1s genes. The other two genes, termed c1rB and c1sB, are expressed exclusively in male reproductive tissues, specifically the coagulating gland and the prostate. The predicted C1rB and C1sB proteins share 96 and 93% amino acid identity with C1rA and C1sA respectively. Most of the substitutions are clustered in the serine protease domains, suggesting differences in catalytic efficiencies and/or substrate specificities or alternatively adaptation to different physiological environments. The high homology of C1rB and C1sB with C1rA and C1sA in the non-catalytic regions indicates that they are probably capable of assembling the C1 complex. The expression of alternative genes encoding isomorphs of activating components of complement in male reproductive tissues raises the possibility of new mechanisms of complement activation in the male genital tract or of novel functions for complement proteases in reproduction.