Developing and testing an instrument for identifying performance incentives in the Greek health care sector

BACKGROUND: In the era of cost containment, managers are constantly pursuing increased organizational performance and productivity by aiming at the obvious target, i.e. the workforce. The health care sector, in which production processes are more complicated compared to other industries, is not an exception. In light of recent legislation in Greece in which efficiency improvement and achievement of specific performance targets are identified as undisputable health system goals, the purpose of this study was to develop a reliable and valid instrument for investigating the attitudes of Greek physicians, nurses and administrative personnel towards job-related aspects, and the extent to which these motivate them to improve performance and increase productivity. METHODS: A methodological exploratory design was employed in three phases: a) content development and assessment, which resulted in a 28-item instrument, b) pilot testing (N = 74) and c) field testing (N = 353). Internal consistency reliability was tested via Cronbach's alpha coefficient and factor analysis was used to identify the underlying constructs. Tests of scaling assumptions, according to the Multitrait-Multimethod Matrix, were used to confirm the hypothesized component structure. RESULTS: Four components, referring to intrinsic individual needs and external job-related aspects, were revealed and explain 59.61% of the variability. They were subsequently labeled: job attributes, remuneration, co-workers and achievement. Nine items not meeting item-scale criteria were removed, resulting in a 19-item instrument. Scale reliability ranged from 0.782 to 0.901 and internal item consistency and discriminant validity criteria were satisfied. CONCLUSION: Overall, the instrument appears to be a promising tool for hospital administrations in their attempt to identify job-related factors, which motivate their employees. The psychometric properties were good and warrant administration to a larger sample of employees in the Greek healthcare system

Translocation of microfilament-associated inhibitory guanine-nucleotide-binding proteins to the plasma membrane in myeloid differentiated human leukemia (HL-60) cells

The cytoskeletal localization of inhibitory guanine-nucleotide-binding (Gi) proteins and the coupling of these proteins to formyl peptide receptors were studied in myeloid differentiated human leukemia (HL-60) cells. Treatment of HL-60 cells with cytochalasin B or botulinum C2 toxin, which leads to the disruption of microfilaments, increased the binding of the stable GTP analogue guanosine 5'[gamma-thio]triphosphate (GTPS[S]) to permeabilized cells by about 30%. In contrast, the microtubule-disrupting agents colchicine and vinblastine, and cytochalasin B treatment of isolated HL-60 membranes did not affect GTP[S] binding. The stimulatory effect of cytochalasin B treatment was concentration and time dependent, with maximal increases observed at 5 micrograms/ml cytochalasin B and an incubation time of 10 min, and was counteracted by the F-actin-stabilizing toxin phalloidin. Cytochalasin B treatment increased the amount of G proteins activated by chemoattractant receptors by about 25%. Furthermore, the number of Gi-protein-coupled receptors for the chemoattractant, N-formyl-Met-Leu-Phe, was increased by about 25% upon cytochalasin B treatment. Based on these functional data, which suggest an association of G proteins with actin filaments, the Triton X-100 (1%)-insoluble cytoskeleton was analyzed for the presence of G proteins. Gia subunits were detected in the cytoskeleton preparations, both by specific antisera and by pertussis-toxin -catalyzed ADP-ribosylation. Cytochalasin B pretreatment depleted the cytoskeleton in Gialpha, with an approximately 20% concomitant increase in membrane Gialpha content. In conclusion, evidence is presented that part of the cellular Gia is localized at actin filaments in HL-60 cells. After filament disruption, these Gia subunits seem to be translocated to the plasma membrance, where they can productively interact with chemoattractant receptor