ABSTRACT
OBJECTIVE: This study was conducted to evaluate the relationship between job stress and quality of life for hospital workers by type of employment. METHODS: Data were obtained for 361 workers in a large hospital 172 of whom were categorized as typical workers defined by permanent employee and 189 of whom were categorized as atypical workers defined by fixed-term contraction. Job stress was assessed using the Korean Occupational Stress Scale-Short Form and the World Health Organization Quality of Life-BREF Questionnaire RESULTS: Atypical workers had significantly higher scores for job-related stress in the domains of insufficient control, over work, job insecurity, and lack of reward in the workplace compared with typical workers, who had higher scores for stress in the domains of job demands and occupational climate. Test scores also indicated that typical workers had a significantly better quality of life than atypical workers, especially in terms of mental health, social relationships and environment. CONCLUSION: These findings suggested that factors contributing to job-related stress were different between typical and atypical hospital and typical workers are likely to have a better quality of life.
Subject(s)
Climate , Contracts , Employment , Mental Health , Quality of Life , Reward , World Health OrganizationABSTRACT
In this study, the molecular mechanism of tyrosine phosphorylation of Roundabout (Robo), the transmembrane receptor for slits, was investigated. The tyrosine phosphorylation of intracellular portion of Robo was increased by the treatment of tyrosine phosphatase inhibitors in human embryonic kidney cells transfected with Robo. The Robo tyrosine phosphorylation was inhibited by the treatment of Src family kinase inhibitor, PP2. The co-transfection of constitutively active form of Fyn, not the dominant negative form of Fyn, and Robo dramatically enhanced the tyrosine phosphorylation of Robo. Furthermore, the SH2 domain of Fyn, which binds to phosphorylated tyrosine residues, interact with Robo, and the interaction was increased by the inhibition of tyrosine phosphatases. These findings indicate that the tyrosine phosphorylation of Robo is regulated by Fyn.