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1.
Article in German | MEDLINE | ID: mdl-31720739

ABSTRACT

BACKGROUND: Profound transformations in the German healthcare system lead to intense working conditions for young employees in inpatient care. Published data suggest associated health risks. OBJECTIVES: This investigation aims to assess current stress factors, their consequences, and subjective measures for improvement. METHODS: During September 2017, a cross-sectional survey was conducted among physicians and nurses ≤35 years of age and with work experience in inpatient care not exceeding six years. Field access was gained via seven scientific and professional societies. The electronic questionnaire consisted of mainly validated instruments. Regression models included confounders into the final data analysis. RESULTS: Included in the final data analysis were 1060 complete cases. The overall response rate was 13%. Different stress factors (e.g. time-related or psychosocial) were found at high levels. These stress factors were connected to reduced health and higher risk of burnout. Furthermore, they were associated with inferior perceived quality of care. Young physicians claimed less documentation requirements and less intense working conditions. Young nurses demanded fair salary and an appropriate nurse-patient allocation. CONCLUSION: Today's working conditions in inpatient care are a threat to the health status of young employees. General conditions, which ensure a sustainable healthy and effective working environment, need to be ensured.


Subject(s)
Burnout, Professional , Physicians , Adult , Cross-Sectional Studies , Germany , Health Status , Humans , Surveys and Questionnaires
4.
PLoS One ; 7(7): e39848, 2012.
Article in English | MEDLINE | ID: mdl-22808067

ABSTRACT

The bacterial adenylyl cyclase toxins CyaA from Bordetella pertussis and edema factor from Bacillus anthracis as well as soluble guanylyl cyclase α(1)ß(1) synthesize the cyclic pyrimidine nucleotide cCMP. These data raise the question to which effector proteins cCMP binds. Recently, we reported that cCMP activates the regulatory subunits RIα and RIIα of cAMP-dependent protein kinase. In this study, we used two cCMP agarose matrices as novel tools in combination with immunoblotting and mass spectrometry to identify cCMP-binding proteins. In agreement with our functional data, RIα and RIIα were identified as cCMP-binding proteins. These data corroborate the notion that cAMP-dependent protein kinase may serve as a cCMP target.


Subject(s)
Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit/metabolism , Cyclic AMP-Dependent Protein Kinase RIalpha Subunit/metabolism , Cyclic CMP/metabolism , Sepharose/chemistry , Adenylate Cyclase Toxin/metabolism , Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit/genetics , Cyclic AMP-Dependent Protein Kinase RIalpha Subunit/genetics , Cyclic CMP/chemistry , Gene Expression Regulation , Guanylate Cyclase/genetics , Guanylate Cyclase/metabolism , HEK293 Cells , HL-60 Cells , HeLa Cells , Humans , Immunoblotting , Isoenzymes/genetics , Isoenzymes/metabolism , Mass Spectrometry , Protein Binding , Signal Transduction
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