ABSTRACT
INTRODUCTION: Hospital Value-Based Purchasing (HVBP) is an initiative that rewards acute-care hospitals with incentive payments for the quality of care they provide. A hospital's trauma certification has the potential to influence HVBP scores as attaining the certification provides indication of the service quality offered by the hospital. As such, this study focuses on hospitals' level of trauma certification attainment through the American College of Surgeons and whether this certification is associated with greater HVBP. METHODS: A retrospective review of the 2015 HVBP database, 2015 Area Health Resources Files (AHRF) database, and the 2015 American Hospital Association (AHA) database is utilized, and propensity score matching was employed to determine the association between level of trauma certification and scores on HVBP dimensions. RESULTS: Results reveal trauma certification is associated with lower HVBP domain scores when compared to hospitals without trauma certification. In addition, hospitals with a greater degree of trauma specialization were associated with lower total performance score and efficiency domain scores. CONCLUSIONS: Although payers attempt to connect hospital reimbursements with quality and outcomes, unintended consequences may occur. In response to these results, HVBP risk adjustment and scoring methods should receive further scrutiny.
Subject(s)
Critical Care/organization & administration , Critical Care/statistics & numerical data , Economics, Hospital/organization & administration , Economics, Hospital/statistics & numerical data , Emergency Medical Services/organization & administration , Emergency Medical Services/statistics & numerical data , Value-Based Purchasing/organization & administration , Value-Based Purchasing/statistics & numerical data , Humans , Retrospective Studies , United StatesABSTRACT
The mouse major urinary proteins (Mups) are encoded by a large family of highly related genes clustered on chromosome 4. Mups, synthesized primarily and abundantly in the liver and secreted through the kidneys, exhibit male-biased expression. Mups bind a variety of volatile ligands; these ligands, and Mup proteins themselves, influence numerous behavioral traits. Although urinary Mup protein levels vary between inbred mouse strains, this difference is most pronounced in BALB/cJ mice, which have dramatically low urinary Mup levels; this BALB/cJ trait had been mapped to a locus on chromosome 15. We previously identified Zhx2 (zinc fingers and homeoboxes 2) as a regulator of numerous liver-enriched genes. Zhx2 is located on chromosome 15, and a natural hypomorphic mutation in the BALB/cJ Zhx2 allele dramatically reduces Zhx2 expression. Based on these data, we hypothesized that reduced Zhx2 levels are responsible for lower Mup expression in BALB/cJ mice. Using both transgenic and knock-out mice along with in vitro assays, our data show that Zhx2 binds Mup promoters and is required for high levels of Mup expression in the adult liver. In contrast to previously identified Zhx2 targets that appear to be repressed by Zhx2, Mup genes are positively regulated by Zhx2. These data identify Zhx2 as a novel regulator of Mup expression and indicate that Zhx2 activates as well as represses expression of target genes.
Subject(s)
Homeodomain Proteins/physiology , Liver/metabolism , Proteins/physiology , Transcription Factors/physiology , Alleles , Animals , Cell Line , Chromatin/metabolism , HEK293 Cells , Hep G2 Cells , Humans , Kidney/metabolism , Ligands , Male , Mice , Mice, Inbred BALB C , Mice, Knockout , Promoter Regions, Genetic , Protein BindingABSTRACT
Analogues of the compound 2,5-di-tert-butylhydroquinone (BHQ) are capable of inhibiting the enzyme sarco/endoplasmic reticulum ATPase (SERCA) in the low micromolar and submicromolar concentration ranges. Not only are SERCA inhibitors valuable research tools, but they also have potential medicinal value as agents against prostate cancer. This study describes the synthesis of 13 compounds representing several classes of BHQ analogues, such as hydroquinones with a single aromatic substituent, symmetrically and unsymmetrically disubstituted hydroquinones, and hydroquinones with omega-amino acid tethers attached to their hydroxyl groups. Structure-activity relationships were established by measuring the inhibitory potencies of all synthesized compounds in bioassays. The assays were complemented by computational ligand docking for an analysis of the relevant ligand/receptor interactions.