487 research outputs found

    The Impact of Balance Billing Laws on Network Provider Participation: Evidence from Three State Laws

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    Surprise balance billing laws have been passed to protect policyholders from being balance billed for surprise out-of-network services. However, little is known about the impacts of surprise balance billing laws without specific payment standards or guidance on providers’ network participation. Existing research only suggests that balance billing laws with specific payment standards can impact provider’s network participation. I conduct three empirical studies of the surprise balance billing laws in Illinois, Florida and Arizona, none of which has specific payment standards or guidance for surprise out-of-network services. In the analysis of the 2011 Illinois balance billing law and the 2016 Florida balance billing law, I use MarketScan data and examine the laws’ impacts on surprise balance billing prevalence in in-network emergent and non-emergent admissions for Anesthesiology, Pathology, Radiology and Emergence Medicine. For the 2017 Arizona balance billing law, I use the combined Vericred provider and network data and Centers for Medicare and Medicaid Services data to assess its impacts on providers’ network participation rate. I find the 2011 Illinois balance billing law, which does not have payment standards and guidance, does not impact the prevalence of surprise out-of-network services except for Radiology services among emergent admissions. Similarly, the 2017 Arizona balance billing law, which also does not have payment standards and guidance, has no impact on the providers’ network participation rate except for Emergent Medicine providers. On the other hand, the 2016 Florida balance billing law, which has payment standards in a range, does significantly impact the prevalence of surprise out-of-network services although the impacts are heterogeneous across different medical fields with a higher prevalence of surprise out-of-network services in Anesthesiology and a lower prevalence in Pathology and Radiology. These results suggest that not only specific payment standards for surprise out-of-network services but also payment standards in a range can prompt providers to change their network participation decisions. On the other hand, when balance billing laws do not have payment standards or guidance, it may be difficult for providers to evaluate the payment rates for surprise out-of-network services. Therefore, providers tend to keep their current network participation decision

    Evaluation of the volatile profile of <i>Tuber liyuanum</i> by HS-SPME with GC-MS

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    <p>The volatile components of <i>Tuber liyuanum</i> were determined by HS-SPME with GC-MS for the first time. The effects of different fibre coating, extraction time, extraction temperature and sample amount were studied to get optimal extraction conditions. The optimal conditions were SPME fibre of Carboxen/PDMS, extraction time of 40 min, extraction temperature of 80 °C, sample amount of 2 g. Under these conditions 57 compounds in volatile of <i>T. liyuanum</i> were detected with a resemblance percentage above 80%. Aldehydes and aromatics were the main chemical families identified. The contribution of 3-Octanone(11.67%), phenylethyl alcohol (10.60%), isopentana (9.29%) and methylbutana (8.06%) for the total volatile profile were more significant in <i>T. liyuanum</i> than other compounds.</p

    MARVELD1 Inhibits Nonsense-Mediated RNA Decay by Repressing Serine Phosphorylation of UPF1

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    <div><p>We have observed low expression levels of MARVELD1, a novel tumor repressor, in multiple tumors; however, its function in normal cells has not been explored. We recently reported that MARVELD1 interacts with importin β1, which plays an important role in nonsense-mediated RNA decay(NMD). Here, we demonstrate that MARVELD1 substantially inhibits nonsense-mediated RNA decay by decreasing the pioneer round of translation but not steady-state translation, and we identify MARVELD1 as an important component of the molecular machinery containing UPF1 and Y14. Furthermore, we determined the specific regions of MARVELD1 and UPF1 responsible for their interaction. We also showed that MARVELD1 promotes the dissociation of SMG1 from UPF1, resulting in the repression of serine phosphorylation of UPF1, and subsequently blocks the recruitment of SMG5, which is required for ensuing SMG5-mediated exonucleolytic decay. Our observations provide molecular insight into the potential function of MARVELD1 in nonsense-mediated RNA decay.</p> </div

    The C-terminal region of UPF1 is necessary to interact with MARVELD1.

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    <p>(A) Schematic representation of full-length Flag-UPF1(1–1118) and three Flag-UPF1 deletion variants. (B) HEK293/MARVELD1 cells were transiently transfected with different Flag-UPF1 deletion variants or the control plasmid pCMV-Flag and analyzed by coimmunoprecipitation using anti-V5. The results are representative of three independently performed experiments.</p

    MARVELD1 represses the recruitment of SMG5 by inhibiting serine phosphorylation of UPF1.

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    <p>(A) HeLa cells transiently transfected with two independent siRNAs against <i>MARVELD1</i> or the negative control siRNA and HEK293/MARVELD1 or the control cells HEK293/Vector were analyzed by coimmunoprecipitation using anti-UPF1 or rabbit (r) IgG in the presence of RNase A. The analysis of the intensity of SMG1 and importin β1 immunoprecipitated by anti-UPF1 is displayed as histograms on the right. The coIPs of SMG1 and importin β1 were both normalized to the amount of UPF1 immunoprecipitated by anti-UPF1. (B) Lysates of HeLa cells transiently depleted of MARVELD1 and HEK293/MARVELD1 were transiently transfected with Flag-UPF1 and immunoprecipitated by anti-Flag or mouse (m) IgG. Western blotting was performed using anti-phosphoserine or anti-SMG5. The intensities of phosphoserine level and the SMG5 immunoprecipitated by anti-Flag were normalized to the total Flag-UPF1 and are displayed as histograms on the right. (C) The effects of siRNA-mediated knockdown of MARVELD1 and the overexpression of MARVELD1-V5 were assessed by western blotting. GAPDH was used as an internal control. The average ± S.E. (<i>error bars</i>) is displayed.</p

    Amino acids 34-69 of MARVELD1 are required to interact with UPF1.

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    <p>(A) Lysates of HEK293 cells that had been transiently transfected with the specified pcDNA3.1-Flag-MARVELD1 construct or the control plasmid pcDNA3.1-Flag were analyzed by western blotting using the specified antibody before or after IP with anti-Flag. (B) Lysates of HEK293 cells that had been transiently transfected with pcDNA3.1-Flag-MARVELD1(1-173), pcDNA3.1-Flag-MARVELD1(Δ34-69) or the control plasmid pcDNA3.1-Flag (Vector) were immunoprecipitated by anti-Flag. Western blotting was performed using the specified antibody before or after IP. (C) HEK293 cells that were transiently cotransfected with the specified pCMV-Flag-MARVELD1 plasmid, either pmCMV-Gl Norm or pmCMV-Gl Ter and phCMV-MUP. Real-time PCR was used to normalize the level of G1 (β-globin) mRNA relative to Mup mRNA, and the normalized level of G1 (β-globin) Norm mRNA in the presence of each pcDNA3.1-Flag plasmid was defined as 1.0. The average ± S.E. (<i>error bars</i>) is displayed. All of the experiments were performed at least twice.</p

    MARVELD1 interacts with proteins involved in NMD.

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    <p>(A) Whole cell extract of HeLa cells treated with or without RNase A was immunoprecipitated by anti-MARVELD1 or, as a control for nonspecific IP, rabbit (r) IgG. (B) HEK293/MARVELD1 cells or the negative control cells HEK293/Vector were immunoprecipitated by anti-V5 in the presence of RNase A. (C) Extracts of HeLa cells were immunoprecipitated by anti-MARVELD1 or, as a control for nonspecific IP, rabbit (r) IgG in the presence or absence of RNase A. (D) Lysates of HEK293/MARVELD1 cells or the negative control cells HEK293/Vector were immunoprecipitated by anti-V5 in the presence of RNase A. All of the experiments were performed independently at least twice.</p
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