Leveraging Telemedicine to Reduce the Financial Burden of Asthma Care.

One of the most compelling arguments for telemedicine is its potential to increase health care access by making care more affordable for patients and families, including those affected by asthma. This goal is critically important in the United States, where the high cost of asthma care is associated with nonadherence to preventive care regimens and suboptimal health outcomes. In this clinical commentary review, we draw from the literature and our own research to identify opportunities for and challenges to leveraging telemedicine to reduce the financial burden of asthma care. Our interviews with 42 families affected by asthma during the COVID-19 pandemic suggest that under favorable circumstances, telemedicine can meaningfully reduce costs, including those related to transportation and missed work, while offering high-quality care. However, families also identified ways in which telemedicine can increase costs. For example, some reported reduced access to support services and material resources such as medication samples, which they relied on to manage costs. In this way, our findings underscore the need for careful care coordination and communication in telemedicine. We conclude by discussing the 4Rs, a structured communication approach designed to support cost conversations, increase care coordination, and help families reduce asthma care cost burden.

Compartment-specific phosphorylation of rat thyroid hormone receptor alpha1 regulates nuclear localization and retention.

The thyroid hormone receptor alpha1 (TRalpha1) is a transcription factor, which can activate or repress gene expression in response to thyroid hormone. In addition, some of its actions, including DNA binding and transcriptional activation, are thought to be regulated by phosphorylation. Results presented here, using Xenopus oocyte microinjection assays, demonstrate that a phosphorylated form of rat TRalpha1 is present in the nucleus, whereas unphosphorylated TRalpha1 remains cytoplasmic. Changes in the phosphorylation state of TRalpha1 occur rapidly and point to the possibility that phosphorylation occurs in the nucleus. Furthermore, increasing the overall phosphorylation state of the cell leads to enhanced nuclear retention of TRalpha1, suggesting that compartment-specific phosphorylation regulates nuclear localization of TRalpha1. Enhanced nuclear retention of TRalpha1 is not dependent on phosphorylation of serine 12, a well-characterized casein kinase II site, nor is phosphorylation of this site necessary for import of TRalpha1 into the Xenopus oocyte nucleus. Similarly, mutational analysis in mammalian cells shows that nuclear localization and partitioning of TRalpha1 to the nuclear matrix are independent of serine 12 phosphorylation. Taken together, these studies suggest that phosphorylation of one or more sites in TRalpha1, excluding serine 12, enhances nuclear retention and/or inhibits nuclear export but is not directly involved in nuclear import.