Durability and disinfection of single-use endotracheal tubes following exposure to commonly available medical disinfecting compounds.

BACKGROUND: Reusing single-use medical supplies offers a capability enhancement during massive casualty incidents when resupply of medical supplies is unavailable in times of national health care crises. This pilot study determined the feasibility of disinfection of endotracheal tubes with commonly used chemical disinfecting agents. METHODS: Endotracheal tubes (ETTs) were subjected to either CaviCide, Neutral Disinfectant Cleaner, Cidex, or saline according to the manufacturer's recommended disinfection contact times. Alterations to the polyvinyl chloride (PVC) integrity by disinfecting agents were determined by volume/pressure measurements within the ETT cuff. To test the disinfection rate, ETTs were inoculated with Staphylococcus Aureus and subjected to experimental disinfection protocol. FINDINGS: There were no significant alterations to ETT tracheal cuff function and mixed results in disinfection among ETTs. ETTs bacterial culture data presented possible contamination among the groups. DISCUSSION: These data support the feasibility of single-use ETT reuse as a last resort while making every attempt and effort to follow established protocols to minimize harm to the patient.

Addressing the impact of trauma before diagnosing mental illness in child welfare.

Congress set requirements for child welfare agencies to respond to emotional trauma associated with child maltreatment and removal. In meeting these requirements, agencies should develop policies that address child trauma. To assist in policy development, this study analyzes more than 14,000 clinical assessments from child welfare in Illinois. Based on the analysis, the study recommends child welfare agencies adopt policies requiring that (1) mental health screenings and assessments of all youth in child welfare include measures of traumatic events and trauma-related symptoms; (2) evidence-based, trauma-focused treatment begin when a youth in child welfare demonstrates a trauma-related symptom; and (3) a clinician not diagnose a youth in child welfare with a mental illness without first addressing the impact of trauma. The study also raises the issue of treatment reimbursement based on diagnosis.

mTOR Ser-2481 autophosphorylation monitors mTORC-specific catalytic activity and clarifies rapamycin mechanism of action.

The mammalian target of rapamycin (mTOR) Ser/Thr kinase signals in at least two multiprotein complexes distinguished by their different partners and sensitivities to rapamycin. Acute rapamycin inhibits signaling by mTOR complex 1 (mTORC1) but not mTOR complex 2 (mTORC2), which both promote cell growth, proliferation, and survival. Although mTORC2 regulation remains poorly defined, diverse cellular mitogens activate mTORC1 signaling in a manner that requires sufficient levels of amino acids and cellular energy. Before the identification of distinct mTOR complexes, mTOR was reported to autophosphorylate on Ser-2481 in vivo in a rapamycin- and amino acid-insensitive manner. These results suggested that modulation of mTOR intrinsic catalytic activity does not universally underlie mTOR regulation. Here we re-examine the regulation of mTOR Ser-2481 autophosphorylation (Ser(P)-2481) in vivo by studying mTORC-specific Ser(P)-2481 in mTORC1 and mTORC2, with a primary focus on mTORC1. In contrast to previous work, we find that acute rapamycin and amino acid withdrawal markedly attenuate mTORC1-associated mTOR Ser(P)-2481 in cycling cells. Although insulin stimulates both mTORC1- and mTORC2-associated mTOR Ser(P)-2481 in a phosphatidylinositol 3-kinase-dependent manner, rapamycin acutely inhibits insulin-stimulated mTOR Ser(P)-2481 in mTORC1 but not mTORC2. By interrogating diverse mTORC1 regulatory input, we find that without exception mTORC1-activating signals promote, whereas mTORC1-inhibitory signals decrease mTORC1-associated mTOR Ser(P)-2481. These data suggest that mTORC1- and likely mTORC2-associated mTOR Ser-2481 autophosphorylation directly monitors intrinsic mTORC-specific catalytic activity and reveal that rapamycin inhibits mTORC1 signaling in vivo by reducing mTORC1 catalytic activity.