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1.
J Pediatr Pharmacol Ther ; 12(2): 102-14, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-23055847

RESUMO

OBJECTIVES: The electronic health record (EHR) can improve patient safety, care efficiency, cost effectiveness and regulatory compliance. Cincinnati Children's Hospital Medical Center (CCHMC) has successfully implemented an Integrating Clinical Information System (ICIS) that includes Computerized Provider Order Entry (CPOE). This review describes some of the unanticipated challenges and solutions identified during the implementation of ICIS. METHODS: Data for this paper was derived from user-generated feedback within the ICIS. Feedback reports were reviewed and placed into categories based on root cause of the issue. Recurring issues or problems which led to potential or actual patient injury are included. RESULTS: NINE DISTINCT CHALLENGES WERE IDENTIFIED: 1) Deterioration in communication; 2) Excessive system alerts to users; 3) Unrecognized discontinuation of medications; 4) Unintended loss of orders; 5) Loss of orders during implementation; 6) Amplification of errors; 7) Unintentional generation of patient care orders by system analysts; 8) Persistence of specific patient care order instructions; 9) Verbal orders entered under the incorrect clinician. CONCLUSIONS: Unanticipated challenges are expected when implementing EHRs. The implementation plan for any EHR should include methods to identify, evaluate and repair problems quickly. While continued challenges with this complex system are expected, we believe that the EHR will continue to facilitate improved patient care and safety. The lessons learned at CCHMC will permit other institutions to avoid some of these challenges and design robust processes to detect and respond to problems in a timely fashion to ensure implementation success.

2.
Methods Mol Biol ; 279: 133-50, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-15199242

RESUMO

Nitric oxide (NO) serves critical signaling, energetic, and toxic functions throughout the biosphere. NO steady-state levels and functions are controlled in part by NO metabolism or degradation. Dioxygen-dependent NO dioxygenases (EC 1.14.12.17) and dioxygen-independent NO reductases (EC 1.7.99.7) are being identified as major routes for NO metabolism in various life forms. Here we describe the use of the Clark-type NO electrode, mechanistic inhibitors, and nitrate/nitrite assays to measure, characterize, and identify major NO metabolic pathways and enzymes in bacteria, fungi, plants, mammalian cells, and organelles. The methods may prove to be particularly useful for mechanistic investigations and the development of inhibitors, inducers, and other novel NO-modulating therapeutics.


Assuntos
Eletrodos Seletivos de Íons , Nitratos/metabolismo , Óxido Nítrico/metabolismo , Nitritos/metabolismo , Oxigênio/metabolismo , Animais , Bovinos , Inibidores Enzimáticos/farmacologia , Oxirredutases/antagonistas & inibidores , Oxirredutases/metabolismo , Superóxido Dismutase/antagonistas & inibidores , Superóxido Dismutase/metabolismo
3.
Free Radic Biol Med ; 37(2): 216-28, 2004 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-15203193

RESUMO

Human intestinal Caco-2 cells metabolize and detoxify NO via a dioxygen- and NADPH-dependent, cyanide- and CO-sensitive pathway that yields nitrate. Enzymes catalyzing NO dioxygenation fractionate with membranes and are enriched in microsomes. Microsomal NO metabolism shows apparent KM values for NO, O2, and NADPH of 0.3, 9, and 2 microM, respectively, values similar to those determined for intact or digitonin-permeabilized cells. Similar to cellular NO metabolism, microsomal NO metabolism is superoxide-independent and sensitive to heme-enzyme inhibitors including CO, cyanide, imidazoles, quercetin, and allicin-enriched garlic extract. Selective inhibitors of several cytochrome P450s and heme oxygenase fail to inhibit the activity, indicating limited roles for a subset of microsomal heme enzymes in NO metabolism. Diphenyleneiodonium and cytochrome c(III) inhibit NO metabolism, suggesting a role for the NADPH-cytochrome P450 oxidoreductase (CYPOR). Involvement of CYPOR is demonstrated by the specific inhibition of the NO metabolic activity by inhibitory anti-CYPOR IgG. In toto, the results suggest roles for a microsomal CYPOR-coupled and heme-dependent NO dioxygenase in NO metabolism, detoxification, and signal attenuation in mammalian cells.


Assuntos
Inibidores Enzimáticos/farmacologia , Microssomos Hepáticos/enzimologia , NADPH-Ferri-Hemoproteína Redutase/metabolismo , Óxido Nítrico/metabolismo , Oxigenases/metabolismo , Células CACO-2 , Linhagem Celular Tumoral , Relação Dose-Resposta a Droga , Radicais Livres , Heme Oxigenase (Desciclizante)/metabolismo , Hemoglobinas/metabolismo , Humanos , Imunoglobulina G/química , Cinética , Microssomos/metabolismo , Modelos Químicos , NADPH-Ferri-Hemoproteína Redutase/antagonistas & inibidores , Óxido Nítrico/química , Oxigênio/metabolismo , Oxigenases/antagonistas & inibidores , Transdução de Sinais , Frações Subcelulares/metabolismo , Superóxidos/metabolismo , Fatores de Tempo , Zinco/química
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