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1.
Clin Toxicol (Phila) ; 51(1): 47-9, 2013 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-23206235

RESUMEN

INTRODUCTION: We report a case of a female neonate who developed respiratory depression following the unintentional administration of methylergonovine. The respiratory depression appeared to improve after the administration of bag mask ventilation, stimulation, and naloxone; and the baby was able to be managed without endotracheal intubation and prolonged positive-pressure ventilation. CASE: A full-term female neonate was delivered vaginally without issue. Approximately 10 min after delivery, the infant was inadvertently administered 0.1 mg of methylergonovine intramuscularly instead of vitamin K. Thirty minutes later the child developed cyanotic extremities and respiratory depression with an oxygen saturation of 75%. Naloxone, 0.4 mg IM, was recommended to mitigate respiratory depression. Within 5 min the patient's respirations improved to 40 breaths per minute, cyanosis improved, and she began resisting ventilations and crying loudly. The child continued to improve and was back to baseline that evening. DISCUSSION: Methylergonovine toxicity in neonates has been commonly associated with respiratory depression necessitating ventilatory support. In consideration of chemical structural similarity between methylergonovine and morphine, as well as signs/symptoms consistent with opioid-induced respiratory depression, naloxone was suggested. CONCLUSION: It appears that naloxone may reverse methylergonovine toxicity in neonates. The identification of a safe and potentially useful antidote to mitigate respiratory depression, potentially avoiding the need for intubation and more invasive interventions in this patient population is important.


Asunto(s)
Errores de Medicación/efectos adversos , Metilergonovina/envenenamiento , Naloxona/uso terapéutico , Antagonistas de Narcóticos/uso terapéutico , Oxitócicos/envenenamiento , Insuficiencia Respiratoria/inducido químicamente , Insuficiencia Respiratoria/tratamiento farmacológico , Terapia Combinada , Cianosis/etiología , Femenino , Humanos , Recién Nacido , Inyecciones Intramusculares , Metilergonovina/administración & dosificación , Metilergonovina/antagonistas & inhibidores , Naloxona/administración & dosificación , Antagonistas de Narcóticos/administración & dosificación , Oxitócicos/administración & dosificación , Oxitócicos/antagonistas & inhibidores , Insuficiencia Respiratoria/fisiopatología , Insuficiencia Respiratoria/terapia , Resultado del Tratamiento
2.
Radiology ; 242(1): 198-207, 2007 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-17185668

RESUMEN

PURPOSE: To determine the feasibility of in vivo localization and quantification of indium 111 (111In)-oxine-labeled bone marrow (BM) with high-resolution whole-body helical single photon emission computed tomography (SPECT) in an established murine model of atherosclerosis and vascular repair. MATERIALS AND METHODS: The institutional animal care and use committee approved this study. BM from young B6 Rosa 26 Lac Z+/+ mice was radiolabeled with 111In-oxine. On days 1, 4, and 7 after administration of radiolabeled cells, five C57/BL6 apolipoprotein E-deficient mice and five wild-type (WT) control mice were imaged with whole-body high-resolution helical SPECT. Quantification with SPECT was compared with ex vivo analysis by means of gamma counting. Autoradiography and beta-galactosidase staining were used to verify donor cell biodistribution. Linear regression was used to assess the correlation between continuous variables. Two-tailed Student t test was used to compare values between groups, and paired two-tailed t test was used to assess changes within subjects at different time points. RESULTS: SPECT image contrast was high, with clear visualization of BM, liver, and spleen 7 days after administration of radiolabeled cells. SPECT revealed that 42% and 58% more activity was localized to the aorta and BM (P<.05 for both), respectively, in apolipoprotein E-deficient mice versus WT mice. Furthermore, 28% and 27% less activity was localized to the liver and spleen (P<.05 for both), respectively, in apolipoprotein E-deficient mice versus WT mice. SPECT and organ gamma counts showed good quantitative correlation (r=0.9). beta-Galactosidase staining and microautoradiography of recipient aortas showed donor cell localization to the intima of visible atherosclerotic plaque but not to unaffected regions of the vessel wall. CONCLUSION: High-resolution in vivo helical pinhole SPECT can be used to monitor and quantify early biodistribution of 111In-oxine-labeled BM in a murine model of progenitor cell therapy for atherosclerosis.


Asunto(s)
Aterosclerosis/diagnóstico por imagen , Aterosclerosis/cirugía , Células de la Médula Ósea/diagnóstico por imagen , Trasplante de Médula Ósea/diagnóstico por imagen , Aumento de la Imagen/métodos , Compuestos Organometálicos , Oxiquinolina/análogos & derivados , Tomografía Computarizada de Emisión de Fotón Único/métodos , Animales , Trasplante de Médula Ósea/métodos , Modelos Animales de Enfermedad , Estudios de Factibilidad , Ratones , Ratones Endogámicos C57BL , Ratones Noqueados , Radiofármacos
3.
J Sports Med Phys Fitness ; 46(1): 132-7, 2006 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-16596112

RESUMEN

AIM: The purpose of this project was to compare the impact of the menstrual cycle on short-term, high intensity (power) performance in active females who either had normal menstrual cycles (NOC) or who were using oral contraceptives (OC). METHODS: Subjects (7 NOC, 17 OC) completed a Margaria-Kalamen staircase test and a Wingate cycle test on 3 occasions: one for familiarization and the other two trials (random order) during menses (MEN) or luteal (LUT) phase. Phase was documented by urinary luteinizing hormone for the NOC. RESULTS: There were no significant differences between MEN and LUT in the NOC group on the Wingate test (n=7) for any of the following: peak power (P=0.33), peak power per kg body weight (P=0.37), anaerobic capacity (P=0.37), anaerobic capacity per kg body weight (P=0.42), power decline (P=0.36), power decline per kg body weight (P=0.35). Also there were no significant differences in power (P=0.95) for the Margaria-Kalamen test (n=6). There were no significant differences between MEN and LUT in the OC group for any of the following variables calculated from the subjects' performance on the Wingate test (n=17): peak power (P=0.39), peak power per kg body weight (P=0.36), anaerobic capacity (P=0.42), anaerobic capacity per kg body weight (P=0.36), power decline (P=0.57), power decline per kg body weight (P=0.66). Also there were no significant differences in power (P=0.44) for the Margaria-Kalamen test (n=11). CONCLUSIONS: For a moderately active group of women, anaerobic power performance was not influenced by menstrual cycle phase in either NOC or OC users.


Asunto(s)
Anticonceptivos Orales/farmacología , Ciclo Menstrual/fisiología , Resistencia Física/fisiología , Adulto , Ejercicio Físico/fisiología , Prueba de Esfuerzo , Femenino , Humanos , Ciclo Menstrual/efectos de los fármacos , Resistencia Física/efectos de los fármacos
4.
FEBS Lett ; 402(1): 62-6, 1997 Jan 27.
Artículo en Inglés | MEDLINE | ID: mdl-9013860

RESUMEN

Analysis of the beta-ketoacyl-ACP synthase (KAS) encoded by the fabF gene of Escherichia coli has been hampered by a reported instability of the cloned gene. Here we describe biochemical characterization of purified, active protein from the recombinant fabF gene. This enzyme has the properties ascribed to KAS II and not those of a putative KAS IV reported to be encoded by fabJ, a genomic clone with DNA sequence identical to that of fabF. We also characterize active protein from a recombinant fabB gene and suggest that this method may have a general utility for analysis of KAS enzymes.


Asunto(s)
3-Oxoacil-(Proteína Transportadora de Acil) Sintasa/genética , 3-Oxoacil-(Proteína Transportadora de Acil) Sintasa/metabolismo , Escherichia coli/enzimología , 3-Oxoacil-(Proteína Transportadora de Acil) Sintasa/química , 3-Oxoacil-(Proteína Transportadora de Acil) Sintasa/aislamiento & purificación , Cerulenina/farmacología , Clonación Molecular , Escherichia coli/genética , Genes Bacterianos , Vectores Genéticos , Proteínas Recombinantes/química , Proteínas Recombinantes/aislamiento & purificación , Proteínas Recombinantes/metabolismo , Especificidad por Sustrato , Temperatura
5.
Plant Physiol ; 109(3): 999-1006, 1995 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-8552723

RESUMEN

Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-sn-glycerol-3-phosphate acyltransferase (LPAAT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39:989-996). Beginning with solubilized membrane preparations, we have used chromatographic separations to identify a polypeptide with an apparent molecular mass of 29 kD, whose presence in various column fractions correlates with the acyltransferase activity detected in those same fractions. Amino acid sequence data obtained from several peptides generated from this protein were used to isolate a full-length clone from a coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA insert with an open reading frame encoding a 308-amino acid protein with a calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid sequence of pCGN5503 to sequences in the data banks revealed significant homology to other putative LPAAT sequences. Expression of the coconut cDNA in Escherichia coli conferred upon those cells a novel LPAAT activity whose substrate activity profile matched that of the coconut enzyme.


Asunto(s)
Aciltransferasas/genética , Cocos/genética , 1-Acilglicerol-3-Fosfato O-Aciltransferasa , Aciltransferasas/aislamiento & purificación , Aciltransferasas/metabolismo , Secuencia de Aminoácidos , Secuencia de Bases , Cocos/enzimología , Sondas de ADN , ADN Complementario/genética , Escherichia coli/genética , Proteínas de Escherichia coli , Biblioteca de Genes , Datos de Secuencia Molecular , Reacción en Cadena de la Polimerasa , Proteínas Recombinantes/metabolismo , Semillas/enzimología , Análisis de Secuencia , Homología de Secuencia de Aminoácido , Especificidad por Sustrato
6.
Plant Physiol ; 100(4): 1751-8, 1992 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-16653193

RESUMEN

Oleoyl-acyl carrier protein (18:1-ACP) thioesterase has been partially purified from developing safflower (Carthamus tinctorius) seeds. Protein species with molecular masses of 34 and 40 kD associated with thioesterase activity were identified and partially sequenced. Analysis of amino-terminal and internal cyanogen bromide peptide sequences revealed no differences in the primary structure of the two species. Amino acid sequence was used to design degenerate oligonucleotides for primers in a polymerase chain reaction (PCR) using safflower embryo cDNA as a template. A 380-base pair PCR product was used to isolate two classes of cDNA clones, designated 2-1 and 5-2, from the embryo cDNA library. Clone 2-1 encodes a 389-amino acid protein including a 60-amino acid transit peptide, and contains all of the protein sequence determined from the 34- and 40-kD proteins. Clone 5-2 encodes a 385-amino acid protein with 80% identity to that encoded by 2-1. Expression of the two safflower cDNA clones in Escherichia coli resulted in a 50- to 100-fold increase in the level of 18:1-ACP thioesterase activity. Both thioesterases are most active on 18:1-ACP; however, the enzyme encoded by 5-2 shows less discrimination against saturated 16- and 18-carbon acyl-ACP substrates.

8.
Pharmacol Biochem Behav ; 3(5): 749-54, 1975.
Artículo en Inglés | MEDLINE | ID: mdl-1208616

RESUMEN

Male Sprague-Dawley rats prepared with chronic electrodes in the mesencephalic reticular formation were trained to perform on a visual attention task. Short trains of electric current delivered to the reticular formation effectively blocked performance in a reversible and reproducible fashion. Subcutaneous administration of 100 mug/kg nicotine (as the base) served to attenuate the behavioral disruption caused by reticular stimulation. The suggestion that it is a nicotine-induced limbic system activation which antagonizes the behavioral disruption caused by electrically-induced reticular over-activation, is discussed.


Asunto(s)
Conducta Animal/efectos de los fármacos , Nicotina/farmacología , Formación Reticular/fisiología , Animales , Atención/efectos de los fármacos , Conducta Animal/fisiología , Estimulación Eléctrica , Masculino , Ratas
13.
Oral Surg Oral Med Oral Pathol ; 31(6): 839, 1971 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-5280469
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