RESUMEN
From January 1, 1997 through June 30, 2000, 224 patients underwent valve replacement with the ATS Medical cardiac valve prosthesis under a USFDA-approved investigational device exemption study. Aortic valve replacement (AVR) was conducted in 152 patients (39 with coronary bypass) and mitral replacement (MVR) in 72 patients (18 with coronary bypass). Overall operative mortality was 1.8% (AVR = 2.8%, MVR = 0%), with only one valve-related death. In 372 patient-years of follow-up, there were an additional four patient deaths, two of which were valve related following a stroke. Valve-related complications included: thromboembolism (linearized rate = 3.8% per patient year), of which 3/11 had chronic deficits (0.8% per patient year); thrombosis (1 MVR = 0.8% per patient year); paravalvular leak (1 AVR = 0.4% per patient year); anticoagulant-related hemorrhage (1 AVR and 5 MVR = 1.6% per patient year) with no patient mortality; prosthetic valve endocarditis (1 MVR = 0.8% per patient year); and valve dysfunction (0%). Echocardiographic gradients were proportional to valve size and did not significantly change over the follow-up period. This study documented the ATS Medical prosthesis to be a valuable addition to the surgeon's armamentarium in the treatment of cardiac valvular disease.
Asunto(s)
Prótesis Valvulares Cardíacas , Adulto , Anciano , Anciano de 80 o más Años , Válvula Aórtica/diagnóstico por imagen , Válvula Aórtica/cirugía , Puente de Arteria Coronaria/mortalidad , Ecocardiografía , Endocarditis/etiología , Seguridad de Equipos , Femenino , Estudios de Seguimiento , Enfermedades de las Válvulas Cardíacas/mortalidad , Enfermedades de las Válvulas Cardíacas/cirugía , Humanos , Masculino , Persona de Mediana Edad , Válvula Mitral/diagnóstico por imagen , Válvula Mitral/cirugía , Complicaciones Posoperatorias/etiología , Tromboembolia/etiología , Resultado del Tratamiento , Estados Unidos/epidemiología , United States Food and Drug AdministrationRESUMEN
Degradation of ethinyl estradiol (EE2) by nitrifying activated sludge was studied with micro-organisms grown in a reactor with feedback of sludge fed with only a mineral salts medium containing ammonium as the sole energy source. Ammonium was oxidised by this sludge at a rate of 50 mg NH4+ g(-1) DW h(-1). This activated sludge was also capable of degrading EE2 at a maximum rate of 1 microg g(-1) DW h(-1). Using sludge with an insignificant nitrifying capacity of 1 mg NH4+ g(-1) DW h(-1), no degradation of EE2 was detected. Oxidation of EE2 by nitrifying sludge resulted in the formation of hydrophilic compounds, which were not further identified. Most probably degradation by nitrifying sludge results in a loss of estrogenic activity, as hydroxylated derivatives of EE2 are known to have a substantially lower pharmacological activity than EE2.
Asunto(s)
Congéneres del Estradiol/metabolismo , Etinilestradiol/metabolismo , Aguas del Alcantarillado , Nitrógeno/metabolismo , Oxidación-Reducción , Eliminación de Residuos Líquidos/métodosRESUMEN
Chronic granulomatous disease (CGD) is characterized by the failure of phagocytic leukocytes to kill certain bacteria and fungi. This is caused by deficiencies in one of the components of NADPH oxidase, the enzyme in phagocytic leukocytes that generates superoxide. In a rare, autosomal recessive form of CGD, a 67-kD cytosolic component of NADPH oxidase (p67-phox) is missing. Until now, mutations in the gene coding for this protein have not been identified. We now report on a 10-year-old girl with lymph node and liver abscesses who was recognized as an A67(0) CGD patient by lack of NADPH oxidase activity in her granulocytes, a cytosolic defect in a cell-free oxidase system, and lack of immunoreactive material with an antiserum against the p67-phox protein. mRNA for this protein was present in normal amounts in her monocytes. This p67-phox mRNA was reverse-transcribed, and the coding region was amplified by polymerase chain reaction in six overlapping fragments and was sequenced. The patient appeared to be homozygous for a G-233-->A mutation, resulting in a nonconservative amino acid change (78Gly-->Glu). This mutation was also found in the genomic DNA of this patient but not in that of 38 normal donors. Both parents and a sister proved to be carriers of the disease, as deduced from the mutation in only one allele. The carrier state was also manifested by intermediate superoxide production by their intact granulocytes and in the cell-free system.
Asunto(s)
Enfermedad Granulomatosa Crónica/enzimología , Enfermedad Granulomatosa Crónica/genética , Heterocigoto , NADH NADPH Oxidorreductasas/deficiencia , Secuencia de Aminoácidos , Secuencia de Bases , Niño , Femenino , Humanos , Datos de Secuencia Molecular , Mutación , NADH NADPH Oxidorreductasas/genética , NADPH OxidasasRESUMEN
Several studies indicated the presence of an hCG-immunoreactive substance in commercial hMG preparations. Because hCG represents LH activity with a relatively very long half-life, differences between hMG preparations with respect to hCG content could imply clinical differences. To investigate whether there is any difference in this respect between the two most widely used hMG preparations, we measured the hCG content of ampules of Humegon and Pergonal retrieved from the market, together representing 51 separate production batches, with one or more different specific immunological assays. There are no significant differences between Humegon and Pergonal with respect to the mean hCG level per ampule as measured by RIA, ELISA, and Delfia. The batch-to-batch consistency for Humegon is higher.
Asunto(s)
Gonadotropina Coriónica/análisis , Menotropinas/químicaRESUMEN
The NADPH oxidase of human eosinophils, measured in the cell-free system, shows the same characteristics as the enzyme from human neutrophils. All proteins required for activity of the enzyme are expressed in eosinophils at a higher level than in neutrophils. Eosinophils isolated from patients with chronic granulomatous disease show the same molecular defects as the neutrophils from these patients.
Asunto(s)
Eosinófilos/enzimología , NADH NADPH Oxidorreductasas/metabolismo , Fosfatasa Alcalina/metabolismo , Western Blotting , Membrana Celular/enzimología , Sistema Libre de Células , Activación Enzimática/efectos de los fármacos , Enfermedad Granulomatosa Crónica/enzimología , Humanos , NADPH Oxidasas , Neutrófilos/enzimología , Dodecil Sulfato de Sodio/farmacologíaRESUMEN
Phagocytic leukocytes contain an activatable NADPH:O2 oxidoreductase. Components of this enzyme system include cytochrome b558, and three soluble oxidase components (SOC I, SOC II, and SOC III) found in the cytosol of resting cells. Previously, we found that SOC II copurifies with, and is probably identical to, a 47-kDa substrate of protein kinase C. In the present study we investigated the change in location of several of these oxidase components after activation of intact neutrophils with phorbol myristate acetate (PMA) and separation of subcellular fraction on sucrose density gradients. On Western blots with fractions of resting cells, the alpha subunit of cytochrome b558 was detected with a monoclonal antibody as a doublet of Mr 22,000 and 24,000 in the specific granules and as a single band of Mr 24,000 in the plasma membrane. PMA induced an increase of cytochrome b558 in the plasma membrane, including the Mr 22,000 band. PMA also induced translocation of the 47-kDa protein from the cytosol to the membrane fraction, as revealed by in vitro phosphorylation experiments. When NADPH oxidase activity was determined in a cell-free system in the presence of sodium dodecyl sulfate and GTP with plasma membranes from resting cells, cytosol from PMA-treated cells was deficient compared with cytosol from resting cells. This deficiency could be partially restored by the addition of SOC I. Concomitantly, SOC I activity appeared in the plasma membranes of PMA-treated cells. These studies support the hypothesis that PMA stimulation of neutrophils results in assembly of oxidase components from the cytosol and the specific granules in the plasma membrane with subsequent expression of NADPH oxidase activity.