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Biomedical subjects

M J Cabañas

Publications and source records attributed to M J Cabañas.

8 recordsLinked to original sources

Recombinant factor VIIa in continuous infusion during central line insertion in a child with factor VIII high-titre inhibitor.

Recombinant factor VIIa (rFVIIa) is a recently added new tool for the treatment of haemophilia patients with inhibitors. A major drawback in the use of rFVIIa is its short half-life, which necessitates frequent bolus injections. Thus the use of rFVIIa in continuous infusion appears to be a good alternative. We describe the use of rFVIIa, administered by continuous infusion with a minipump during the insertion of a central venous catheter in a child with a high-titre factor VIII inhibitor. rFVIIa was administered as an intravenous bolus (90 micrograms kg-1 [4.5 kIU kg-1]), 1 h prior to central line insertion, after which the continuous infusion was immediately started for 5 days. The infusion rate was based on the clearance obtained from a previous pharmacokinetic study. Effective haemostasis and normal healing of surgical incisions were achieved after central line insertion. No local thrombophlebitis nor evidence of generalized activation of the coagulation cascade was observed. Single-dose pharmacokinetic parameter values were clearance (Cl) 34.6 mL h-1 kg-1, volume of distribution (Vd) 40.6 mL kg-1 and mean residence time (MRT) 1.17 h. The recovery was 2.27% U-1 kg-1. rFVIIa showed a monophasic decay. Cl during continuous infusion was 23.4 +/- 6.9 mL h-1 kg-1. The administration of rFVIIa by continuous infusion is effective, safe and more convenient when compared to other clotting factors. Moreover, continuous infusion provides significant economic savings (77% decrease in rFVIIa requirements).

Autoantibodies↗

Errors evolution and analysis in antineoplastic drug preparation during one year.

We analyzed the errors occurring in the preparation circuit of cytotoxic mixtures of the Centralized Cytotoxic Preparation Unit during one year. Analysis of their evolution meant the investigation of twenty parameters susceptible to error. Each parameter was considered one error opportunity. Error has been defined either by the lack of data or mistake in the controlled parameter. In 4,734 preparations (94,680 parameters) there were 314 errors. The percentage of error per parameter in the first month of study was 0.74; at sixth was 0.34 and the last month was 0.26. Only in four months the day of maximum number of preparations coincided with the day of maximum number of errors. We conclude that the percentage of errors in the preparation process is low with a tendency to decrease and that the number of daily preparations is not the single factor that influences the production of errors.

Antineoplastic Agents↗

Anesthetic efficacy of eutectic prilocaine-lidocaine cream in pediatric oncology patients undergoing lumbar puncture.

OBJECTIVE: To evaluate the efficacy of eutectic mixture of local anesthetics 5% (Emla) in reducing pain associated with lumbar punctures in children. DESIGN: Prospective, double-blind, randomized, placebo-controlled trial. SETTING: University pediatric hospital. PATIENTS: Eleven pediatric oncology patients (mean age 6.6 y, range 4-16) who underwent 31 lumbar punctures. MAIN OUTCOME MEASURES: The analgesic effect was measured by using two methods. The first was a 10-point visual analog scale reported by the patient and the second was an 8-point behavioral pain scale assessed by the nurse who applied the cream. RESULTS: Emla cream was associated with significantly lower pain scores than those with placebo as measured by the patient when the puncture was successful on the first attempt (2.0 +/- 1.6 Emla group, 3.8 +/- 1.9 placebo group; p < 0.05). CONCLUSIONS: The use of Emla cream may reduce pain substantially only in patients who undergo a successful lumbar puncture on the first attempt.

Adolescent↗

Nonenzymic translocation and spontaneous release of noncognate peptidyl transfer ribonucleic acid from Escherichia coli ribosomes.

Poly(uridylic acid)-programmed ribosomes have been used to synthesize the noncognate peptidyl-tRNA Ac-Phe-Tyr-tRNATyr and its cognate counterpart Ac(Phe)2-tRNAPhe. After synthesis, Ac(Phe)2-tRNAPhe remains, as expected, in the ribosomal acceptor (A) site, but the noncognate AcPhe-Tyr-tRNATyr does not; part of it spontaneously falls off the ribosome and the rest translocates, without elongation factor (EF) G, to the ribosomal donor site. The inhibitor of translocation viomycin prevents both the spontaneous release and the nonenzymatic translocation by confining the noncognate peptidyl-tRNA to the A site. Under these conditions, the interaction of AcPhe-Tyr-tRNATyr with the A site appears to be similar to that of Ac(Phe)2-tRNAPhe without the antibiotic, and EF-G promotes the translocation and subsequent elongation of both peptidyl-tRNAs to comparable extents. The results indicate that, without viomycin, the noncognate peptidyl-tRNA is weakly held in the ribosomal A site and support the proposal that the release of peptidyl-tRNA occurring during protein synthesis in vivo is related to a ribosomal editing mechanism which discards mistranslated nascent proteins [Menninger, J. R. (1977) Mech. Ageing Dev. 6, 131].

Escherichia coli↗

The binding of non-cognate Tyr-tRNATyr to poly(uridylic acid)-programmed Escherichia coli ribosomes.

The poly(U)-dependent binding of Tyr-tRNATyr to Escherichia coli ribosomes has been studied using a highly purified system. Binding is maximal at 10 mM magnesium acetate (up to 0.7 molecule Tyr-tRNATyr/ribosome), and requires the presence of elongation factor (EF) T (a mixture of EF-Ts and EF-Tu), GTP, NH4+ ions and an aminoglycoside antibiotic (streptomycin, neomycin B, kanamycin B or gentamicin C1a). Under limiting and up to saturating concentrations of EF-T, one molecule of GTP is hydrolyzed per molecule of Tyr-tRNATyr bound, suggesting that 'proof-reading' mechanisms involving the hydrolysis of GTP are inoperative in the presence of the antibiotics. Binding of Tyr-tRNATyr apparently takes place at the ribosomal acceptor site, since peptide bonds are readily formed with N-acetyl-Phe-tRNA prebound to the ribosomal donor site. In contrast to Phe-tRNAPhe binding, Tyr-tRNATyr binding is impaired by the omission of the 50-S subunit, the replacement of GTP by its non-hydrolyzable analogs guanyl-5'-yl methylene diphosphonate and guanyl-5'-yl iminodiphosphonate, and also by the presence of the antibiotic streptogramin A. This suggests that the correct interaction of Tyr-tRNATyr with the peptidyl transferase centre is essential for the stability of this ligand on the ribosome. Moreover, the aminoglycoside antibiotics are also necessary, even after the binding reaction is complete, to maintain Tyr-tRNATyr on the ribosome.

Aminoglycosides↗