Enoxaparin dosing errors in the emergency department / 世界急诊医学杂志（英文）

BACKGROUND:The study aimed to determine the frequency of enoxaparin dosing errors for patients who had a measured emergency department (ED) weight compared to those who did not have a measured ED weight, and to determine if demographic variables (e.g., weight, height, age, English-speaking, race) impact the likelihood of receiving an inappropriate dose. METHODS:This is a retrospective, electronic chart review of patients who received a dose of enoxaparin in the ED between January 1, 2008 and July 1, 2013. We identified all patients >18 years who received a dose of enoxaparin while in the ED, were admitted, and had at least one inpatient weight within the first four days of hospitalization. Patients were excluded if they received enoxaparin for prophylaxis or a dose of more than 1.25 mg/kg. RESULTS:A total of 1,944 patients were included. Patients were more likely to experience an error if they did not have a measured ED weight. Over-doses of >10 mg were more likely to occur in patients without a measured ED weight. Patients with no documented ED weight or with a staff-estimated ED weight were more likely to experience a dosing error than those with a patient-stated weight. Patients were more likely to experience an error if their first inpatient weight was more than 96 kg, they were more than 175-cm tall, or were English speaking. CONCLUSION:Dosing errors are more likely to occur when patients are not weighed in the ED. Modifications to current workflows to incorporate weighing those patients who receive weight-dosed medications may be warranted.

Isolation and properties of a multicatalytic proteinase complex from Xenopus laevis skin secretion

A multicatalytic proteinase complex present in the skin secretion of Xenopus laevis was purified and its enzymatic activity towards natural and synthetic peptides was investigated. We identified three activities: i) a C-terminal deamidation enzyme activity which exhibited selectivity for the Asp-Phe-NH2 and Phe-Leu-NH2 motifs of cerulein, minigastrin Leu-enkephalinamide, (des-Tyr1)Leu-enkephalinamide and diaminobenzylthiocyanate-DVDERDVRGFASFL NH2 (DABTCDR8kermit); ii) an endopeptidase activity that cleaves peptide bonds on the carboxyl side of hydrophobic amino acid residues such as Tyr-Gly of LHRH, Ile-Ala of PGLa and Leu-Ala of buccalin; iii) an enzyme activity that cleaves peptide bonds at the dibasic sites of peptides of the dynorphin family. The molecular weight determined by Sephacryl S-400 molecular sieve filtration indicated an Mr about 600 kDa. The activities characterized here exhibit and optimal pH of about 7.4. The activities of the multicatalytic complex were differentially inhibited by the classical inhibitors of proteases

Human neuroblastoma cells express a novel metallo-endopeptidase activity able to inactivate atrial natriuretic factor: inhibition during retinoic acid-induced differentiation

A new metallo-endopeptidase which hydrolyzes atrium natriuretic factor (ANF) has been isolated from human neuroblastoma NB-OK-1 cells. In the present study we show that this metallo-endopeptidase is also present in several other human neuroblastoma cell lines, which include CHP 100, SH-SY5Y, SK-N-BE(2), BE(2)-C and BE(2)M-17. Additionally, we show that this endopeptidase activity is reduced to about 20 per cent of the control during retinoic acid (RA)-induced neuronal differentiation in the RA-sensitive SK-N-BE(2) cells, but not in the RA-resistant BE(2)-M17 cells. This suggests that the inhibition is related to neuronal differentiation and not to a direct effect of 5 microM RA on the enzyme activity. This new enzyme is clearly distinct from neutral endopeptidase (NEP, EC 3.4.24.11) and angiotensin-converting enzyme (ACE,EC 3.4.15.1), since specific inhibitors for these endopeptidases (10 microM phosphoramidon and 1 mM captopril, respectively) had no effect on their activity. However, this enzyme was inhibited 100 per cent by 10 mM o-phenanthroline showing an inhibitory spectrum similar to that of another novel metallo-endopeptidase recently isolated in our laboratory from Xenopus laevis skin secretion. Although the physiological function of this new enzyme in human neuroblastoma cells is not known at the present time, we suggest that it may participate in inactivation of neuropeptides such as atrium natriuretic factor (ANF), substance P, somatostatin-14 and bradykinin in vivo