Caesarean section for twin pregnancy in a parturient with Brugada syndrome.

Brugada syndrome is a common cause of sudden cardiac death. We report the anaesthetic management of a woman with Brugada syndrome for elective caesarean section of twins. There are few reports of this disease in pregnancy and we believe this is the first of elective caesarean section in a parturient with the syndrome. The characteristic electrocardiographic changes of the syndrome are linked to sodium channel blockers including local anaesthetics such as bupivacaine. The use of bupivacaine for intrathecal central neuraxial blockade as well as other drugs commonly used in obstetric anaesthesia is discussed.

Underwater-seal nasogastric tube drainage to relieve gastric distension caused by air swallowing.

Air swallowing can occur as a psychogenic phenomenon, because of abnormal anatomy, or during non-invasive positive pressure ventilation. Gross distension of the stomach with air can have severe consequences for the respiratory and gastrointestinal systems. We report the case of a 62-year-old man with severe dynamic hyperinflation due to chronic obstructive pulmonary disease, who developed respiratory failure requiring intubation a few hours after radical prostatectomy. Following a percutaneous tracheostomy and weaning of sedation on day six, his abdomen began to enlarge progressively. X-rays revealed massive gastric distension due to air swallowing, which continued despite all efforts to optimise therapy. The use of an underwater seal drainage system on a nasogastric tube improved ventilation and ultimately aided weaning from mechanical support.

Home care business opportunities in Europe.

The demand for home care services will continue to grow exponentially around the world. This demand is being driven by demographics, technology, and personal choice. Providers of home care have a great deal to teach and learn from each other. The opportunities for collaboration and joint ventures are great now and will continue to increase with the passing of time. This article has been extracted from a 1996 panel discussion at the International Home Care Forum held in Nashville, Tennessee.

Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis.

Site-directed mutagenesis of the acute-phase human serum amyloid A (SAA1 alpha) protein was used to evaluate the importance of the N-terminal amino acid residues, namely RSFFSFLGEAF The full-length cDNA clone of SAA1 alpha (pA1.mod.) was used to create two mutations, namely Gly-8 to Asp-8 and an 11 amino acid truncation between Arg-1 and Phe-11 respectively. Wild-type and mutant cDNAs were expressed in Chinese hamster ovary (CHO) cells under the control of the human cytomegalovirus promoter, which resulted in the secretion of the processed proteins into the culture media. Wild-type recombinant human SAA (rSAA) protein was shown to have pI values of 6.0 and 6.4, similar to the human SAA isoform SAA1 alpha and SAA1 alpha desArg found in acute-phase plasma. N-terminal sequencing of 56 residues confirmed its identity with human SAA1 alpha. The total yield of wild-type rSAA measured by ELISA was between 3.5 and 30 mg/l. The two mutations resulted in reduced expression levels of the mutant SAA proteins (3-10 mg/l). Further measurements of rSAA concentration in lipid fractions of culture medium collected at a density of 1.21 g/ml (high-density liporotein; HDL) and 1.063-1.18 g/ml (very-low-density lipoprotein/low-density lipoprotein; VLDL/LDL) showed that 76% of the wild-type protein was found in the HDL fraction and the remaining 24% in the infranatant non-lipid fraction. In contrast the relative concentration of mutant rSAA in HDL and infranatant fractions was reversed. This is consistent with the previously proposed involvement of the 11 amino acid peptide in anchoring. SAA protein on to HDL3 [Turnell, Sarra, Glover, Baum, Caspi, Baltz and Pepys (1986) Mol. Biol. Med. 3, 387-407]. Wild-type rSAA protein was shown to from amyloid fibrils in vitro under acidic conditions as shown by electron microscopy, and stained positive with Congo Red and exhibited apple-green birefringence when viewed under polarized light. Under the same conditions mutSAA(G8D) and mutSAA delta 1-11 did not form amyloid fibrils. In conclusion, replacement of Gly-8 by Asp-8 or deletion of the first 11 amino acid residues at the N-terminus of rSAA diminishes its capacity to bind to HDL and decreases amyloid fibril formation.