Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162871 (abdominal aortic aneurysm)
 8,664 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Blood purification, mainly plasma exchange (PE), was carried out for 13 cases of acute, and two cases of chronic postoperative liver failure. Four of thirteen acute cases (31%) survived. Although only one of eight with chronic liver disease survived, three of five without chronic liver disease survived. In most of those who lived, other organ failure occurred less often; total bilirubin and blood ammonia were less than 15 mg/dl and 200 micrograms/dl, respectively, before PE: and total bilirubin, blood ammonia, and branched chain amino acid/aromatic amino acid (BCAA/AAA) ratios recovered after five or fewer sessions of PE. Two chronic cases, treated for 1 and 4 years, respectively, were good candidates for liver or multiple organ transplantation. Although both died, PE was effective in reducing jaundice and in improving consciousness and general condition. Plasma exchange should be introduced early after assessing the changes in total bilirubin, blood ammonia, and coma grade in patients with acute postoperative liver failure. Plasma exchange could be useful as a chronic hepatic support system for those awaiting liver transplantation.
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PMID:Blood purification for postoperative liver failure with special reference to chronic hepatic support for those awaiting liver transplantation. 175 Nov 73

Serum amino acid determinations were made in 40 patients with chronic cor pulmonale in the period of 1985-1987 in our hospital. There were slight type 14 cases. severe type 26 cases (including pulmonary encephalopathy 10 cases). In severe type the ratio of branched chain amino acid to aromatic amino acid (BACC/AAA) was significantly lower than normal (P less than 0.01) and there was significant negative correlation between PaCO2 and BCAA/AAA (r = -0.49 P less than 0.05). The plasma amino acid pattern in severe type cor pulmonale is similar to that found in hepatic encephalopathy. The mechanism of coma in cor pulmonale is at least in some degree, similar with that of hepatic encephalopathy.
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PMID:[Plasma amino acid changes in 40 cases of chronic cor pulmonale]. 263 32

In this study, we tested a new artificial liver device using liver pieces in 8-h hemoperfusion of comatous porcine blood and compared two alternative tissue preparations. Acute hepatic coma in the pigs was induced by complete devascularization of the liver. The animals were killed in stage IV coma (15-25 h after the operation), and 1 l blood was perfused over 200 g fresh or DMSO-preserved liver cubes. After the devascularization GOT, GPT, GLDH, AP, LDH, SDH, bilirubin, free fatty acid, and bile acid levels in serum increased progressively. Ammonia concentrations underwent a rapid increase in the first 9 h of coma development from 126.0 +/- 9.9 to 321.9 +/- 62.2 mumol/l. Most of the amino acids in serum were elevated and molar ratio of BCAA/AAA declined from 3.87 +/- 0.79 to 0.92 +/- 0.24. In the course of hemoperfusion ammonia was removed from the perfusate to 71% of the initial values using fresh and to 39% using preserved tissue. Correspondingly, there was an increase in urea concentrations. Amino acid metabolism was ameliorated during the perfusion; Fischer's quotient increased from 0.91 +/- 0.15 to 1.38 +/- 0.14 (fresh liver) and from 0.89 +/- 0.14 to 2.11 +/- 0.44 (preserved liver); neuroexcitatory amino acids Asp and Glu were markedly elevated. Energy charge of the liver cells increased and reached levels exceeding 0.5 in both experimental groups, a balanced energy metabolism was maintained and suggests active metabolization by the liver pieces. In comparison with fresh tissue, preserved liver cubes proved effective. We consider our artificial liver device capable of temporary hepatic support in acute necrosis of the liver and suppose that its efficiency can be potentiated by combining this system with other procedures.
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PMID:Successful treatment of hepatic coma by a new artificial liver device in the pig. 408 14

We investigated the possibilities of liberation of toxic coma potentiating substances from the damaged hepatic tissues during the hemoperfusion over small liver pieces. Concentrations of nearly all amino acids rose during the perfusion due to the damage of hepatic tissues, but the molar ratio of BCAA to AAA was not changed. Free fatty acid levels in the perfusates increased slightly, however, methylmercaptan level remained constant. These results suggest that liberated substances from the damaged liver would not potentiate hepatic encephalopathy. Therefore, hemoperfusion over small liver pieces should be an useful method for hepatic assist because of excellent detoxification effects.
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PMID:Amino acid metabolism during hemoperfusion over biological materials. 633 66

Using the galactosamine induced hepatic coma rat model, we studied the effects of coated charcoal hemoperfusion on amino acids in plasma and CSF in grade III hepatic coma. We found that 1 hour of hemoperfusion significantly reduced AAAs and BCAAs in plasma and increased the molar ratio of BCAA:AAA. When rats in grade III coma were treated with 2 consecutive 1-hour hemoperfusions, the substantial reduction of plasma AAAs resulted in a significant decrease of AAA levels in CSF.
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PMID:Effect of charcoal hemoperfusion on amino acid disturbance in experimental hepatic coma. 649 Jan 92

N-Ethylmaleimide-sensitive fusion protein (NSF) and its yeast orthologue, Sec18, are cytoplasmic AAA(+) ATPases required for most intracellular membrane fusion events. The primary function of NSF is thought to be the disassembly of cis-SNARE complexes, thus allowing trans-SNARE complex formation and subsequent membrane fusion. The importance of NSF/Sec18 in intracellular membrane traffic in vivo is highlighted by the inhibition of neurotransmission in Drosophila comatose (NSF) mutants and of constitutive secretion in yeast sec18 mutants. However, the underlying biochemical defects in these mutant proteins are largely unknown. Here, we identify the sec18-1 mutation as a G89D substitution in the N domain of Sec18p. This mutation results in an inhibition of the mutant protein's ability to bind to Sec17p (yeast alpha-SNAP). In contrast, engineering the comatose(st53)() mutation (S483L) into mammalian NSF (S491L) has no effect on alpha-SNAP binding. Instead, the stimulation of ATPase activity by alpha-SNAP required for wild-type NSF to disassemble SNARE complexes does not occur in the mutant NSF(st53) protein. This biochemical phenotype predicts a dominant negative effect, which was confirmed by engineering the st53 mutation into Sec18 (A505L), resulting in a dominant lethal phenotype in vivo. These findings suggest a biochemical basis for the block in membrane fusion observed in the mutant organisms. Furthermore, the mutants characterized here define key residues involved in two essential, but mechanistically distinct, biochemical functions of NSF: SNAP binding and SNAP-dependent ATPase stimulation.
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PMID:Analysis of NSF mutants reveals residues involved in SNAP binding and ATPase stimulation. 1195 72