Use of antipyretics for preventing febrile seizure recurrence in children: a systematic review and meta-analysis.

The efficacy of antipyretics for preventing febrile seizure recurrence has been reported by a recent study, and the results might overturn previous evidence. We systematically reviewed the efficacy of antipyretics in the prevention of febrile seizure recurrence in children focused on the timing of its administration. We searched the Medline, Embase, and Cochrane Central Register of Controlled Trials databases for randomized and quasi-randomized trials and prospective non-randomized studies of aged up to 60 months, diagnosed with febrile seizure, who were treated with antipyretics. Data were extracted from eight studies. Only one study reported that antipyretics prevented the recurrence of febrile seizures within the same fever episode (9.1% in the acetaminophen group vs. 23.5% in the control group, p < 0.01). Four studies found no evidence for the efficacy of antipyretics in preventing febrile seizure recurrence in distant fever episodes (odds ratio, 0.92; 95% confidence interval, 0.57-1.48, for two randomized controlled studies).Conclusion: This review provides very limited support for the use of antipyretics in preventing febrile seizure recurrence within the same fever episode and no evidence for its use in distant fever episodes. New studies are required to evaluate this topic further and determine whether the effectiveness of antipyretics is based on intervention timing. What is Known: • Reviews of prophylactic drug management among febrile seizure children found that antipyretics had no significant benefits. • Recent data suggest that antipyretics are effective in preventing febrile seizures. What is New: • Weak evidence suggests a possible role in preventing febrile seizure recurrence within the same fever episode. • There is clearly no role for antipyretic prophylaxis in preventing febrile seizures during distant fever episodes.

Inosine-5'-monophosphate is a candidate agent to resolve rigor mortis of skeletal muscle.

The object of the present study was to reveal the action of inosine-5'-monophosphate (IMP) toward myofibrils in postmortem muscles. IMP solubilized isolated actomyosin within a narrow range of KCl concentration, 0.19-0.20 mol/L, because of the dissociation of actomyosin into actin and myosin, but it did not solubilize the proteins in myofibrils with 0.2 mol/L KCl. However, IMP could solubilize both proteins in myofibrils with 0.2 mol/L KCl in the presence of 1 m mol/L pyrophosphate or 1.0-3.3 m mol/L adenosine-5'-diphosphate (ADP). Thus, we presumed that pyrophosphate and ADP released thin filaments composed of actin, and thick filaments composed of myosin from restraints of myofibrils, and then both filaments were solubilized through the IMP-induced dissociation of actomyosin. Thus, we concluded that IMP is a candidate agent to resolve rigor mortis because of its ability to break the association between thick and thin filaments.

[Reliability and validity of the Japanese version of the DAST-20].

OBJECTIVE: Assessing the degree of problems related to drug abuse is important in each treatment setting. The Drug Abuse Screening Test-20 (DAST-20) is a brief, simple 20-item instrument to measure the degree of problems related to drug use. The objective of the present study is to examine the reliability and validity of the Japanese version of the DAST-20. METHODS: We translated the DAST-20 into Japanese using back translation. The anonymous self-administered questionnaire was completed by 310 drug users at the Drug Addiction Rehabilitation Centers (DARC group, n = 113) and at HIV/AIDS regional hospitals (HIV group, n = 197) in Japan. RESULTS: The average DAST-20 score was 7.6 (DARC group = 14.7, HIV group = 2.8). Each item score was highly correlated with the total score (r = 0.45-0.88). A high internal consistency (Cronbach's α = 0.95) was observed (men = 0.95, women = 0.84). Overall test-retest reliability was 0.86 (men = 0.85, women = 0.90). The total DAST-20 score was strongly positively correlated with the Severity of Dependence Scale-J score (r = 0.85), but moderately positively correlated with the Alcohol Use Disorders Identification Test score (r = 0.41). In addition, confirmatory factor analysis indicated an acceptable fit to the data (goodness-of-fit index [GFI] = 0.893, adjusted goodness-of-fit index [AGFI] = 0.854, comparative fit index [CFI] = 0.948, root mean square residual [RMR] = 0.008, root mean square error of approximation [RMSEA] = 0.073). CONCLUSION: Our results clearly suggest that the Japanese version of the DAST-20 has sufficient internal consistency and acceptable levels of concurrent validity and construct validity.

C-terminal processing of tyrosinase is responsible for activation of Pholiota microspora proenzyme.

Tyrosinase is expressed as a 67-kDa protein in Pholiota microspora (synonym Pholiota nameko), whereas the same enzyme purified from fruiting bodies of P. microspora is a 42-kDa protein that is cleaved with a C-terminal 25-kDa polypeptide from the 67-kDa protein. To confirm the role of C-terminal processing in enzyme activity, we expressed a recombinant 67-kDa tyrosinase in Escherichia coli cells. To obtain a soluble protein, the recombinant tyrosinase was expressed as a thioredoxin fusion protein with an enterokinase-cleavable site. Enterokinase digestion of the fusion protein produced a recombinant 67-kDa tyrosinase that did not have any catalytic activity. However, chymotrypsin digestion of the fusion protein produced a recombinant 44-kDa tyrosinase that was catalytically active and had a 25-kDa cleaved C-terminal. Kinetic parameters of the 44-kDa tyrosinase were similar to those of the 42-kDa tyrosinase purified from the fruiting bodies. These results suggest that tyrosinase is expressed in P. microspora as a latent 67-kDa proenzyme and is converted to the mature active 42-kDa enzyme by proteolytic processing of the C-terminal.

Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko.

Tyrosinase (monophenol, 3,4-dihydroxy L-phenylalanine (L-DOPA):oxygen oxidoreductase, EC 1.14.18.1) was isolated from fruit bodies of Pholiota nameko and purified to homogeneity. The purified enzyme was a monomer with a molecular weight of 42,000 and contained 1.9 copper atoms per molecule. The N-terminal of the purified enzyme could not be detected by Edman degradation, probably due to blocking, while the C-terminal sequence of the enzyme was determined to be -Ala-Ser-Val-Phe-OH. The amino acid sequence deduced by cDNA cloning was made up of 625 amino acid residues and contained two putative copper-binding sites highly conserved in tyrosinases from various organisms. The C-terminal sequence of the purified enzyme did not correspond to that of the deduced sequence, but agreed with Ala384-Ser385-Val386-Phe387 in sequence. When the encoded protein was truncated at Phe387, the molecular weight of the residual protein was calculated to be approximately 42,000. These results suggest that P. nameko tyrosinase is expressed as a proenzyme followed by specific cleavage to produce a mature enzyme.