No abstract

The end product of purine metabolism varies from species to species. The degradation of purines to urate is common to all animal species, but the degradation of urate is much less complete in higher animals. The comparison of subcellular distribution, intraperoxisomal localization forms, molecular structures, and some other properties of urate-degrading enzymes (urate oxidase, allantoinase, and allantoicase) among animals is described. Liver urate oxidase (uricase) is located in the peroxisomes in all animals with urate oxidase. On the basis of the comparison of intraperoxisomal localization forms, mol wt, and solubility of liver urate oxidase among animals, it is suggested that amphibian urate oxidase is a transition form in the evolution of aquatic animals to land animals. Allantoinase and allantoicase are different proteins in fish liver, but the two enzymes form a complex in amphibian liver. The subcellular localization of allantoinase and allantoicase varies among fishes. Hepatic allantoinase is located both in the peroxisomes and in the cytosol in saltwater fishes, and only in the cytosol in freshwater fishes. Hepatic allantoicase is located on the outer surface of the peroxisomal membrane in the mackerel group and in the peroxisomal matrix in the sardine group. Amphibian hepatic allantoinase-allantoicase complex is probably located in the mitochondria. On the basis of previous data, changes of allantoinase and allantoicase in molecular structure and intracellular localization during animal evolution may be as follows: Fish liver allantoinase is a single peptide with a mol wt of 54,000, and is located both in the peroxisomes and in the cytosol, or only in the cytosol. Fish liver allantoicase consists of two identical subunits with a mol wt of 48,000, and is located in the peroxisomal matrix or on the outer surface of the peroxisomal membrane. The evolution of fishes to amphibia resulted in the dissociation of allantoicase into subunits, and in the association of allantoinase with the subunit of allantoicase. This amphibian enzyme was lost by further evolution.

Abstract:In Once considered as a phytopathogen, Burkholderia cepacia, a multi-drug-resistant bacteria, is now recognized as an important pathogen in the lung of patients with cystic fibrosis (CF) and can lead to severe pneumonia and death (15). B. cepacia strain KF1 isolated from a non-CF patient with pneumonia, produces extracellular metalloprotease in large quantities (37), and causes lung infections in mice on intratracheal inoculation (42). We have been analyzing the mechanism of protease production to explore its involvement in the pathogenesis.In a previous study, we showed that the protease-negative, lipase-positive mutant KFT1007, a Tn5-Tp insertion mutant of B. cepacia KF1, was impaired in the dsbB gene which encodes a membranebound disulfide bond oxidoreductase, DsbB, resulting in secretion of a premature and catalytically inactive form of protease (1). In Escherichia coli, DsbB couples with DsbA, a periplasmic disulfide bond oxidoreductase that directly makes S-S bonds on target molecules (26). Thus, the reduced-DsbA is reoxidized by oxidized-DsbB that is recycled with the aid of a respiratory electron transfer chain (14). The DsbA-DsbB circuit in E. coli is involved in flagellar basal body assembly (9), type IV pilin biogenesis (44), and the maturation of heat-stable enterotoxin (22) and alkaline phosphatase (10). In some Gram-negative bacteria, homologs of E. coli DsbA and their target proteins are found in Vibrio cholerae TcpG for enterotoxin (23)

PurposeThe purpose of this study was to evaluate the correlation between histological invasiveness and the computed tomography (CT) value and size in pure ground-glass nodules (GGNs) to determine optimal “follow-up or resection” strategies.MethodsBetween 2001 and 2014, 78 resected, pure GGNs were retrospectively evaluated. The maximum diameter and CT value of pure GGNs were measured using a computer graphics support system.ResultsAll GGNs with a maximum diameter ≤10 mm and CT value ≤−600 Hounsfield units (HU) were considered to be noninvasive lesions, while 21 of 26 (81 %) with a maximum diameter >10 mm and CT value >−600 HU were considered to be invasive lesions. With respect to the correlation between each histological type and pure GGN with a maximum diameter ≤10 mm and CT value ≤−600 HU, the specificity was 90 % and the sensitivity and negative predictive value were both 100 % in atypical adenomatous hyperplasia (AAH), while the specificity was 58 % and the sensitivity and positive predictive value were 0 % in minimally invasive and invasive adenocarcinoma.ConclusionPure GGNs with a maximum diameter of ≤10 mm and CT value of ≤−600 HU are nearly always pre-invasive lesions; therefore, surgery should be carefully selected in such patients.

Eight Beagle dogs were inoculated intrabronchially with 5 x 10(9) live, avirulent cells of Bordetella bronchiseptica L-414 strain (phase I cells) (B. bronchiseptica) to investigate the serum levels of their C-reactive protein, the white blood cell counts, the antibody responses to B. bronchiseptica in the sera and tracheal secretions, and the effects of prednisolone given to four of the dogs on C-reactive protein (CRP), white blood cells (WBC) and immune responses. In two Beagle dogs inoculated intrabronchially with sterile physiological saline, the concentrations of CRP and the WBC counts did not increase. CRP was markedly increased one day after inoculation in the dogs inoculated with B. bronchiseptica to 385.0-720.0 micrograms/ml (mean 498 +/- 132 micrograms/ml) in the group given the B. bronchiseptica inoculation only, and to 372.0-649.0 micrograms/ml (mean 551 +/- 106 micrograms/ml) in the group treated with prednisolone following inoculation of B. bronchiseptica, as determined by an enzyme-linked immunosorbent assay (ELISA). The CRP levels were 23-95 times the pre-inoculation values, which indicated that prednisolone had no effect on the production of CRP. In the prednisolone-treated group, the WBC count increased and stayed at an increased level for approximately 12 days. An indirect fluorescent antibody test led to the detection of anti-B. bronchiseptica IgM and IgG antibodies in the sera from 5 days after B. bronchiseptica inoculation and S-IgA and IgG anti-B. bronchiseptica antibodies in the tracheal secretions on the day after the challenge exposure to B. bronchiseptica. The increase in CRP after challenge exposure to B. bronchiseptica was significantly (p < 0.05) smaller than that found after the first inoculation of B. bronchiseptica.