Effect of nitrous oxide and methionine on hepatic S-adenosylmethionine levels and in vivo histidine oxidation in rats.

Nitrous oxide (N2O) decreased in vivo oxidation of histidine in rats fed a basal diet marginally deficient in methionine, although hepatic levels of S-adenosylmethionine (AdoMet) were not significantly altered. Excess dietary methionine increased hepatic levels of AdoMet and increased histidine oxidation. However, it did not protect histidine oxidation when the rats were treated with N2O. Parenteral administration of methionine greatly increased hepatic levels of AdoMet and increased histidine oxidation in normal and N2O treated rats. This indicates that when hepatic levels of AdoMet are greatly elevated by administration of methionine, N2O does not affect in vivo histidine oxidation.     

Increase in hepatic ubiquinone on administration of diethylhexyl phthalate to the rat

It is shown for the first time that the content of ubiquinone of liver increases (2.5 fold) on dietary administration of the widely-used industrial Plasticizer diethylhexyl Phthalate to the rat. The increase is localized almost entirely in mitochondria in which the concentration of the quinone Per mg Protein is 1.7 times the control. IncorPoration of the radioactive Precursor (acetate) reveals that the biosynthesis of ubiquinone is increased in the livers of Plasticizer-administered animals. The rate of degradation is not altered.     

Infectivity and Sedimentation of Rhinovirus Ribonucleic Acid

Ribonucleic acid extracted from the virions of two human rhinoviruses is infective and is similar in size to poliovirus ribonucleic acid.     

Effects of prenatal X-irradiation: studies on the mechanism of X-irradiation-induced inhibition of microsomal enzyme development in rat liver

Exposure of pregnant rats to 25 R of x-irradiation on the fourteenth gestation day has produced in the male offspring an impairment of the development of the hepatic microsomal enzyme system which metabolizes hexobarbital. However, irradiation did not suppress the increase of enzyme activity brought about by the administration of chemical inducers (pheno-barbital). Actinomycin, on the other hand, inhibited to varying degrees both the ontogenic and phenobarbital-induced increases in enzyme activity. The effects on the enzyme system have been supported by in vivo measurements of the duration of hexobarbital hypnosis. The ontogenic increase in enzyme activity is hormone-dependent, while that following phenobarbital administration is independent of hormonal regulation as evidenced by the response in hypophysectomized or sexually immature animals. It is concluded from these results that the inhibitory effect of x-irradiation on the hepatic enzyme system is mediated through an action on the hormonal regulation of enzyme activity. Evidence for this hypothesis is discussed.     

Inhibition of Immune Complex-Induced Inflammation by A small Molecular Weight Selectin Antagonist

The anti-inflammatory effect of a small molecular weight antagonist of P- and E-selectin-dependent cell adhesion was examined. The glycolipid sulphatide was shown to block the adherence of thrombin-activated rat platelets to HL-60 cells. This interaction is known to be dependent on P-selectin. The rat dermal reverse passive Arthus reaction was used to assess the effect of sulphatide on a neutrophil dependent inflammatory response. Sulphatide dosedependently blocked both the vascular permeability increase and cell infiltration after intraperitoneal administration. These results show that a small molecular weight compound which blocks P- and E-selectin dependent adhesion in vitro can effectively block the inflammation due to immune complex deposition. A compound with this type of profile may have therapeutic potential in the treatment of immune complex mediated diseases.     

Evidence for the presence of a receptor for the cytolethal distending toxin (CLDT) of Campylobacter jejuni on CHO and HeLa cell membranes and development of a receptor-based enzyme-linked immunosorbent assay for detection of CLDT

Abstract Using ligand blotting, it was found that partially purified cytolethal distending toxin prepared from and enterotoxigenic strain of Campylobacter jejuni , bound to two peptides of molecular masses of approximately 59 kDa and 45 kDa and to a single peptide of 59 kDa in protein blots prepared from HeLa and CHO cell membranes, respectively. In contrast, labile toxin of Escherichia coli and cholera toxin bound to a single peptide of the same molecular mass (15 kDa) on protein blots prepared from both CHO and HeLa cell crude membranes resolved by gel electrophoresis. This banding pattern was identical using SDS-solubilized membrane, with or without heat treatment, but no band was obtained when reduced (treatment with 2-mercaptoethanol) samples were used for the gel electrophoresis. The differences between receptors of cytolethal distending toxin and cholera toxin/labile toxin were exploited to develop a receptor-based enzyme-linked immunosorbent assay for detection of cytolethal distending toxin which involved the consecutive addition of either solubilized CHO or HeLa membranes, antigen and antibody. This enzyme-linked immunosorbent assay consistently detected crude cytolethal distending toxin diluted up to 16-fold. The receptor-based enzyme-linked immunosorbent assay for detection of cytolethal distending toxin developed in this study is a suitable alternative assay which can be performed easily in laboratories with minimal facilities and, more importantly, the results are available within a few hours as compared to times of up to 5 days in the conventional tissue culture detection of cytolethal distending toxin.