Incidence of herpes infection of the uterine cervix observed in cytologic specimens in the Tokyo metropolitan area

In a high-volume cytology laboratory in the metropolitan Tokyo area, the incidence of cytologically diagnosed herpes infection in cervical scraping smears of the female genital tract was studied according to the year-by-year changes, age distribution, seasonal variation and types of cytologic alteration. The overall incidence over the 12 years studied was 0.007% (87 cases among 1,230,773 examined). The incidence varied from 0.003% to 0.005% in the early 1970s (except for 1973) and increased to 0.011% in the last three years (1980 to 1982). A large increase was noted in younger age groups in comparison with middle and older age groups. There was a tendency for the infection rate to be higher in the spring (0.011%) and lower in the fall (0.005%). Multinucleation and a ground-glass appearance were observed in the infected cells in almost every case while eosinophilic inclusion bodies were found in 20.7% of the cases.     

Purification and characterization of rat brain prostaglandin D synthetase

Prostaglandin D synthetase was purified 2,600-fold from rat brain to apparent homogeneity, as judged by polyacrylamide gel electrophoresis and ultracentrifugation. The purified enzyme was a monomeric protein with a molecular weight of 27,000 +/- 1,000. The pI value, sedimentation coefficient, and partial specific volume were 4.6, 4.1 s, and 0.73 ml/g, respectively. The enzyme was stable between pH 4 and 11 at the temperature lower than 25 degrees C and resistant to a heat treatment under alkaline conditions (pH 8-11). About 50% of the activity was detected after a heat treatment at 100 degrees C for 5 min at pH 10. However, the enzyme was readily inactivated by the isomerase reaction of prostaglandin H2 to prostaglandin D2. The enzyme required sulfhydryl compounds such as dithiothreitol, glutathione, beta-mercaptoethanol, cysteine, and cysteamine for the reaction, but stoichiometric oxidation of these sulfhydryl compounds was not observed. The optimum pH, Km value for prostaglandin H2, and the turnover number were 9.5, 14 microM, and 170 min-1, respectively. The antibody was raised against the purified enzyme in a rabbit, which showed only one positive band in immunoblotting after gel electrophoresis of crude extracts of the brain at the same position as that of the purified enzyme. More than 90% of the prostaglandin D synthetase activity in the brain was absorbed by an excess amount of the antibody, indicating that our preparation is a major component of the enzyme responsible for the biosynthesis of prostaglandin D2 in the brain.     

Mammalian signal peptidase: partial purification and general characterization of the signal peptidase from microsomal membranes of porcine pancreas

Signal peptidase has been enriched extensively from microsomal membranes of porcine pancreas. Microsomal membranes were washed with 1 M KCl and Brij 35, and then solubilized with 1% Nonidet P-40. The solubilized signal peptidase was purified by DEAE-cellulose chromatography and Sepharose CL-6B filtration. Cleavage of pre-human placental lactogen with the partially purified enzyme gave the mature form, whose NH2-terminus was identified as valine. The signal peptidase is heat-labile and approximately 90% of the enzymatic activity was lost at 60 degrees C within 1 min. The pH optimum of the activity was 7 to 8. Chymostatin and o-phenanthroline at concentrations of 2.5 mM inhibited the signal peptidase activity by 62% and 30%, respectively.     

Gastric K+-stimulated p-nitrophenylphosphatase cytochemistry

Summary A cytochemical study of gastric K⁺-stimulated p-nitrophenylphosphatase (K-NPPase) activity, corresponding to a K⁺-stimulated phosphoprotein phosphatase of H-K-ATPase system, has been made by a new cytochemical method.Sections of fixed guinea pig gastric mucosa in a mixture of 2% paraformaldehyde and 0.25% glutaraldehyde, were incubated with the incubation medium (1.0 M glycine-0.1 M KOH buffer, pH 9.0, 2.5 ml; 1.1 M KCl, 0.5 ml; 10 mM lead citrate dissolved in 50 mM KOH, 4 ml; levamisole, 6.0 mg; dimethyl sulfoxide, 2.0 ml; 0.1 M p-nitrophenylphosphate (Mg-salt), 1.0 ml; ouabain, 73.0 mg) for 30 min at room temperature. Under a light microscope the specific gastric K-NPPase reaction was distributed only in the parietal cells of the fundic glands. The electron microscopic cytochemistry showed that the gastric K-NPPase activity was localized on the membrane lining the apical surfaces, secretory canaliculi and tubulovesicles. On the other hand, ouabain-sensitive K-NPPase activity (Na-K-ATPase) was demonstrated to localize only in the basolateral membrane of parietal cells with Mayahara's method.These findings support the interrelationships between the apical surface membrane, secretory canalicular membrane and tubulovesicles, and the functional differentiation of the membrane between the secretory membrane and basolateral membrane.In honour of Prof. P. van DuijnPart of this paper was presented at the 24th Annual Meeting of the Japan Society of Histochemistry and Cytochemistry held in Nagoya, October 27–28, 1983 (Ogawa KS, Fujimoto K, Ogawa K (1983) A new lead citrate method for the cytochemical demonstration of the H⁺–K⁺-ATPase with p-NPP as a substrate. Acta Histochem Cytochem 16:662)This study was supported by Grants-in-Aid for Encouragement of Young Scientists No. 60770019 to K. Fujimoto from the Ministry of Education, Science and Culture, the Japanese Government     

Influence of phospholipase treatments on ligand bindings to a benzodiazepine receptor-GABA receptor-chloride ionophore complex

Treatment of rat cerebellar membranes with phospholipase A2 (PLA2) or phospholipase C (PLC) increased basal [3H]diazepam binding at 0 degrees C with concomitant disappearance of the stimulatory effect of Cl- ion on the binding. On the other hand, these treatments did not affect the stimulatory effect of GABA, nor the maximum enhancement obtained in the presence of both GABA and Cl- ion. These results suggest that PLA2 or PLC modified the phospholipids responsible for the interaction between the benzodiazepine receptor and the Cl- ionophore. This assumption was supported by the results of thermodynamic experiments which showed that the changes in thermodynamic parameters occurring after the addition of Cl- ion resembled those after PLA2 or PLC treatment. Since the effect of PLA2 was evident at very low concentrations, and a PLC concentration of at least one order of magnitude higher was required to induce a similar effect, the change of phospholipids especially to lysophospholipids seems to be of particular importance. Protein release from the membrane, which also occurs after PLA2 or PLC treatment, did not appear to be responsible for the present phenomenon.     

The interaction between lipid peroxidation and prostaglandin synthesis in rabbit kidney-medulla slices.

Lipid peroxidation induced by ascorbic acid and Fe2+ was inhibited by mepacrine (phospholipase A2 inhibitor) and aspirin (prostaglandin cyclo-oxygenase inhibitor) in rabbit kidney-medulla slices. Moreover, ascorbic acid and Fe2+ potentiated the inhibitory effect on prostaglandin E2 formation by mepacrine, but they had no influence on prostaglandin E2 production decreased by aspirin. Lipid peroxidation induced by ascorbic acid and Fe2+ appears to be affecting the activity of prostaglandin endoperoxide synthase. These results suggest that lipid peroxidation is connected closely with the prostaglandin-generating system, and it has the potential to modulate the turnover of arachidonic acid and prostaglandin synthesis.