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Biomedical subjects

J S Zhao

Publications and source records attributed to J S Zhao.

12 recordsLinked to original sources

Three-dimensional quantitative structure activity relationship (3D-QSAR) analysis for in vitro toxicity of chlorophenols to HepG2 cells.

In the present paper, comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA) were applied to investigate two 3D-QSAR models for the cytotoxicity of chlorophenols. These models have evaluated the intensity of chlorophenols' toxicity on HepG2 cells in vitro. The CoMFA model has both high consistency and predictability. The contribution of the electrostatic field to biological activity is greater than that of the steric field. The CoMSIA model used in this study includes two fields, one is hydrophobic field, and the other is electrostatic field. The relative contribution of them is 0.789:0.211. Consisted with the CoMFA model, the CoMSIA electrostatic filed also plays a dominant role. The CoMFA and CoMSIA contour maps significantly elucidated that the electrostatic field is more important than the other fields and might be one of the reasons resulting in potential reactive mechanism involved in cell proliferation inhibition.

Cell Line, Tumor↗

Process for degradation of nitrobenzene: combining electron beam irradiation with biotransformation.

Electron beam irradiations of aqueous solutions containing 15-30 mg/L of nitrobenzene at 60 kGy dose removed 78% of the contaminant. Three mononitrophenols were detected as by-products of electron beam treatment of nitrobenzene. A mixed culture enriched on a mixture of 2-, 3-, and 4-nitrophenol degraded both the residual nitrobenzene and the nitrophenol products. Percentage removal of nitrobenzene increased with increasing electron beam dose. This observation led to the conceptual design of a two-stage electron beam microbial process for degradation of nitrobenzene. Three groups of pure isolates were characterized from the mixed culture based on their abilities to grow on cor- responding nitrophenol substrates: Group A, 2NP(-)3NP(-)4NP(+); Group B, 2NP(+)3NP(+)4NP(-); and Group C, 2NP(-)3NP(+)4NP(-). Bacteria that grew on 3-NP transformed nitrobenzene into ammonia in the electron beam-treated nitrobenzene samples.

Biotransformation↗

Substrate selectivity of a 3-nitrophenol-induced metabolic system in Pseudomonas putida 2NP8 transforming nitroaromatic compounds into ammonia under aerobic conditions.

The 3-nitrophenol-induced enzyme system in cells of Pseudomonas putida 2NP8 manifested a wide substrate range in transforming nitroaromatic compounds through to ammonia production. All of the 30 mono- or dinitroaromatic substrates except 4-nitrophenol, 2,4-dinitrophenol, 2,4,6-trinitrophenol, 3-nitroaniline, 2-nitrobenzoic acid, and 2-nitrofuran were quickly transformed. Ammonia production from most nitroaromatic substrates appeared to be stoichiometric.

Aerobiosis↗

Biotransformation of hydroxylaminobenzene and aminophenol by Pseudomonas putida 2NP8 cells grown in the presence of 3-nitrophenol.

Biotransformation products of hydroxylaminobenzene and aminophenol produced by 3-nitrophenol-grown cells of Pseudomonas putida 2NP8, a strain grown on 2- and 3-nitrophenol, were characterized. Ammonia, 2-aminophenol, 4-aminophenol, 4-benzoquinone, N-acetyl-4-aminophenol, N-acetyl-2-aminophenol, 2-aminophenoxazine-3-one, 4-hydroquinone, and catechol were produced from hydroxylaminobenzene. Ammonia, N-acetyl-2-aminophenol, and 2-aminophenoxazine-3-one were produced from 2-aminophenol. All of these metabolites were also found in the nitrobenzene transformation medium, and this demonstrated that they were metabolites of nitrobenzene transformation via hydroxylaminobenzene. Production of 2-aminophenoxazine-3-one indicated that oxidation of 2-aminophenol via imine occurred. Rapid release of ammonia from 2-aminophenol transformation indicated that hydrolysis of the imine intermediate was the dominant reaction. The low level of 2-aminophenoxazine-3-one indicated that formation of this compound was probably due to a spontaneous reaction accompanying oxidation of 2-aminophenol via imine. 4-Hydroquinone and catechol were reduction products of 2- and 4-benzoquinones. Based on these transformation products, we propose a new ammonia release pathway via oxidation of aminophenol to benzoquinone monoimine and subsequent hydrolysis for transformation of nitroaromatic compounds by 3-nitrophenol-grown cells of P. putida 2NP8. We propose a parallel mechanism for 3-nitrophenol degradation in P. putida 2NP8, in which all of the possible intermediates are postulated.

Aminophenols↗

Cometabolic biotransformation of nitrobenzene by 3-nitrophenol degrading Pseudomonas putida 2NP8.

A strain of Pseudomonas putida (2NP8) capable of growing on both 2-nitrophenol and 3-nitrophenol, but not on nitrobenzene (NB), was isolated from municipal activated sludge. 2-Nitrophenol was degraded by this strain with production of nitrite. Degradation of 3-nitrophenol resulted in the formation of ammonia. Cells grown on 2-nitrophenol did not degrade nitrobenzene. A specific nitrobenzene degradation activity was induced by 3-nitrophenol. Ammonia, nitrosobenzene, and hydroxylaminobenzene have been detected as metabolites of nitrobenzene degradation by cells grown in the presence of 3-nitrophenol. These results indicated a NB cometabolism mediated by 3-nitrophenol nitroreductase.

Biodegradation, Environmental↗

Microbial degradation of nitrobenzene and mono-nitrophenol by bacteria enriched from municipal activated sludge.

Using a mixture of three mono nitrophenols as sole carbon, nitrogen and energy sources, mixed cultures were enriched from municipal activated sludge to degrade both nitrophenols and nitrobenzene. Bacterial growth and degradation rate could be increased by supplementing the medium with 0.1% YE. Microorganisms were isolated from the nitrophenols enrichment, and they were identified as strains of Comamonas testosteroni and Acidovorax delafieldii. These strains showed broad degradation ability toward nitrophenols and nitrobenzene.

Biodegradation, Environmental↗

Impaired lung branching morphogenesis in the absence of functional EGF receptor.

The mammalian lung develops through branching morphogenesis which is controlled by growth factors, hormones, and extracellular matrix proteins. We have evaluated the role of EGF-receptor signaling in lung morphogenesis by analyzing the developmental phenotype of lungs in mice with an inactivated the EGF-receptor gene both in vivo and in organ culture. Neonatal EGF-receptor-deficient mice often show evidence of lung immaturity which can result in visible respiratory distress. The lungs of these mutant mice had impaired branching and deficient alveolization and septation, resulting in a 50% reduction in alveolar volume and, thus, a markedly reduced surface for gas exchange. The EGF-receptor inactivation also resulted in type II pneumocyte immaturity, which was apparent from their increased glycogen content and a reduced number of lamellar bodies. The defective branching was already evident at Day 12 of embryonic development. When explants of embryonic lungs from Day 12 embryos were cultured under defined conditions, the branching defect in EGF-receptor-deficient lungs was even more pronounced, with only half as many terminal buds as normal lungs. EGF treatment stimulated the expression of surfactant protein C and thyroid transcription factor-1 in cultured normal lungs, but not in EGF-receptor-deficient lungs, suggesting that EGF-receptor signaling regulates the expression of these marker genes during type II pneumocyte maturation. Taken together, our data indicate that signal transduction through the EGF receptor plays a major role in lung development and that its inactivation leads to a respiratory distress-like syndrome.

Animals↗

A molecular model of braid-like DNA structure.

The three-dimensional molecular models of DNA triple helices and triple-stranded brain-like structure were built up by molecular architecture, and their structural features and energy decomposition were examined. The results showed: (i) The base triplet is the element forming braid-like and triple helix DNA; (ii) Under specified conditions, DNA could form the triplet-stranded braid-like structure; (iii) DNA stability of the braid-like structure is less than that of the triple helix structure.

Bacteriophage lambda↗

[Comparative pathologic study on the peri-ulcer mucosal lesion around benign and malignant gastric ulcer].

3441 peri-ulcerous mucosal lesions around benign and malignant gastric ulcers (1479 benign gastric ulcers, 421 cancerous degeneration of benign ulcers and 1541 ulcerative carcinomas) were studied comparatively. It was found that the ulcer of cancerous degeneration of benign ulcer was small and the epithelial regeneration at the ulcer's edge and fusion of the muscularis mucosa with the muscularis propria were very common. The cancerous tissue, extending down to the submucosa, was found at the margin but not at the base of the ulcer. Lymph node metastasis was rare. Therefore, the cancerous degeneration of ulcer was most likely an early carcinoma. These findings conform well with Hauser's criteria. Chronic atrophic gastritis intestinal metaplasia (IIb and type II), moderate and severe dysplasia were more commonly observed in cancerous degeneration of ulcers than in benign peptic ulcers or ulcerative carcinoma. These results suggest that multiple biopsies should be taken from the edge of chronic ulcers.

Adenocarcinoma↗

Formation in vitro of the pTP-dCMP initiation complex of human adenovirus type 12.

We report the covalent addition of [32P]dCMP to a protein from group A adenovirus 12 (Ad12)-infected human (KB) cells in vitro, using crude extracts. Synthesis of the 60K protein-dCMP complex required a DNA template containing a terminally located adenovirus replication origin; the protein-dCMP bond was alkali-labile but acid-stable. We therefore conclude that this product is the Ad12 terminal protein precursor (pTP)-dCMP initiation complex for DNA replication. Synthesis of Ad12 pTP-dCMP was specific for dCTP but was stimulated by dATP. In contrast to Ad2, the Ad12 initiation reaction required ATP. Antipeptide antiserum targeted to Ad DNA polymerase inhibited Ad12 pTP-dCMP synthesis in vitro, providing evidence that Ad DNA polymerase catalyse dCMP addition to pTP during initiation.

Adenoviruses, Human↗