Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
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Escherichia coli K-12 cell suspensions in buffer were exposed to ozone at a concentration of 600 ppm. Measurements were made of cell viability, glyceraldehyde-3-phosphate dehydrogenase, malate dehydrogenase, lactate dehydrogenase, glutathione disulfide reductase, nonprotein sulfhydryl and total sulfhydryl compounds. Cell viability was not affected when E. coli K-12 was exposed to ozone for less than 10 minutes. The most sensitive parameter was glyceraldehyde-3-phosphate dehydrogenase followed by nonprotein sulfhydryl and total sulfhydryl compounds. Effects on malate dehydrogenase, lactate dehydrogenase and glutathione disulfide reductase were negligible. Cell survival and induction of lipid oxidation were also determined using two strains of E. coli K-12 (rec A, deficient in DNA repair and wild-type). The extent of membrane lipid oxidation correlated with cell viability in a dose-dependent manner and the survival curves of both strains showed similar sensitivity to ozone. The data suggest that the sulfhydryl group in the membrane is the primary target of ozone attack. Rec A DNA repair system does not appear to play a role in ozone resistance.
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PMID:Effect of ozone on metabolic activities of Escherichia coli K-12. 902 Apr 3

Serum response factor (SRF), a transcription factor ubiquitously involved in the processes of cellular proliferation and differentiation, has been implicated in cardiac and skeletal muscle development because of its strong expression in embryonic muscle lineages, and its necessity for the transcription of transiently transfected muscle genes that contain SRF binding sites. This study was designed to ascertain whether SRF is required for the expression of an endogenous SRF-dependent gene during differentiation of early embryonic cardiac myocytes by introducing a dominant-negative SRF construct via retroviral delivery. Although no effect on overt cellular differentiation was detected, semi-quantitative RT-PCR revealed that expression of the SRF-dependent gene cardiac alpha-actin was inhibited, whereas expression of the non-SRF-dependent genes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and cardiac troponin-C was unaffected. No effect on myocyte proliferation was detected. Curiously, immunohistochemical localization of SRF protein suggested that whereas endogenous SRF was homogeneously dispersed throughout the cytoplasm and nucleus, the dominant-negative SRF protein was concentrated in the nucleus. These results extend previous findings using transiently transfected genes to the endogenous level, indicating that SRF is required for the full expression of muscle genes that contain SRF binding sites during cardiac myocyte differentiation.
Anat Rec A Discov Mol Cell Evol Biol 2003 Apr
PMID:Inhibition of the cardiac alpha-actin gene in embryonic cardiac myocytes by dominant-negative serum response factor. 1262 74