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Query: UMLS:C0242706 (hyperoxia)
 5,219 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rana catesbeiana Shaw tadpoles and adults were maintained at 20-23 degrees C under aerial and aquatic normoxia (PO2 150 mmHg), hyperoxia (PO2 275 mmHg) and hypoxia (PO2 75 mmHg) for 4 weeks, after which the following blood measurements were made: haematocrit, red blood cell count, haemoglobin concentration, mean corpuscular haemoglobin concentration, O2 capacity, O2 equilibrium curve, Bohr shift, Hill's coefficient and intraerythrocytic concentration of nucleotide triphosphates (ATP + GTP) and 2,3-DPG. Normoxic tadpoles had much higher blood O2 affinity (P50 9-10 mmHg) than adults (P50 35 mmHg) but a lower haemoglobin concentration, haematocrit and O2 capacity. The concentration of intraerythrocytic phosphates was higher in normoxic tadpoles than in adults, indicating that the higher O2 affinity of normoxic tadpole blood was due to the haemoglobins themselves, rather than affinity modulators. Chronic hypoxia in tadpoles produced little change in whole blood P50, and no significant change in any other blood variable. In adult bullfrogs, on the other hand, O2 capacity doubled through polycythaemia, and the P50 decreased by 11 mmHg (35%), though apparently not from any significant change in concentration of intraerythrocytic phosphates. Hyperoxia produced no haematological changes in either larvae or adults. In adult bullfrogs exposed to chronic hypoxia, the morphology of the gas exchange organs does not change (Burggren & Mwalukomo, 1983), but instead profound adjustments occur in the blood, favouring O2 transport under these conditions. The blood of the tadpole shows little or no response to chronic hypoxia, with morphological adjustments in skin, gills and lungs constituting the major response.
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PMID:Respiration during chronic hypoxia and hyperoxia in larval and adult bullfrogs (Rana catesbeiana). II. Changes in respiratory properties of whole blood. 660 82

Exposure to hyperoxia has been demonstrated to alter the cell number of lung fibroblasts in vivo. The precise mechanism of lung fibroblast proliferation after hyperoxic exposure has not been elucidated, however. We examined the growth characteristics of lung fibroblasts isolated from 21-day-old rats exposed to air or 100% O2 for 8 days. Cell proliferation was assessed by hemocytometry, [3H]thymidine incorporation, and fractional labeling with the thymidine analog bromodeoxyuridine. Under all conditions tested, fibroblasts isolated from O2-exposed rats grew more rapidly than those from air-exposed rats. Conditioned medium from fibroblasts isolated from hyperoxia-exposed rats failed to increase the [3H]thymidine incorporation of control cells to that observed in cells isolated from hyperoxia-exposed animals, suggesting that an autocrine growth factor was not responsible for the excess proliferation. Sensitivity to exogenous growth factors was assessed by measuring the response to increasing concentrations of insulin-like growth factor-1 (IGF-1). Relative to 1% fetal bovine serum (FBS), concentrations of IGF-1 between 3 and 30 ng/ml significantly increased the [3H]thymidine incorporation of fibroblasts derived from hyperoxic animals, whereas control cells were unresponsive to IGF-1 stimulation. The apparent sensitivity to IGF-1 led us to assess the effect of in vivo hyperoxic exposure on the expression of c-Ha-ras, which encodes a membrane-bound, GTP-binding/hydrolyzing protein essential for progression through G1 in the cell cycle. ras mRNA levels in quiescent, control cells were minimal but increased following serum stimulation. The c-Ha-ras expression of lung fibroblasts from hyperoxia-exposed animals, on the other hand, was substantial in quiescent cells and remained high after serum exposure.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In vivo hyperoxic exposure increases cultured lung fibroblast proliferation and c-Ha-ras expression. 781 67

Hyperoxia is cytotoxic and depresses many cellular metabolic functions including protein synthesis. Translational control is exerted primarily during initiation by two mechanisms: 1) through inhibition of translation initiation complex formation via sequestration of the cap-binding protein, eukaryotic initiation factor (eIF) 4E, with inhibitory 4E-binding proteins (4E-BP); and 2) by prevention of eIF2-GTP-tRNA(i)(Met) formation and eIF2B activity by phosphorylated eIF2alpha. In this report, exposure of human lung fibroblasts to 95% O2 decreased the incorporation of thymidine into DNA at 6 h and the incorporation of leucine into protein beginning at 12 h. The reductions in DNA and protein synthesis were accompanied by increased phosphorylation of eIF4E protein and reduced phosphorylation of 4E-BP1. At 24 h, hyperoxia shifted 4E-BP1 phosphorylation to lesser-phosphorylated isoforms, increased eIF4E expression, and increased the association of eIF4E with 4E-BP1. Although hyperoxia did not change eIF2alpha expression, it increased its phosphorylation at Ser51, but not until 48 h. In addition, the activation of eIF2alpha was not accompanied by the formation of stress granules. These findings suggest that hyperoxia diminishes protein synthesis by increasing eIF4E phosphorylation and enhancing the affinity of 4E-BP1 for eIF4E.
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PMID:Hyperoxia alters the expression and phosphorylation of multiple factors regulating translation initiation. 1554 44