| 1. |
- Knudsen, D. J., et al.
(författare)
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Sub-kilometer thermal plasma structure near 1750 km altitude in the polar cusp/cleft
- 1994
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Ingår i: Geophysical Research Letters. - 0094-8276. ; 21:17, s. 1907-1910
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Tidskriftsartikel (refereegranskat)abstract
- We present Freja Cold Plasma Analyzer (CPA) measurements from an encounter with the low altitude (approx.1750 km) polar cusp during which the CPA measured 2-D images of the thermal (0-16 eV) particle distributions at 1.2 s time resolution, and simultaneously made rapid estimates (600/s) of integrated thermal particle flux into the instrument. The high resolution data show bursty ion flux enhancements of the order of tens of percent on time scales of tens of ms, or alternatively, hundreds of m spatial scales. The flux of electrons from 0-16 eV also varied by tens of percent and on temporal/spatial scales comparable to those in the ion cases. There is some evidence that the thermal particle flux variations are associated with intense low-frequency electromagnetic fluctuations with temporal/spatial scales identical to those seen by the CPA (tens of ms. hundreds of m).
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| 2. |
- Olsson, U, et al.
(författare)
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Effects of selenium deficiency on xenobiotic-metabolizing and other enzymes in rat liver.
- 1993
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Ingår i: International Journal for Vitamin and Nutrition Research. - 0300-9831 .- 1664-2821. ; 63:1
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Tidskriftsartikel (refereegranskat)abstract
- The present study was undertaken to characterize effects of selenium (Se) deficiency on 16 enzymes recovered in either one or more of the subcellular fractions of rat liver (as a basis for future studies on the mechanisms underlying the observed changes). Male rats were fed a Torula-yeast based diet with 0.23 mg Se/kg or the same diet with 0.009 mg Se/kg, from weaning and for 10 weeks. Statistically significant effects of Se deficiency were the following: Se-dependent glutathione peroxidase decreased to 0.14% of the Se-adequate controls, while cytosolic glutathione transferase increased 3-fold in Se deficiency when CDNB was the substrate, but decreased significantly when trans-stilbene oxide (diagnostic for subunit 4) was used as the substrate. Cytosolic DT-diaphorase increased about 7-fold in Se deficiency. Further, DT-diaphorase in the microsomal fraction was also significantly increased in Se deficiency, as were the microsomal and mitochondrial epoxide hydrolases and microsomal glutathione transferase. Furthermore, increased activity of the peroxisomal marker enzyme catalase (P < 0.05) was noted in Se-deficient rats. It is our working hypothesis that changes in enzyme activities in Se deficiency are mainly due to changed levels of endogenously generated metabolites or altered functions of endocrine tissues.
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| 3. |
- Olsson, U, et al.
(författare)
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The involvement of selenium in peroxisome proliferation caused by dietary administration of clofibrate to rats.
- 1992
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Ingår i: Chemico-Biological Interactions. - 0009-2797 .- 1872-7786. ; 85:1
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Tidskriftsartikel (refereegranskat)abstract
- The effects of dietary treatment with clofibrate (0.5% w/w for 10 days) on the livers of selenium-deficient male rats were examined. The peroxisome proliferation (as determined by electron microscopy) in the livers of selenium-deficient animals was much less pronounced than in the case of selenium-adequate rats and no increase in peroxisomal fatty acid beta-oxidation (assayed both as antimycin-insensitive palmitoyl-CoA oxidation and lauroyl-CoA oxidase activity) was observed in the deficient animals. On the other hand, in selenium-deficient rats clofibrate caused increases in the specific activity of microsomal lauric acid omega- and omega-1-hydroxylation and an apparent change in mitochondrial size, seen as a redistribution of mitochondria from the 600 x g(av) pellet to the 10,000 x g(av) pellet, which were approximately 50% as great as the corresponding effects on control animals. Obviously, then, these three different effects of clofibrate are not strictly coupled and may involve at least partially distinct underlying mechanisms. Initial experiments demonstrated that peroxisome proliferation could be obtained by exposing primary hepatocyte cultures derived from selenium-deficient rats to clofibric acid (an in vivo hydrolysis product of clofibrate which is the proximate peroxisome proliferator), nafenopin or mono(2-ethylhexyl)phthalate. This finding suggests that selenium deficiency does not have a direct influence on the basic process(es) underlying peroxisome proliferation, but rather has indirect effects, influencing, for example, the pharmacokinetics of clofibrate and/or hormonal factors.
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| 4. |
- Eriksson, A M, et al.
(författare)
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Is the cytosolic catalase induced by peroxisome proliferators in mouse liver on its way to the peroxisomes?
- 1992
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Ingår i: FEBS Letters. - 0014-5793 .- 1873-3468. ; 308:2
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Tidskriftsartikel (refereegranskat)abstract
- Dietary treatment of male C57B1/6 mice with clofibrate, nafenopin or WY-14.643 resulted in a modest (at most 2-fold) increase in the total catalase activity in the whole homogenate and mitochondrial fraction prepared from the livers of these animals. On the other hand, the catalase activity recovered in the cytosolic fraction was increased 12- to 18-fold, i.e. 30-35% of the total catalase activity in the hepatic homogenate was present in the high-speed supernatant fraction after treatment with these peroxisome proliferators. A study of the time course of the changes in peroxisomal and cytosolic catalase activities demonstrated that the peroxisomal activity both increased upon initiation of exposure and decreased after termination of treatment several days after the increase and decrease, respectively, in the corresponding cytosolic activity. This finding suggests that the cytosolic catalase may be on its way to incorporation into peroxisomes.
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| 5. |
- Eriksson, A M, et al.
(författare)
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Studies on the intracellular distributions of soluble epoxide hydrolase and of catalase by digitonin-permeabilization of hepatocytes isolated from control and clofibrate-treated mice.
- 1991
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Ingår i: European Journal of Biochemistry. - 0014-2956 .- 1432-1033. ; 198:2
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Tidskriftsartikel (refereegranskat)abstract
- Digitonin permeabilization of hepatocytes from control and clofibrate-treated (0.5% by mass, 10 days) male C57bl/6 mice was used to study the intracellular distributions of soluble ('cytosolic') epoxide hydrolase and of catalase. The following conclusions were drawn. (1) About 60% of the total soluble epoxide hydrolase activity in control mouse hepatocytes is situated in the cytosol. (2) The rest is not mitochondrial, but probably peroxisomal. (3) Of the total catalase activity in control mouse hepatocytes, 5-10% is found in the cytosol. (4) Treatment of mice with clofibrate increases the total hepatocyte activity of soluble epoxide hydrolase 4-fold, but does not influence the relative distribution of this enzyme between cytosol and peroxisomes. (5) The total catalase activity is increased 3.5-fold by clofibrate treatment and 15-35% of this activity is shifted from the peroxisomes to the cytosol.
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| 6. |
- Eriksson, Jan W, et al.
(författare)
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Insulin concentrations and insulin sensitivity after short-term amiloride in healthy subjects
- 1994
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Ingår i: European Journal of Clinical Pharmacology. - 0031-6970 .- 1432-1041. ; 46:5, s. 469-472
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Tidskriftsartikel (refereegranskat)abstract
- We have evaluated the short-term effects of amiloride on insulin action in vivo, since amiloride is known to impair insulin action in vitro.Seven healthy subjects were treated according to a randomized, double-blind, cross-over protocol. The treatment periods were 3 days each with amiloride 15 mg daily and placebo. Insulin action on glucose turnover was assessed directly after each treatment period with the hyper-insulinaemic euglycaemic glucose clamp technique.At the two insulin concentrations studied (∼ 30 mU·l−1 and ∼ 200 mU·l−1), the glucose infusion rate required to maintain constant euglycaemia did not differ after either amiloride or placebo. The rates of glucose production and utilization were also similar, whereas the so-called insulin sensitivity index at the lower insulin concentration was significantly reduced (by about 15 %) after amiloride. Moreover, amiloride produced significantly higher fasting insulin and C-peptide concentrations, whereas fasting glucose and NEFA concentrations were unaltered.In conclusion, these data suggest that short-term amiloride slightly impairs insulin sensitivity with respect to glucose uptake. However, overall glucose homoeostasis does not appear to be affected, probably due to a compensatory rise in plasma insulin.
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