| 11. |
- Hollands, K G T, et al.
(author)
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Glazings and Coatings
- 2001
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In: Solar Energy: The State of the Art, edited by J. Gordon (James & James Science Publishers, London, England, 2001) pp. 29-107.. ; , s. 29-107
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Journal article (peer-reviewed)
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| 12. |
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| 13. |
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| 14. |
- Julius, S., et al.
(author)
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Cardiovascular risk reduction in hypertensive black patients with left ventricular hypertrophy: the LIFE study
- 2004
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In: J Am Coll Cardiol. - 0735-1097. ; 43:6, s. 1047-55
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Journal article (peer-reviewed)abstract
- OBJECTIVES: We report on a subanalysis of the effects of losartan and atenolol on cardiovascular events in black patients in the Losartan Intervention For Endpoint reduction in hypertension (LIFE) study. BACKGROUND: The LIFE study compared losartan-based to atenolol-based therapy in 9,193 hypertensive patients with left ventricular hypertrophy (LVH). Overall, the risk of the primary composite end point (cardiovascular death, stroke, myocardial infarction) was reduced by 13% (p = 0.021) with losartan, with similar blood pressure (BP) reduction in both treatment groups. There was a suggestion of interaction between ethnic background and treatment (p = 0.057). METHODS: Exploratory analyses were performed that placed LIFE study patients into black (n = 533) and non-black (n = 8,660) categories, overall, and in the U.S. (African American [n = 523]; non-black [n = 1,184]). RESULTS: A significant interaction existed between the dichotomized groups (black/non-black) and treatment (p = 0.005); a test for qualitative interaction was also significant (p = 0.016). The hazard ratio (losartan relative to atenolol) for the primary end point favored atenolol in black patients (1.666 [95% confidence interval (CI) 1.043 to 2.661]; p = 0.033) and favored losartan in non-blacks (0.829 [95% CI 0.733 to 0.938]; p = 0.003). In black patients, BP reduction was similar in both groups, and regression of electrocardiographic-LVH was greater with losartan. CONCLUSIONS: Results of the subanalysis are sufficient to generate the hypothesis that black patients with hypertension and LVH might not respond as favorably to losartan-based treatment as non-black patients with respect to cardiovascular outcomes, and do not support a recommendation for losartan as a first-line treatment for this purpose. The subanalysis is limited by the relatively small number of events.
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| 15. |
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| 16. |
- Sun, Yongxin, et al.
(author)
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Alpha1-antichymotrypsin/Alzheimer's peptide Abeta(1-42) complex perturbs lipid metabolism and activates transcription factors PPARgamma and NFkappaB in human neuroblastoma (Kelly) cells.
- 2002
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In: Journal of Neuroscience Research. - : Wiley. - 1097-4547 .- 0360-4012. ; 67:4, s. 511-522
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Journal article (peer-reviewed)abstract
- Amyloid-beta peptide (A) and the serpin proteinase inhibitor 1-antichymotrypsin (ACT) are components of the amyloid plaques associated with Alzheimer's disease (AD). A exists in soluble monomeric and oligomeric forms and in an insoluble polymerised fibrillar form, but it is not clear which of these plays the most important role in the etiology of AD. In vitro, A1-42 interacts with ACT, and as a result of this, ACT loses its proteinase inhibitor activity and polymerisation of A1-42 is promoted. Here we provide evidence that new molecular forms resulting from incubation of ACT with A1-42 have multiple cellular level effects on neuronal cells. The mixture of soluble A and an ACT/A complex formed by 2 hr incubation at a 10:1 molar ratio of A:ACT strongly induce cellular proliferation and expression of transcription factors peroxisome proliferator-activated receptor-gamma (PPAR) and NFB, and also increase uptake and depress degradation of native and oxidised low-density lipoprotein (LDL) by cells. Similar but less pronounced effects are seen when cells are exposed to the A peptide alone preincubated for 2 hr. A1-42 and to a lesser extent ACT/A1-42 complex mixture prepared by 2 hr incubation both inhibit association of native LDL with cells. Neither ACT alone nor the A1-42 and ACT/A1-42 forms prepared by 24-hr incubation show any significant effects in these assays. We propose that specific molecular forms of A1-42 and ACT/A1-42 complex mixture, both dependent on the abundances of A1-42 and ACT/A1-42 in vivo and on their time of exposure to each other, have cellular effects which are important for the initiation and progression of the pathologies associated with AD.
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| 17. |
- Sun, Yongxin, et al.
(author)
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Glioma cell activation by Alzheimer's peptide Abeta1-42, alpha1-antichymotrypsin, and their mixture.
- 2002
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In: Cellular and Molecular Life Sciences. - 1420-9071. ; 59:10, s. 43-1734
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Journal article (peer-reviewed)abstract
- We compared the effects of Alzheimer’s peptide (Ab1–42), a1-antichymotrypsin (ACT) and an ACT/Ab1–42 mixture on human glioma DK-MG cells. The solution of Ab (5 mM) formed by 2-h incubation at room temperature induced tumour necrosis factor-a (TNF-a) and interleukin (IL)-6 levels by 55 and 45%, respectively, and increased gelatinase B activity by 67%, while exposure of cells to the ACT/Ab1–42 mixture (1:10 molar ratio ACT: Ab1–42) under the same experimental conditions showed no effect on IL-6 levels or gelatinase B activity, but strongly induced TNF-a (by 190%), compared to the con- CMLS, Cell. Mol. Life Sci. 59 (2002) 1734–1743 1420-682X/02/101734-11 © Birkhäuser Verlag, Basel, 2002 CMLS Cellular and Molecular Life Sciences trols. Stimulation of the cells with Ab1–42 alone, but not with ACT, increased by about 20% low-density lipoprotein (LDL) uptake and mRNA levels for LDL receptor and HMG-CoA reductase, while the ACT/Ab1–42 mixture significantly increased LDL uptake (by 50%), up-regulated mRNA levels for LDL receptor and HMG-CoA reductase by 48 and 63%, respectively, and increased lipid accumulation by about 20-fold. These data suggest a possible new role for Ab in Alzheimer’s disease through its interaction with the inflammatory reactant, ACT.
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| 19. |
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| 20. |
- Wärnmark, A, et al.
(author)
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The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
- 2001
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 276:49, s. 45939-45944
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Journal article (peer-reviewed)abstract
- The N-terminal regions of the estrogen receptor ve (ER alpha -N) and beta (ER beta -N) were expressed and purified to homogeneity. Using NAM and circular dichroism spectroscopy, we conclude that both ER alpha -N and ER beta -N are unstructured in solution. The TATA box-binding protein (TBP) has been shown previously to interact with ERa-N in vitro and to potentiate ER-activated transcription. We used surface plasmon resonance and circular dichroism spectroscopy to confirm and further characterize the ER-N-TBP interaction. Our results show that the intrinsically unstructured ERa-N interacts with TBP, and suggest that structural changes are induced in ERa-N upon TBP interaction. Conformational changes upon target factor interaction have not previously been demonstrated for any N-terminal region of nuclear receptors. In addition, no binding of ER beta -N to TBP was detected. This difference in TBP binding could imply differential recruitment of target proteins by ERa-N and ER beta -N. The affinity of the ER alpha -N-TBP interaction was determined to be in the micromolar range (K-D = 10(-6) to 10(-5) m). Our results support models of TBP as a target protein for the N-terminal activation domain of ER alpha. Further, our results suggest that target proteins can induce and/or stabilize ordered structure in N-terminal regions of nuclear receptors upon interaction.
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