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Sökning: swepub > (2003)

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  • Magnusson, J, et al. (författare)
  • A kinetic study in adults with food hypersensitivity assessed as eosinophil activation in fecal samples
  • 2003
  • Ingår i: Clinical and Experimental Allergy. - : Wiley. - 0954-7894 .- 1365-2222. ; 33:8, s. 1052-1059.
  • Tidskriftsartikel (refereegranskat)abstract
    • BACKGROUND: Immune-mediated food hypersensitivity affecting the gut is difficult to evaluate, and objective tools to diagnose local gastrointestinal (GI) inflammatory reactions are lacking. OBJECTIVES: To determine whether allergic manifestations in adults with a history of food-related GI symptoms could be assessed in feces during symptomatic and non-symptomatic periods, using the surrogate markers, eosinophil cationic protein (ECP), eosinophil protein X (EPX) and myeloperoxidase (MPO). METHODS: Thirteen subjects with food hypersensitivity-related GI symptoms, confirmed by a positive double-blind placebo-controlled food challenge (DBPCFC), were subjected to an open kinetic food challenge design for 6 weeks. Symptoms were recorded and scored during the 3-week study period and stool samples were obtained every day. The surrogate markers ECP, EPX and MPO were measured in the supernatants from feces samples. RESULTS: A significant increase in abdominal pain, distension and flatulence was observed during challenge, with a gradual decrease during elimination diet. Both between days and subjects, EPX levels were more frequently increased compared to ECP and MPO. Individuals with a history of a short duration of symptoms had significantly higher mean levels of EPX and MPO than those with a longer duration of symptoms. CONCLUSIONS: An overall increase in levels of eosinophil markers, in particular EPX, was observed in feces from patients with food-related GI symptoms. However, rather than being a tool to differentiate symptomatic from non-symptomatic periods, EPX might be used for detecting an ongoing clinical or subclinical chronic inflammation, that may have an impact on the patient's clinical course of GI symptoms.
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  • Jägerbrand, Annika K., et al. (författare)
  • Responses of bryophytes to simulated environmental change at Latnjajaure, northern Sweden
  • 2003
  • Ingår i: Journal of Bryology. - : Taylor & Francis. - 0373-6687 .- 1743-2820. ; 25:3, s. 163-168
  • Tidskriftsartikel (refereegranskat)abstract
    • We simulated a predicted environmental change in a subarctic-alpine plant community to study short-term growth in Hylocomium splendens, and three-year effects in abundance changes of the five most common bryophytes at Latnjajaure, northern Sweden. The experiment had a factorial design with increased temperature and nutrients, alone and in combination. Moss growth was measured during the 1995 growing season, and we measured species abundance before and after three years of environmental perturbation. The combined treatments of fertilizer and temperature enhancement caused a decreased growth in length and dry weight in H. splendens. There was a significant decrease in abundance of Rhytidium rugosum in the combined temperature and fertilizer treatment. The other four common bryophyte species (Aulacomnium turgidum, Dicranum groenlandicum, Hylocomium splendens, and Ptilidium ciliare) showed weaker, but not significant trends in the same direction. As the bryophytes are an important component of arctic and subarctic vegetation, we expect that they will play a key role in the impact of anticipated Global Change on the ecosystems.
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  • Johansson, A., et al. (författare)
  • Synthesis and photophysics of one mononuclear Mn(III) and one dinuclear Mn(III,III) complex covalently linked to a ruthenium(II) tris(bipyridyl) complex
  • 2003
  • Ingår i: Inorganic Chemistry. - : American Chemical Society (ACS). - 0020-1669 .- 1520-510X. ; 42, s. 7502-7511
  • Tidskriftsartikel (refereegranskat)abstract
    • The preparation of donor (D)-photosensitizer (S) arrays, consisting of a manganese complex as D and a ruthenium tris(bipyridyl) complex as S has been pursued. Two new ruthenium complexes containing coordinating sites for one (2a) and two manganese ions (3a) were prepared in order to provide models for the donor side of photosystem II in green plants. The manganese coordinating site consists of bridging and terminal phenolate as well as terminal pyridyl ligands. The corresponding ruthenium-manganese complexes, a manganese monomer 2b and dimer 3b, were obtained. For the dimer 3b, our data suggest that intramolecular electron transfer from manganese to photogenerated ruthenium(III) is fast, k(ET) > 5 x 10(7) s(-1).
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  • Carlberg, Inger, et al. (författare)
  • A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
  • 2003
  • Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 100:2, s. 757-62
  • Tidskriftsartikel (refereegranskat)abstract
    • The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of Arabidopsis and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions.
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  • Ehrenberg, M., et al. (författare)
  • Systems biology is taking off
  • 2003
  • Ingår i: Genome Research. - : Cold Spring Harbor Laboratory. - 1088-9051 .- 1549-5469. ; 13, s. 2475-2484
  • Tidskriftsartikel (refereegranskat)
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