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  • S. Karger AG  (7)
  • 1
    In: Nephron Clinical Practice, S. Karger AG, Vol. 97, No. 2 ( 2004-11-17), p. c41-c48
    Abstract: 〈 i 〉 Background/Aim: 〈 /i 〉 A defect in skeletal muscle mitochondrial metabolism develops in patients with chronic renal failure on haemodialysis. Treatment with carnitine, a compound essential for normal mitochondrial function, has been suggested to have significant benefits in such patients, so we carried out a study to see if carnitine acts by improving muscle bioenergetics and function. 〈 i 〉 Methods: 〈 /i 〉 In a phase II randomised double-blind trial, patients with end-stage renal disease received placebo or intravenous 〈 i 〉 L 〈 /i 〉 -carnitine (20 mg/kg dry body weight three times weekly after haemodialysis) for 16 weeks (n = 13 in each group). 〈 sup 〉 31 〈 /sup 〉 P magnetic resonance spectroscopy, 〈 sup 〉 1 〈 /sup 〉 H magnetic resonance imaging and near-infrared spectroscopy were used to measure muscle bioenergetics and function at baseline and at 16 weeks. 〈 i 〉 Results: 〈 /i 〉 There were no significant differences between groups at baseline. Mean plasma carnitine rose 10-fold in the carnitine group but was unchanged in the placebo group. 〈 i 〉 L 〈 /i 〉 -Carnitine had no statistically significant effect on any of the parameters measured. The rate of proton efflux from muscle, as a measure of tissue perfusion, was low in both groups and was not affected by treatment. 〈 i 〉 Conclusions: 〈 /i 〉 The study failed to show any significant effect of 16 weeks’ 〈 i 〉 L 〈 /i 〉 -carnitine supplementation on these objective measures of muscle metabolism and function. Slow proton efflux from muscle provides evidence supporting low blood flow and, therefore, decreased oxygen availability, as an underlying mechanism for muscle mitochondrial dysfunction in this disorder.
    Type of Medium: Online Resource
    ISSN: 1660-2110
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2004
    detail.hit.zdb_id: 2098336-0
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  • 2
    Online Resource
    Online Resource
    S. Karger AG ; 1970
    In:  Acta Haematologica Vol. 44, No. 2 ( 1970), p. 111-123
    In: Acta Haematologica, S. Karger AG, Vol. 44, No. 2 ( 1970), p. 111-123
    Type of Medium: Online Resource
    ISSN: 0001-5792 , 1421-9662
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1970
    detail.hit.zdb_id: 1481888-7
    detail.hit.zdb_id: 80008-9
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  • 3
    Online Resource
    Online Resource
    S. Karger AG ; 1999
    In:  International Archives of Allergy and Immunology Vol. 120, No. 1 ( 1999), p. 30-42
    In: International Archives of Allergy and Immunology, S. Karger AG, Vol. 120, No. 1 ( 1999), p. 30-42
    Abstract: 〈 b 〉 Background: 〈 /b 〉 This study was performed to get further insights into antibody responses to cross–reactive carbohydrate determinants (CCD), including initial experiments to prove the biological activity of anti–CCD IgE. Earlier studies have shown that IgE specific for CCD occurs in about 25% of celery–allergic patients. The clinical significance of these antibody specificities is doubtful. 〈 b 〉 Methods: 〈 /b 〉 Patient sera were selected on the basis of a positive case history of celery allergy and multiple binding to high molecular weight celery allergens on immunoblots. Specific IgE to native and heated celery tuber was determined by the enzyme allergosorbent test (EAST). N–glycans were purified after extensive digestion of specific glycoproteins, such as pineapple stem bromelain, bovine fibrin, and human IgG, and used as antigens in an IgE ELISA as well as in EAST and immunoblotting inhibition experiments. Dose–related histamine release was performed with BSA neoglycoproteins containing 3–4 units of the purified glycopeptides. 〈 b 〉 Results: 〈 /b 〉 Seven celery–allergic patients were identified who clearly presented IgE against the N–glycan purified from bromelain which is a common structure within the plant kingdom. Chemical defucosylation showed that α1,3–fucose is a key structure for IgE binding. In patients with anti–CCD IgE, the maximal inhibition of celery EAST by the bromelain glycan ranged from 22 to 100%. Inhibition of celery immunoblots by preincubation of patient serum with this glycan led to a quenching of multiple bands at masses 〉 40 kD. After linking the bromelain glycopeptide to BSA, a strong dose–related histamine release was obtained in a celery–allergic patient, occurring at lower concentrations than with the recombinant major protein allergen from celery, Api g 1. 〈 b 〉 Conclusions: 〈 /b 〉 Our results demonstrate that IgE specific for CCD is common in celery–allergic patients, and can represent the major proportion of IgE against this food. α1,3–fucose was confirmed to be an essential part of the IgE epitope. Immunoblotting inhibition indicated the presence of this carbohydrate determinant on multiple glycoproteins in celery extract. Although histamine release was only performed in 1 patient, our data show that proteins carrying multiple glycan units can be biologically active in patients sensitized to CCD.
    Type of Medium: Online Resource
    ISSN: 1018-2438 , 1423-0097
    RVK:
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1999
    detail.hit.zdb_id: 1482722-0
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  • 4
    Online Resource
    Online Resource
    S. Karger AG ; 1999
    In:  International Archives of Allergy and Immunology Vol. 118, No. 2-4 ( 1999), p. 411-413
    In: International Archives of Allergy and Immunology, S. Karger AG, Vol. 118, No. 2-4 ( 1999), p. 411-413
    Abstract: Grass pollen allergens of group I are particularly important because of their high IgE prevalence and occurrence in all grass species. Four independent IgE–binding regions and one continous epitope were identified. The posttranslational modifications on the molecule increased allergenicity. Phl p 1 is a cysteine protease, as determined by specific substrates, inhibitors and consensus sequence motifs. In analogy to other allergens and/or proteases, we deduce that Phl p 1 might enhance the permeability of the epithelium, influence T helper cells to bias Th2, and increase the IgE production of plasma cells. Thus, the group I allergens seem to be the crucial components in a pollen extract which can mediate sensitization and enhance the triggering of symptoms leading to the persistence of a grass pollen allergy.
    Type of Medium: Online Resource
    ISSN: 1018-2438 , 1423-0097
    RVK:
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1999
    detail.hit.zdb_id: 1482722-0
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  • 5
    Online Resource
    Online Resource
    S. Karger AG ; 2002
    In:  Transfusion Medicine and Hemotherapy Vol. 29, No. 6 ( 2002), p. 305-307
    In: Transfusion Medicine and Hemotherapy, S. Karger AG, Vol. 29, No. 6 ( 2002), p. 305-307
    Type of Medium: Online Resource
    ISSN: 1660-3796 , 1660-3818
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2002
    detail.hit.zdb_id: 2100533-3
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  • 6
    Online Resource
    Online Resource
    S. Karger AG ; 1912
    In:  Dermatology Vol. 19, No. 1 ( 1912), p. 22-45
    In: Dermatology, S. Karger AG, Vol. 19, No. 1 ( 1912), p. 22-45
    Type of Medium: Online Resource
    ISSN: 1018-8665 , 1421-9832
    RVK:
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1912
    detail.hit.zdb_id: 1482189-8
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  • 7
    Online Resource
    Online Resource
    S. Karger AG ; 1916
    In:  Dermatology Vol. 23, No. 5 ( 1916), p. 257-287
    In: Dermatology, S. Karger AG, Vol. 23, No. 5 ( 1916), p. 257-287
    Type of Medium: Online Resource
    ISSN: 1018-8665 , 1421-9832
    RVK:
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1916
    detail.hit.zdb_id: 1482189-8
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