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| 2. |
- Ahrenstedt, Örjan, et al.
(författare)
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Enhanced local production of the complement components in the small intestine in Crohn's disease
- 1990
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Ingår i: New England Journal of Medicine. - 0028-4793 .- 1533-4406. ; 322, s. 1345-1349
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Tidskriftsartikel (refereegranskat)abstract
- There is evidence that complement components may be formed locally in inflammatory lesions containing monocytes and macrophages. To investigate the role of complement in Crohn's disease we measured jejunal-fluid concentrations of the complement components C4, C3, and factor B by perfusion of a closed segment of the jejunum in 22 patients with Crohn's disease thought to be limited to the terminal ileum.The mean (±SEM) jejunal-fluid C4 concentration was 2.0±0.3 mg per liter, significantly higher than the mean level in 35 healthy controls (0.7±0.1 mg per liter; P<0.001). The mean C3 concentration was 1.0±0.1 mg per liter in the patients and 0.7±0.1 mg per liter in the controls (P<0.05). The factor B levels were similar in the two groups. Calculated rates of intestinal secretion of these components showed differences of the same magnitude. Leakage of protein from plasma was not increased. The jejunal-fluid serum ratios of these complement proteins indicated that their appearance in the lumen of the jejunum was due at least in part to local mucosal synthesis. The increased jejunal secretion of C4, but not C3 or factor B, paralleled the clinical activity of Crohn's disease. Values were normal in first-degree relatives of the patients (n = 13), patients with celiac disease (n = 8), and patients with ulcerative colitis (n = 4).We conclude that increased secretion of complement by clinically unaffected jejunal tissue in patients with Crohn's disease reflects the systemic nature of this disorder and may be due to the stimulated synthesis of complement by activated intestinal monocytes and macrophages.
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| 3. |
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| 4. |
- Graham, Gil, et al.
(författare)
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Motion in a Vertical Circle
- 1997
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Ingår i: Physics Education. - : IOP Publishing. - 0031-9120 .- 1361-6552. ; 32:5, s. 313-
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Tidskriftsartikel (refereegranskat)
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| 5. |
- Hänni, Mari, et al.
(författare)
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Quantitation of atherosclerosis by magnetic resonance imaging and 3-D morphology operators
- 1999
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Ingår i: Magnetic Resonance Imaging. - 0730-725X .- 1873-5894. ; 17:4, s. 585-591
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Tidskriftsartikel (refereegranskat)abstract
- The objective was to ascertain whether MRI and image processing can be used to quantify atherosclerosis by measuring wall thickness in rabbit aorta. The abdominal aortas of 2 healthy and 5 atherosclerotic rabbits were examined with a gradient-echo inflow angiography sequence (2DI) and a proton density weighted turbo-spin-echo sequence (PDW). Using thresholding by four observers and 3D morphology operators, segmentation of the artery and vein lumina was performed from the 2DI sequence, and of surrounding fat and muscle from the PDW sequence. Remaining voxels adjacent to the aortic lumen were classified as vessel wall. By measuring the vessel wall volume and the lumen volume, the wall percentage was calculated. The values were significantly higher for the diseased animals than for unaffected individuals (p < 0.01). It is concluded that aortic wall thickening in atherosclerotic rabbits can be measured quantitatively by using MRI combined with 3D morphology image processing operators.
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| 6. |
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| 7. |
- Nilsson, Lennart
(författare)
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Lipoamidase
- 1994
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Lipoamidase, an enzyme which removes lipoic acid from the e-amino group of a lysine residue in 2-oxoacid dehydrogenase complexes, has been measured in human serum and breast milk, and in different rat tissues. Serum from a boy with biotinid~e deficiency had low lipoarnidase activity measured as lipoyl-lysine hydrolase (LLH) and lipoyl-PABA hydrolase (LPH). Unexpectedly, LPH was not decreased in the same order as LLH and biotinidase, indicating that LPH in serum differs from the main lipoamidase.Lipoamidase measured as LLH and LPH was purified 20 000-fold to homogeneity from human serum, and after SDS/PAGE gave one band with an apparent molecular weight of 76 kDa. Lipoarnidase was eo-purified with biotinidase indicating that these enzyme activities belong to the same protein. After IEP in the presence of cysteine as thiol stabilizer two peaks were obtained, one of them probably being a cysteine adduct.The properties of the enzymes from a crude preparation of rat liver microsomes also indicated that lipoamidase measured as LLH belongs to the same enzyme protein as biotinidase, whereas LPH is another enzyme. These enzymes were solubilized from rat liver microsomes andseparated from each other by arrunonium sulphate fractionation. From these studies I conclude that lipoamidase activities in human serum and in rat liver are not derived from a genuine lipoamidase. Lipoamidase measured as LLH is the same enzyme as biotinidase and LPH is an enzyme different from biotinidase. Because we do not yet know the biological function of LPH, I prefer the names lipoyl-p-aminbenzoic acid hydrolase and lipoyl-X hydrolase.
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| 8. |
- Nilsson, Örjan, et al.
(författare)
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Datorn i skolfysiken
- 1990
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Ingår i: Kosmos 1990. - Uppsala : Swedish Science Press. ; , s. 193-214
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Bokkapitel (populärvet., debatt m.m.)
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