lnu.sePublications
Change search
Refine search result
1 - 23 of 23
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Christerson, Ulrika
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Keita, Åsa V
    Söderholm, Johan D
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Increased expression of protease-activated receptor-2 in mucosal mast cells in Crohn's ileitis2009In: Journal of Crohn's & Colitis, ISSN 1873-9946, E-ISSN 1876-4479, Vol. 3, no 2, p. 100-108Article in journal (Refereed)
    Abstract [en]

    Background and aims

    Activation of protease-activated receptor-2 (PAR-2) may stimulate various events of importance in inflammatory processes, including release of inflammatory mast cell mediators. PAR-2 is frequently up-regulated during inflammatory conditions, but it is not known if the expression is altered in Crohn's disease. The aim of the present study was to investigate the ileal mucosal PAR-2 expression in Crohn's ileitis, with particular emphasis on the expression in ileal mucosal mast cells.

    Methods

    Surgical specimens from the distal ileum were collected from patients with Crohn's ileitis and patients with colonic cancer as controls. The overall expression of PAR-2 was investigated by Western blot, and the presence of PAR-2 expressing mucosal mast cells by immunohistochemistry and cell counting. The effect of tumor necrosis factor-α (TNF-α) on the PAR-2 expression in a human mast cell line (HMC-1) was investigated by RT-PCR and immunocytochemistry.

    Results

    In Crohn's specimens, the fraction of PAR-2-expressing mucosal mast cells was increased about 2.5 times (P < 0.001; n = 14) compared with specimens from control patients (n = 6). No difference was found between inflamed (n = 6) and uninflamed Crohn's specimens (P > 0.05; n = 8). Exposure to TNF-α for 48 h up-regulated PAR-2 mRNA and protein expression in the HMC-1 cell line.

    Conclusion

    PAR-2 is up-regulated on ileal mucosal mast cells in Crohn's ileitis, possibly due to the action of inflammatory cytokines, such as TNF-α. This may contribute to perpetuating the inflammatory process in the intestinal mucosa in Crohn's ileitis.

  • 2.
    Christerson, Ulrika
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Keita, Åsa V
    Söderholm, Johan D
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Potential role of protease-activated receptor-2-stimulated activation of cytosolic phospholipase A2 in intestinal myofibroblast proliferation: Implications for stricture formation in Crohn´s disease2009In: Journal of Crohn's & Colitis, ISSN 1873-9946, E-ISSN 1876-4479, Vol. 3, no 1, p. 15-24Article in journal (Refereed)
    Abstract [en]

    Background and aims

    Myofibroblast hyperplasia contributes to muscularis mucosae thickening and stricture formation in Crohn's disease (CD). Protease-activated receptor-2 (PAR-2) and cytosolic phospholipase A2 (cPLA2) are known regulators of cell growth, but their significance in intestinal myofibroblast proliferation remain to be elucidated. The principle aims of the present study were to investigate if PAR-2 is expressed in the expanded muscularis mucosa in ileal CD specimens, if inflammatory cytokines may stimulate PAR-2 expression in intestinal myofibroblasts, and if PAR-2 and cPLA2 may regulate intestinal myofibroblast growth.

    Methods

    Immunohistochemistry was used for detection of PAR-2 in ileal CD specimens. Studies on PAR-2 expression, PLA2 activation and cell growth were performed in a human intestinal myofibroblast cell line, CCD-18Co. PAR-2 expression was investigated by RT-PCR and immunocytochemistry. PLA2 activity was analyzed by quantification of released 14C-arachidonic acid (14C-AA). Cell growth was examined by 3H-thymidine incorporation and cell counting.

    Results

    The thickened muscularis mucosae of the CD specimens showed strong PAR-2 expression. In cultured myofibroblasts, tumor necrosis factor-α (TNF-α) up-regulated PAR-2 mRNA and protein, and potentiated PAR-2-stimulated 14C-AA release by two known PAR-2 activators, trypsin and SLIGRL-NH2. The release of 14C-AA was dependent on cPLA2. Trypsin stimulated the proliferation of serum-starved cells, and inhibition of cPLA2 reduced normal cell growth and abolished the growth-promoting effect of trypsin.

    Conclusions

    The results suggest that PAR-2-mediated cPLA2 activation might be of importance in intestinal myofibroblast proliferation. The results also point to the possibility that PAR-2 up-regulation by inflammatory cytokines, like TNF-α, may modulate this effect.

     

     

     

     

     

  • 3.
    Christerson, Ulrika
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Keita, Åsa, V
    Linköping University, Sweden.
    Winberg, Martin E.
    Linköping University, Sweden.
    Söderholm, Johan D.
    Linköping University, Sweden;County Council Östergötland, Sweden.
    Gustafson-Svärd, Christina
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Possible Involvement of Intracellular Calcium-Independent Phospholipase A(2) in the Release of Secretory Phospholipases from Mast Cells-Increased Expression in Ileal Mast Cells of Crohn's Disease2019In: Cells, E-ISSN 2073-4409, Vol. 8, no 7, p. 1-15, article id 672Article in journal (Refereed)
    Abstract [en]

    Increased activity of secretory phospholipases A(2) (sPLA(2)) type-II was previously observed in ileum of Crohn's disease (CD). Our aims were to explore the involvement of calcium-independent (i)PLA(2 beta) in the release of sPLA(2)s from the human mast cell (MC) line (HMC-1) and investigate expressions of cytosolic (c)PLA(2) alpha, iPLA(2)beta, sPLA(2)-IIA and sPLA(2)-V in MCs of CD ileum. The release of sPLA(2) was investigated in HMC-1 by immunocytochemistry and ELISA. The expression intensities of PLA(2)s in mucosal MCs, and the proportion of PLA(2)-positive MCs, were investigated in normal ileum and in ileum from patients with CD by immunohistochemistry. The calcium ionophore-stimulated release of sPLA(2)-IIA and sPLA(2)-V from HMC-1 was reduced by the iPLA(2)-inhibitor bromoenol lactone. All four PLA(2)s were detectable in mucosal MCs, both in normal ileum and in CD, but the proportion of iPLA(2)beta-containing mucosal MCs and the expression intensity of sPLA(2)-IIA was increased in CD. Results indicate that iPLA(2)beta is involved in the secretion of sPLA(2)s from HMC-1, and suggest that iPLA(2)beta-mediated release of sPLA(2) from intestinal MCs may contribute to CD pathophysiology. Ex vivo studies on isolated mucosal mast cells are however needed to clarify the precise role of MC PLA(2)s in the inflammatory processes of CD.

  • 4. Dimberg, J
    et al.
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Weström, B
    Tagesson, C
    Söderkvist, P
    Group I phospholipase A2 mRNA expression in rat glandular stomach and pancreas. Ontogenic development and effects of cortisone acetate1992In: Biochim Biophys Acta, Vol. 1130, p. 47-51Article in journal (Refereed)
  • 5. Dimberg, J
    et al.
    Lilja, I
    Weström, B
    Tagesson, C
    Söderkvist, P
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ontogeny of group II phospholipase A2 gene expression in rat stomach and ileum1995In: Biol Neonate, Vol. 67, p. 113-121Article in journal (Refereed)
  • 6.
    Gustafson-Svärd, Christina
    et al.
    Linköping University.
    Franzén, L
    Tagesson, C
    Phospholipase activation and arachidonic acid release in isolated intestinal epithelial cells1988In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 23, no 4, p. 413-421Article in journal (Refereed)
    Abstract [en]

    A novel method for studying the mobilization of free arachidonic acid (AA) in isolated intestinal epithelial cells is described. The method is based on labeling the cellular phospholipids with 14C-AA and studying the release of this 14C-AA on subsequent phospholipase activation. Cells of high viability were isolated from the small intestine of guinea pigs and incubated with 14C-AA for 2 h; most of the incorporated 14C-AA was then esterified into phosphatidylethanolamine and phosphatidylcholine. When the labeled cells were stimulated with the calcium ionophore A23187 in the presence of external calcium, they released significant amounts of AA. In contrast, the cells released no AA when stimulated with A23187 in the absence of external calcium or in the presence of chlorpromazine or 4-bromophenacyl bromide, both of which are known to inhibit phospholipase A2 activity. On the other hand, the cells released significant AA in response to exogenous phospholipase C from Clostridium perfringens. These findings indicate that AA release in intestinal cells may be caused by calcium-mediated phospholipase A2 activation or by products of microbial phospholipase C activity. They also suggest the further use of 14C-AA-labeled cells for studying agents and mechanisms that may influence the release of AA in the gastrointestinal tract.

  • 7.
    Gustafson-Svärd, Christina
    et al.
    Clinical Research Center, Linköping University .
    Kald, B
    Sjödahl, R
    Tagesson, C
    Phospholipase C from Clostridium perfringens stimulates formation of platelet-activating factor (PAF-acether) in cultured intestinal epithelial cells (INT 407)1991In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 26, no 10, p. 1000-1006Article in journal (Refereed)
    Abstract [en]

    This study demonstrates the ability of phospholipase C from Clostridium perfringens to stimulate the generation of platelet-activating factor (PAF-acether) in cultured intestinal epithelial cells (INT 407). Cells were exposed to phospholipase C for up to 60 min, and the content of PAF-acether within the cells and in the extracellular medium was determined. Phospholipase C caused a time-dependent formation of PAF-acether within the cells and also release of PAF-acether to the medium. In contrast, phospholipase C did not affect the cellular acetylhydrolase activity or the ability of the cells to metabolize extracellularly added C-14-PAF-acether. These findings suggest the possibility that intestinal epithelial cells, when stimulated with a naturally occurring intestinal bacterial toxin, generate and release PAF-acether. The possibility that this might contribute to the pathophysiology of inflammatory bowel disease is discussed. 

  • 8.
    Gustafson-Svärd, Christina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lilja, I
    Hallböök, O
    Sjödahl, R
    Cyclooxygenase and colon cancer; clues to the aspirin effect?1997In: Ann Med, Vol. 29, p. 247-252Article in journal (Refereed)
  • 9.
    Gustafson-Svärd, Christina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lilja, I
    Hallböök, O
    Sjödahl, R
    Cyclooxygenase-1 and cyclooxygenase-2 gene expression in human colorectal adenocarcinomas and in azoxymethane induced colonic tumours in rats1996In: Gut, Vol. 38, p. 79-84Article in journal (Refereed)
  • 10.
    Gustafson-Svärd, Christina
    et al.
    Clinical Research Center, Linköping University.
    Lindahl, M
    Tagesson, C
    Hydrogen peroxide stimulates phospholipase A2 -mediated arachidonic acid release in cultured intestinal epithelial cells (INT 407)1991In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 26, no 3, p. 237-247Article in journal (Refereed)
    Abstract [en]

    The mechanisms by which hydrogen peroxide and, for comparison, 4-beta-phorbol-12-myristate-13-acetate (PMA) stimulate release of radiolabeled arachidonic acid (C-14-AA) in cultured intestinal epithelial cells (INT 407) were investigated. Both hydrogen peroxide and PMA caused a rapid (3 min) and dose-related intracellular release of free C-14-AA, followed by a dose- and time-dependent release of C-14-AA into the extracellular medium, but hydrogen peroxide was about 50,000 times less effective than PMA in releasing C-14-AA. No C-14-AA was released on stimulation with 4-alpha-phorbol-12,13-di-decanoate (PDD), a phorbol ester that does not activate protein kinase C. The C-14-AA release was reduced by the phospholipase A2 inhibitors nordihydroguaiaretic acid and 4-bromophenacyl bromide and by the calmodulin/protein kinase C inhibitor trifluoperazine and the protein kinase C inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7). However, H-7 was less effective than the other inhibitors in reducing the hydrogen peroxide-stimulated C-14-AA release. The hydrogen peroxide-stimulated, but not the PMA-stimulated, rapid (3 min) C-14-AA release was associated with an increased influx of extracellular calcium. Stimulation of the cells with PMA resulted in phosphorylation of a cellular protein of about 32 kDa, whereas no phosphorylation of this protein was detected after stimulation with hydrogen peroxide. Taken together, these findings indicate that (i) both PMA and hydrogen peroxide may stimulate phospholipase A2-mediated AA release from human intestinal epithelial cells; (ii) this stimulation is brought about via protein kinase C and calmodulin-mediated events; (iii) PMA-stimulated C-14-AA release is associated with phosphorylation of a 32-kDa protein, possibly lipocortin, whereas the hydrogen peroxide-stimulated release is not; and (iv) calmodulin is more important for the hydrogen peroxide-stimulated C-14-AA release than is protein kinase C. The possibility that hydrogen peroxide-evoked AA release may contribute to the mucosal abnormality in Crohn's disease is discussed. 

  • 11.
    Gustafson-Svärd, Christina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Sjödahl, R
    Lilja, I
    Tagesson, C
    Cytosolic phospholipase A2 and cyclooxygenase-2 mediate release and metabolism of arachidonic acid in tumor necrosis factor-α-primed cultured intestinal epithelial cells (INT 407)1995In: Scand J Gastroenterol, Vol. 30, p. 1000-1007Article in journal (Refereed)
  • 12.
    Gustafson-Svärd, Christina
    et al.
    Clinical Research Center, Linköping University .
    Sjödahl, R
    Tagesson, C
    Phospholipase activation and arachidonic acid release in intestinal epithelial cells from patients with Crohn´s disease1990In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 25, no 11, p. 1151-1160Article in journal (Refereed)
    Abstract [en]

    A method for studying the mobilization of free arachidonic acid (AA) in viable isolated human intestinal epithelial cells has been developed and applied to the study of patients with Crohn's disease. Cells were isolated from morphologically unaffected parts of the distal ileum and incubated with 14C-AA; most of the incorporated 14C-AA was then found in phospholipids (mainly phosphatidylcholine) and in a pool of neutral lipids (mainly triacylglycerols). Cells from patients with Crohn's disease incorporated more 14C-AA into their neutral lipids than did cells from control patients. When the labeled cells were stimulated with phospholipase C from Clos-tridium perfringens or with the calcium ionophore A23187, they released significant amounts of AA, mainly from phosphatidylcholine. There was no difference between cells from Crohn patients and controls in the 14C-AA amounts released, but unstimu-lated and phospholipase C-stimulated cells from prednisolone-treated Crohn patients released less AA than cells from control patients. The A23187-stimuiated AA release was completely inhibited by the phospholipase A2 inhibitor 4-bromophenacyl bromide, whereas the phospholipase C-stimulated release was not. These findings suggest that AA release in human small-intestinal epithelial cells may be caused by calcium-mediated phospholipase A2 activation or by products of microbial phospholipase C activity and that prednisolone reduces the mobilization of free AA in intestinal epithelial cells. They also illustrate the potential use of isolated epithelial cells for revealing mechanisms underlying AA release in the intestinal mucosa in different disease states. 

  • 13.
    Gustafson-Svärd, Christina
    et al.
    Clinical Research Center and Depts. of Occupational Medicine and Clinical Chemistry, Linköping University.
    Tagesson, C
    Phospholipase activation and arachidonic acid release in cultured intestinal epithelial cells (INT 407)1989In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 24, no 4, p. 475-484Article in journal (Refereed)
    Abstract [en]

    The release of free arachidonic acid (AA) in cultured intestinal epithelial cells (INT 407) was investigated. INT-407 cells were first incubated overnight with radio-labeled 14C-AA, and most of the incorporated 14C-AA esterified into phos-phatidylethanolamine, phosphatidylcholine, and phosphatidylinositol. Labeled cells were then exposed to different stimulating agents and the release of free 14C-AA determined. The calcium ionophore A23187 caused a dose-dependent AA release that was preceded by a rapid uptake and a subsequent efflux of 45Ca2+. By contrast, phospholipase C from Clostridium perfringens caused a great AA release that was accompanied by an apparent uptake and a sustained intracellular accumulation of 45Ca2+. The cells also released AA when exposed to the protein kinase C activator, 4β-phorbol-12-myristate-13-acetate (PMA), and this agent, like the diacylglycerol l-oleoyl-2-acetyl-rac-glycerol, significantly potentiated the AA release caused by A23187. Not only A23187-mediated but also phospholipase C- and PMA-mediated AA release was inhibited by 4-bromophenacyl bromide, a known phospholipase A2 inhibitor. These findings, taken together, indicate that AA release in intestinal epithelial cells can be caused by (i) Ca2+-mediated phospholipase activation, (ii) products of phospholipase C activity, and (iii) stimulation of protein kinase C. It is suggested, therefore, that AA release in intestinal epithelial cells is governed by intracellular Ca2+, protein kinase C-mediated protein phosphorylation, and activation of phospholipase A2. 

  • 14.
    Gustafson-Svärd, Christina
    et al.
    Clinical Research Center, Linköping University .
    Tagesson, C
    Phospholipase C from Clostridium perfringens stimulates phospholipase A2-mediated arachidonic acid release in cultured intestinal epithelial cells (INT 407)1990In: Scandinavian Journal of Gastroenterology, ISSN 0036-5521, E-ISSN 1502-7708, Vol. 25, no 4, p. 363-371Article in journal (Refereed)
    Abstract [en]

    The mechanisms by which phospholipase C from Clostridium perfringens stimulates release of arachidonic acid (AA) in cultured intestinal epithelial cells (INT-407) were investigated. INT-407 cells were first allowed to incorporate 14C-labeled AA into their phospholipids; the labeled cells were then exposed to phospholipase C, and the release of free l4C-AA was determined. Phospholipase C caused a rapid (3 min) intracellular rise of free l4C-AA, followed by a considerable, dose- and time-dependent release of l4C-AA into the extracellular medium. For comparison, the calcium ionophore A23187 also caused a rapid mobilization of free 14C-AA, but a much lower extracellular 14C-AA release than phospholipase C during longer (1 h) incubation. The 14C-AA release was accompanied by a degradation of l4C-myo-inositol-labeled phosphatidylinositols and was reduced by the protein kinase C inhibitor l-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7). Both phospholipase C- and A23187-stimulated 14C-AA release was associated with degradation of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol and was reduced by nor-dihydroguaiaretic acid and 4-bromophenacyl bromide, two known phospholipase A2 inhibitors. In addition, the 14C-AA release was reduced by the calmodulin inhibitors trifluoperazine, compound 48/80, and A'-(6-aminohexyl)-5-chloro-l-naphthalene-sulfonamide (W-7). These findings indicate that phospholipase C from C. perfringens stimulates phospholipase A2-mediated AA release from human intestinal epithelial cells and suggest that this stimulation is brought about via processes involving phosphatidylinositol breakdown and activation of calmodulin and protein kinase C. It is possible that this phospholipase C-evoked AA release may contribute to the mucosal pathologic condition in diseases with altered intestinal microbial flora. 

  • 15.
    Gustafson-Svärd, Christina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Tagesson, C
    Boll, R-M
    Kald, B
    Tumor necrosis factor -α potentiates phospholipase A2 -stimulated release and metabolism of arachidonic acid in cultured intestinal epithelial cells (INT 407)1993In: Scand J Gastroenterol, Vol. 28, p. 323-330Article in journal (Refereed)
  • 16.
    Gustafson-Svärd, Christina
    et al.
    LINKOPING UNIV, DEPT CLIN CHEM, S-58183 LINKOPING, SWEDEN.
    Tagesson, Christer
    LINKOPING UNIV, CLIN RES CTR, S-58183 LINKOPING, SWEDEN .
    Influence of organic solvent mixtures on biological membranes - A simple experimental model1985In: British journal of industrial medicine, ISSN 0007-1072, Vol. 42, no 9, p. 591-595Article in journal (Refereed)
    Abstract [en]

    A simple experimental model was used to study the influence of organic solvents and solvent mixtures on the integrity of biological membranes. Radiolabelled membranes were prepared biosynthetically by growing Escherichia coli in the presence of 14C-oleic acid; the bulk of the radioactivity was incorporated into 14C-phosphatidylethanolamine, the predominant phospholipid species in E coli membranes. The radiolabelled bacteria were incubated at 37 degrees C in the presence of solvent, and the mixture filtrated through a Millipore 0.45 micron filter. This filtration retained radiolabel associated with the bacteria, and only radiolabel released as a result of solvent action was allowed through the filter. The radioactivity in the filtrate was then counted and expressed as a percentage of the total radioactivity. Results showed that aliphatic alcohols released membrane constituents in relation to their hydrocarbon chain length (1-propanol greater than 2-propanol greater than ethanol greater than methanol); the effects of aliphatic alcohols were potentiated by acetone, ethyl methyl ketone, ethylene glycol, and N,N'-dimethylformamide, and the effects of ethanol were potentiated by 1-butanol, benzyl alcohol, and ethylacetate. These findings point to the possibility that certain mixtures of organic solvents are more damaging to membranes than the components of the mixture would indicate, and suggest that the experimental model used might help in showing mixtures that are particularly harmful. 

  • 17.
    Gustafson-Svärd, Christina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Åkesson Nilsson, G
    Mattsson, M
    Sundin, P
    Wesén, C
    Removal of xenobiotic dichlorostearic acid from phospholipids and neutral lipids in cultured human cell lines by ß-oxidation and secretion of dichloromyristic acid2001In: Pharmacol & Toxicol, Vol. 89, p. 56-64Article in journal (Refereed)
  • 18. Kald, B
    et al.
    Boll, R-M
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Sjödahl, R
    Tagesson, C
    Phospholipase C from Clostridium perfringens stimulates acetyltransferase-dependent formation of platelet-activating factor in cultured intestinal epithelial cells (INT 407)1994In: Scand J Gastroenterol, Vol. 29, p. 243-247Article in journal (Refereed)
  • 19. Kald, B
    et al.
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Weström, B
    Tagesson, C
    Platelet-activating factor (PAF-acether) formation in neonatal intestinal mucosa and in cultured intestinal epithelial cells1992In: Eur Surg Res, Vol. 24, p. 325-332Article in journal (Refereed)
  • 20. Lilja, I
    et al.
    Dimberg, J
    Sjödahl, R
    Tagesson, C
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Effects of endotoxin and dexamethasone on group I and II phospholipase A2 in rat ileum and stomach1994In: Gut, Vol. 35, p. 40-45Article in journal (Refereed)
  • 21. Lilja, I
    et al.
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Franzén, L
    Sjödahl, R
    Tumour necrosis factor-α in ileal mast cells in patients with Crohn´s disease2000In: Digestion, Vol. 61, p. 68-76Article in journal (Refereed)
  • 22. Lilja, I
    et al.
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Franzén, L
    Sjödahl, R
    Andersen, S
    Johansen, B
    Presence of group IIa secretory phospholipase A2 in mast cells and macrophages in normal human ileal submucosa and in Crohn´s disease2000In: Clin Chem Lab Med, Vol. 38, p. 1231-1236Article in journal (Refereed)
  • 23. Lilja, I
    et al.
    Olaison, G
    Sjödahl, R
    Smedh, K
    Tagesson, C
    Gustafson-Svärd, Christina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn´s ileitis1995In: Gut, Vol. 37, p. 380-385Article in journal (Refereed)
1 - 23 of 23
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf