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Sökning: WFRF:(Thorsson B) > (2000-2004)

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1.
  • Sennström, Maria B., et al. (författare)
  • Human cervical ripening, an inflammatory process mediated by cytokines
  • 2000
  • Ingår i: Molecular Human Reproduction. - : Oxford University Press (OUP). - 1360-9947 .- 1460-2407. ; 6:4, s. 81-375
  • Tidskriftsartikel (refereegranskat)abstract
    • An extensive remodelling process, referred to as cervical ripening, takes place in the cervical tissue during pregnancy and labour. It is recognized as softening and dilation of the cervical canal, and starts as a slow process during pregnancy, becoming rapid close to partum. In this study we focus on cytokines as possible mediators of this final remodelling. mRNA levels for interleukin (IL)-8, IL-6 and granulocyte colony-stimulating factor (G-CSF) were upregulated in the ripe postpartum cervical tissue (n = 8) compared to the unripe state (n = 9). Likewise, released cytokine concentrations increased from non-pregnant (n = 11) to the term-pregnant group (n = 13) with a further increase at partum (n = 16). IL-8 concentrations increased 4-fold from non-pregnant to term-pregnant (P<0.01), and a further 10-fold to postpartum state (P<0.0001). Concentrations of IL-6 and G-CSF were similarly increased. Specific IL-8 immunostaining was identified in the epithelia of pregnant cervical tissue (n = 7) and was most pronounced in the epithelia and stroma of postpartum tissue (n = 4). In conclusion, IL-8, IL-6 and G-CSF increase in the human cervix during the ripening process, indicating their important role in the cervical remodelling. These data demonstrate that cervical ripening is similar to an inflammatory process.
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3.
  • Juhasz, P., et al. (författare)
  • ESI and MALDI LC/MS-MS approaches for large scale protein, identification and quantification : Are they equivalent?
  • 2002
  • Ingår i: ; , s. 55-56
  • Konferensbidrag (refereegranskat)abstract
    • An approach for large scale protein identification and quantification was described. The peptide mixtures from the strong cation exchange (SCX) fractionated protein digests were separated and analyzed by HPLC MS/MS. The human fibrobalst nuclei were purified from stimulated and non-stimulated cells. The quantification results with MALDI and ESI LC/MS were shown to be identical within experimental error.
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