Cristin-resultat-ID: 1662890
Sist endret: 19. februar 2019, 11:44
NVI-rapporteringsår: 2018
Resultat
Vitenskapelig artikkel
2019

Di-n-butyl phthalate modifies PMA-induced macrophage differentiation of THP-1 monocytes via PPARγ

Bidragsytere:
  • Vegard Sæter Grytting
  • Bergitte Olderbø
  • Jørn Andreas Holme
  • Jan Tore Samuelsen
  • Anita Solhaug
  • Rune Becher
  • mfl.

Tidsskrift

Toxicology in Vitro
ISSN 0887-2333
e-ISSN 1879-3177
NVI-nivå 1

Om resultatet

Vitenskapelig artikkel
Publiseringsår: 2019
Publisert online: 2018
Trykket: 2019
Volum: 54
Sider: 168 - 177

Importkilder

Scopus-ID: 2-s2.0-85054156552

Beskrivelse Beskrivelse

Tittel

Di-n-butyl phthalate modifies PMA-induced macrophage differentiation of THP-1 monocytes via PPARγ

Sammendrag

The present study examined the effects of di-n-butyl phthalate (DBP) on phorbol myristate acetate (PMA)-induced macrophage differentiation of THP-1 monocytes, determined by morphological classification and flow cytometry. Focusing on the expression of the surface marker CD36, the potential role of peroxisome proliferator-activated receptor gamma (PPARγ) was examined using various PPARγ agonists and antagonists. As the PPARγ ligand-binding domain contains multiple ligand-binding sites (LBS), agonist and antagonists targeting the different sites were used. DBP accelerated PMA-induced morphological changes and increased expression of CD36, although to a lesser degree than the PPARγ agonists rosiglitazone and 15-deoxy-Δ12,14-prostaglandin J2 (15d-PGJ2). A proteomics screening revealed that DBP enhanced the expression of PPARγ-regulated proteins. During combined exposures, DBP partly attenuated the effect of rosiglitazone, an agonist binding reversibly to PPARγ's canonical LBS. In contrast, DBP increased expression of CD36 in combination with 15d-PGJ2 which binds irreversibly to the canonical LBS. Thus, DBP appears to interact with both the canonical and alternative LBS. Accordingly, the antagonist GW9662, which binds to the canonical LBS, only partly reduced the DBP-induced CD36 expression, while the dual-site antagonist SR16832 completely blocked the effects of DBP. Overall, the results show that DBP modifies PMA-induced differentiation of THP-1 cells through interaction with PPARγ.

Bidragsytere

Vegard Sæter Grytting

  • Tilknyttet:
    Forfatter
    ved Smittevern ved Folkehelseinstituttet

Bergitte Pearl Olderbø

Bidragsyterens navn vises på dette resultatet som Bergitte Olderbø
  • Tilknyttet:
    Forfatter
    ved NIOM - Nordisk Institutt for Odontologiske Materialer

Jørn Andreas Holme

  • Tilknyttet:
    Forfatter
    ved Smittevern ved Folkehelseinstituttet

Jan Tore Samuelsen

  • Tilknyttet:
    Forfatter
    ved NIOM - Nordisk Institutt for Odontologiske Materialer

Anita Solhaug

  • Tilknyttet:
    Forfatter
    ved Forskningsgruppe toksinologi ved Veterinærinstituttet
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