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Tytuł oryginału: Interleukin 1á induces functional prostaglandin E synthase in cultured human umbilical vein endothelial cells.
Autorzy: Uracz W[ojciech], Uracz D[anuta], Olszanecki R[afał], Gryglewski R. J.
Źródło: J. Physiol. Pharmacol. 2002: 53 (4 p. 1) s.643-654, il., bibliogr. 52 poz.
Sygnatura GBL: 302,092

Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • in vitro

    Streszczenie angielskie: Prostaglandin endoperoxide H2 (PGH2) is generated from arachidonic acid by either consitutive (COX)-1) or inducible (COX-2) cyclooxygenases. In arterial wall PGH2 is converted by PGI2 synthase (PGI-S) to prostacyclin (PGI2), and in plateles by thromboxane synthase (TX-S) to thromboxane (TXA2). Other prostanoids as PGD2, PGF2ŕ or PGE2 were belived to arise non-enzymatically from PGH2. Only recently , human prostaglandin E synthase (PGE-S) has been identified and cloned as a membrane bound, microsomal, glutathione-dependent inducible enzyme. Here we demonstrated that interleukin 1 á (IL-1á) is an inducer of COX-2 and PGE-S in human umbilical vein endothelial cells (HUVEC). Functional expression of PGE-S was measured at the level of specific mRNA by semi-quantitative RT-PCR, PGE-S protein was detected by Western blot in HUVEC, while PGE2 was measured by immunoassay in the supernatant. Actinomycin D, a classical transcription inhibitor, was used to prove that indeed IL-1á induced the functional PGE-S enzyme. PGE2 generation in HUVEC was inhibited by indomethacin, acetamoniphen and dexamethasone. In conclusion, we found that in cultured endothelial cells IL-1á induced as evidenced by the appearance of its transcript and its functional enzyme. The induction of endothelial PGE-S and COX-2 appeared to be and their transcripts were induced as fast as one might expect from immediate early genes. It means that IL-1á-triggered-PGE2 biosynthesis in endothelial cells is probably regulated by induction of both COX-2 and ...

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