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Tytuł oryginału: Functional reconstitution of Ral-binding GTPase activating protein, RLIP76, in proteoliposomes catalyzing ATP-dependent transport of glutathione conjugate of 4-hydroxynonenal.
Autorzy: Sharma Rajendra, Sharma Abha, Yang Yusong, Awasthi Sanjay, Singhal Sharad S., Zimniak Piotr, Awasthi Yogesh C.
Źródło: Acta Bioch. Pol. 2002: 49 (3) s.693-701, il., bibliogr. s. 700-701
Sygnatura GBL: 303,116

Hasła klasyfikacyjne GBL:
  • mikrobiologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Streszczenie angielskie: Earlier studies from our laboratories have shown that RLIP76, a previously described Ral-binding GTpase activating protein (Jullien-Flores et al., 1995, J. Biol. Chem. 270: 22473), is identical with the xenobiotic transporter DNP-SG ATPase, adn can catalyze ATP-dependent transport of glutathione-conjugates as well as doxorubin (Awasthi et al., 2000, Biochemistry, 39: 9327). We have now reconstituted purified bacterially expressed RLIP76 in proteoliposomes, and have studied ATP-dependent uptake of the glutathione conjugate of 4-hydroxynonenal (GS-HNE) by these vesicles. Results of these studies show that RLIP76 reconstituted in proteoliposomes catalyzes ATP-dependent transport of GS-HNE against a concentration gradient. The transport of GS-HNE is saturable with respect to ATP as well as GS-HNE with Km values of 1.4 mM and 2.5 ćM, respectively. These studies demonstrate that RLIP76 mediates active transport of GS-HNE, adn are consistent with our previous work showing that RLIP76-mediated efflux of GS-HNE regulates the intracellular concentration of 4-HNE and thereby affects 4-HNE mediated signaling.

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    Tytuł oryginału: Transport functions and physiological significance of 76 kDa Ral-binding GTPase activating protein (RLIP76).
    Autorzy: Awasthi Sanjay, Sharma Rajendra, Yang Yusong, Singhal Sharad S., Pikula Sławomir, Bandorowicz-Pikula Joanna, Singh Shivendra V., Zimniak Piotr, Awasthi Yogesh C.
    Źródło: Acta Bioch. Pol. 2002: 49 (4) s.855-867, il., tab., bibliogr. s. 863-867
    Sygnatura GBL: 303,116

    Typ dokumentu:
  • tytuł obcojęzyczny

    Streszczenie angielskie: We have recently demonstrated that a previously known Ral-binding GTPase activating protein, RLIP76, can also catalyze ATP-dependent transport of various structurally unrelated xeno- and endobiotics irrespective of their net charge (Awasthi et al., 2000, Biochemistry, 39: 9327). RLIP76 is a non-ATP binding cassette (ABC) protien but it has two ATP-binding sites and shows basal ATPase activity which is stimulated in the presence of its transport substrates (allocrites) such as doxorubicin (DOX) and S-(2,4-dinitrophenyl) glutathione (DNP-SG). Proteoliposomes reconstituted with purified RLIP76 catalyze ATP-dependent, saturable transport of DOX, as well as of glutathione-conjugates including leukotrienes (LTC4) and the GSH-conjugate of 4-hydroxynonenal (GS-HNE). In erythrocytes the majority of transport activity for DOX, GS-HNE, and LTCA is a ccounted for by RLIP76. Cells exposed to mild oxidative stress show a rapid and transient induction of RLIP76 resulting in an increased efflux of GS-HNE and acquire resistance to oxidative stress mediated toxicity and apoptosis. Cells transfected with RLIP76 acquire resistance to DOX through increased efflux of the drug suggesting its possible role in the mechanisms of drug-resistance. In this article, we discuss the significance of transport functions of RLIP76 highlighting its role in the defense mechanisms against oxidative injury, and modulation of signaling mechanisms.

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