Počet záznamů: 1  

Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier

  1. 1. 0142202 - FGU-C 20010257 RIV US eng J - Článek v odborném periodiku
    Engstová, Hana - Žáčková, Markéta - Růžička, Michal - Meinhardt, A. - Hanuš, Jan - Krämer, R. - Ježek, Petr
    Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier.
    Journal of Biological Chemistry. Roč. 276, č. 7 (2001), s. 4683-4691 ISSN 0021-9258
    Grant CEP: GA ČR GA301/95/0620; GA ČR GA301/98/0568; GA MŠk ME 085; GA MŠk ME 389
    Grant ostatní:US(US) Czechoslovak Science and Technology Program 94043
    Výzkumný záměr: CEZ:AV0Z5011922
    Klíčová slova: phosphate transport * fatty acids
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 7.258, rok: 2001

    The electroneutral Pi uptake via the phosphate carrier (PIC) in rat liver and heart mitochondria is inhibited by fatty acids (FAs), by 12-(4-azido-2-nitrophenylamino) dodecanoic (AzDA), heptylbenzoic (M doses); by lauric, palmitic or 12-azidododecanoic acids (0.1 mM doses). In turn, reconstituted E.coli- expressed yeast PIC mediated anionic FA uniport with a similar pattern leading to FA cycling and H+ uniport. Kinetics of Pi/Pi exchange on recombinant PIC in the presence of AzDA better corresponded to a competive inhibition mechanism. Methanephosphonate was identified as a new PIC substrate. Decanephosphonate, butane-phosphonate, 4-nitrophenylphosphate and other Pi analogs were not translocated and did not inhibit Pi transport. However, methylenediphosphonate and iminodi(methylenephosphonate) inhibited both electroneutral Pi uptake and FA cycling via PIC. AzDA analog, 16-(4-azido-2-nitrophenylamino)-[3H4]-hexadecanoic acid (3H-AzHA) bound upon photoactivation to several mitochondrial proteins, including the 30 and 34 kD bands. The latter was ascribed to PIC due to its specific elution pattern on Blue Sepharose and Affi-Gel. 3H-AzHA photolabeling of recombinant PIC was prevented by methanephosphonate, diphosphonates and after premodification with 4-azido-2-nitrophenylphosphate. Hence, the demonstrated PIC interaction with monovalent long-chain FA anions, but with divalent phosphonates of short chain only, indicates a pattern distinct from that valid for the mitochondrial uncoupling protein-1.
    Trvalý link: http://hdl.handle.net/11104/0039909