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Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier
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SYSNO ASEP 0142202 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier Author(s) Engstová, Hana (FGU-C) RID, ORCID
Žáčková, Markéta (FGU-C)
Růžička, Michal (FGU-C)
Meinhardt, A. (DE)
Hanuš, Jan (UEB-Q)
Krämer, R. (DE)
Ježek, Petr (FGU-C) RID, ORCIDSource Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 276, č. 7 (2001), s. 4683-4691Number of pages 9 s. Language eng - English Country US - United States Keywords phosphate transport ; fatty acids Subject RIV CE - Biochemistry R&D Projects GA301/95/0620 GA ČR - Czech Science Foundation (CSF) GA301/98/0568 GA ČR - Czech Science Foundation (CSF) ME 085 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ME 389 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z5011922 - FGU-C Annotation 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. Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2002
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