Počet záznamů: 1

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

SYSNO ASEP	0142202
Druh ASEP	J - Článek v odborném periodiku
Zařazení RIV	J - Článek v odborném periodiku
Poddruh J	Ostatní články
Název	Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier
Tvůrce(i)	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, ORCID}
Zdroj.dok.	Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258 Roč. 276, č. 7 (2001), s. 4683-4691
Poč.str.	9 s.
Jazyk dok.	eng - angličtina
Země vyd.	US - Spojené státy americké
Klíč. slova	phosphate transport ; fatty acids
Vědní obor RIV	CE - Biochemie
CEP	GA301/95/0620 GA ČR - Grantová agentura ČR
	GA301/98/0568 GA ČR - Grantová agentura ČR
	ME 085 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
	ME 389 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
CEZ	AV0Z5011922 - FGU-C
Anotace	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.
Pracoviště	Fyziologický ústav
Kontakt	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Rok sběru	2002

Počet záznamů: 1