Respiration, oxidative phosphorylation, and uncoupling protein in Candida albicans

dc.creatorCavalheiro, R.A.
dc.creatorFortes, F.
dc.creatorBorecký, J.
dc.creatorFaustinoni, V.C.
dc.creatorSchreiber, A.Z.
dc.date2004-10-01
dc.date2014-07-17T15:05:06Z
dc.date2015-11-26T11:25:39Z
dc.date2014-07-17T15:05:06Z
dc.date2015-11-26T11:25:39Z
dc.date.accessioned2018-03-28T20:39:36Z
dc.date.available2018-03-28T20:39:36Z
dc.identifierBrazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 37, n. 10, p. 1455-1461, 2004.
dc.identifier0100-879X
dc.identifierS0100-879X2004001000003
dc.identifier10.1590/S0100-879X2004001000003
dc.identifierhttp://dx.doi.org/10.1590/S0100-879X2004001000003
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004001000003
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/24234
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/24234
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1233394
dc.descriptionThe respiration, membrane potential (Dy), and oxidative phosphorylation of mitochondria in situ were determined in spheroplasts obtained from Candida albicans control strain ATCC 90028 by lyticase treatment. Mitochondria in situ were able to phosphorylate externally added ADP (200 µM) in the presence of 0.05% BSA. Mitochondria in situ generated and sustained stable mitochondrial Dy respiring on 5 mM NAD-linked substrates, 5 mM succinate, or 100 µM N,N,N',N'-tetramethyl-p-phenylenediamine dihydrochloride plus 1 mM ascorbate. Rotenone (4 µM) inhibited respiration by 30% and 2 µM antimycin A or myxothiazole and 1 mM cyanide inhibited it by 85%. Cyanide-insensitive respiration was partially blocked by 2 mM benzohydroxamic acid, suggesting the presence of an alternative oxidase. Candida albicans mitochondria in situ presented a carboxyatractyloside-insensitive increase of Dy induced by 5 mM ATP and 0.5% BSA, and Dy decrease induced by 10 µM linoleic acid, both suggesting the existence of an uncoupling protein. The presence of this protein was subsequently confirmed by immunodetection and respiration experiments with isolated mitochondria. In conclusion, Candida albicans ATCC 90028 possesses an alternative electron transfer chain and alternative oxidase, both absent in animal cells. These pathways can be exceptional targets for the design of new chemotherapeutic agents. Blockage of these respiratory pathways together with inhibition of the uncoupling protein (another potential target for drug design) could lead to increased production of reactive oxygen species, dysfunction of Candida mitochondria, and possibly to oxidative cell death.
dc.description1455
dc.description1461
dc.languageen
dc.publisherAssociação Brasileira de Divulgação Científica
dc.relationBrazilian Journal of Medical and Biological Research
dc.rightsaberto
dc.sourceSciELO
dc.subjectCandida albicans spheroplasts
dc.subjectMitochondria
dc.subjectRespiratory chain
dc.subjectMitochondrial membrane potential
dc.subjectUncoupling protein
dc.titleRespiration, oxidative phosphorylation, and uncoupling protein in Candida albicans
dc.typeArtículos de revistas


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