PMID- 14592541
OWN - NLM
STAT- MEDLINE
DCOM- 20040712
LR  - 20191210
IS  - 1357-2725 (Print)
IS  - 1357-2725 (Linking)
VI  - 36
IP  - 1
DP  - 2004 Jan
TI  - In situ evidence of an alternative oxidase and an uncoupling protein in the 
      respiratory chain of Aspergillus fumigatus.
PG  - 162-72
AB  - Aspergillus fumigatus is an unusual pathogen in immunocompetent individuals; its 
      incidence has increased in the last decades in patients immunocompromised, like 
      those with chronic granulomatosis disease and AIDS. The aim of this study was to 
      identify differences between the respiratory chain of host and the fungus 
      planning to use the later as a pharmacological target. We evaluated respiration, 
      membrane potential and oxidative phosphorylation of mitochondria of the 
      spheroplasts of A. fumigatus in situ, after permeabilization with digitonin. 
      Firstly, a functional respiratory chain (complex I-V) was demonstrated: adenosine 
      5'-diphosphate (ADP) induced an oligomycin-sensitive transition from resting to 
      phophorylating respiration in the presence of the oxidizable substrates malate, 
      glutamate, alpha-ketoglutarate, pyruvate, dihydroorotate, succinate, 
      N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD) and exogenous NADH. In addition, 
      the ability of the fungus to oxidize exogenous NADH, as well as the insensitivity 
      of its respiration to rotenone, in association with the sensitivity to flavone, 
      indicate the presence of an alternative NADH-ubiquinone oxidoreductase; the 
      partial sensitivity of respiration to antimycin A and cyanide, in association 
      with the sensitivity to benzohydroxamic acid, indicates the presence of an 
      alternative oxidase. The fatty acid-uncoupled respiration was partly reversed by 
      bovine serum albumin (BSA) and guanosine 5'-triphosphate (GTP) and was 
      insensitive to either carboxyatractyloside or ADP. These results, together with 
      evidences obtained using antibodies raised against uncoupling protein (UCP) from 
      potato, indicate in addition, the presence of an uncoupling protein in the 
      respiratory chain of A. fumigatus.
FAU - Tudella, Valeria G
AU  - Tudella VG
AD  - Departament of Clinical, Toxicological and Bromatological Analysis, Faculty of 
      Pharmaceutical Sciences, University of Sao Paulo, Ribeirao Preto 14040-903, SP, 
      Brazil.
FAU - Curti, Carlos
AU  - Curti C
FAU - Soriani, Frederico M
AU  - Soriani FM
FAU - Santos, Antonio C
AU  - Santos AC
FAU - Uyemura, Sergio A
AU  - Uyemura SA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Int J Biochem Cell Biol
JT  - The international journal of biochemistry & cell biology
JID - 9508482
RN  - 0 (Antifungal Agents)
RN  - 0 (Cyanides)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Flavonoids)
RN  - 0 (Hydroxamic Acids)
RN  - 0 (Indicators and Reagents)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Uncoupling Agents)
RN  - 61D2G4IYVH (Adenosine Diphosphate)
RN  - 642-15-9 (Antimycin A)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.- (alternative oxidase)
RN  - EC 7.1.1.2 (Electron Transport Complex I)
RN  - K8YW73872D (benzohydroxamic acid)
RN  - KOO5CM684H (Digitonin)
SB  - IM
MH  - Adenosine Diphosphate/metabolism
MH  - Antifungal Agents/pharmacology
MH  - Antimycin A/pharmacology
MH  - Aspergillus fumigatus/drug effects/*enzymology/*metabolism
MH  - Cyanides/pharmacology
MH  - Digitonin/pharmacology
MH  - Electron Transport Complex I/*metabolism
MH  - Enzyme Inhibitors/pharmacology
MH  - Flavonoids/pharmacology
MH  - Hydroxamic Acids/pharmacology
MH  - Indicators and Reagents/pharmacology
MH  - Intracellular Membranes/metabolism
MH  - Membrane Potentials
MH  - Mitochondria/drug effects/enzymology
MH  - Mitochondrial Proteins
MH  - Oxidative Phosphorylation/*drug effects
MH  - Oxidoreductases/*metabolism
MH  - Oxygen Consumption/drug effects
MH  - Permeability/drug effects
MH  - Plant Proteins
MH  - Uncoupling Agents/pharmacology
EDAT- 2003/11/01 05:00
MHDA- 2004/07/13 05:00
CRDT- 2003/11/01 05:00
PHST- 2003/11/01 05:00 [pubmed]
PHST- 2004/07/13 05:00 [medline]
PHST- 2003/11/01 05:00 [entrez]
AID - S1357272503001948 [pii]
AID - 10.1016/s1357-2725(03)00194-8 [doi]
PST - ppublish
SO  - Int J Biochem Cell Biol. 2004 Jan;36(1):162-72. doi: 
      10.1016/s1357-2725(03)00194-8.