PMID- 19412660
OWN - NLM
STAT- MEDLINE
DCOM- 20100618
LR  - 20240209
IS  - 1466-1268 (Electronic)
IS  - 1355-8145 (Print)
IS  - 1355-8145 (Linking)
VI  - 14
IP  - 6
DP  - 2009 Nov
TI  - Activation of Hsp90/NOS and increased NO generation does not impair mitochondrial 
      respiratory chain by competitive binding at cytochrome c oxidase in low oxygen 
      concentrations.
PG  - 611-27
LID - 10.1007/s12192-009-0114-0 [doi]
AB  - Nitric oxide (NO) is known to regulate mitochondrial respiration, especially 
      during metabolic stress and disease, by nitrosation of the mitochondrial electron 
      transport chain (ETC) complexes (irreversible) and by a competitive binding at O2 
      binding site of cytochrome c oxidase (CcO) in complex IV (reversible). In this 
      study, by using bovine aortic endothelial cells, we demonstrate that the 
      inhibitory effect of endogenously generated NO by nitric oxide synthase (NOS) 
      activation, by either NOS stimulators or association with heat shock protein 90 
      (Hsp90), is significant only at high prevailing pO2 through nitrosation of 
      mitochondrial ETC complexes, but it does not inhibit the respiration by 
      competitive binding at CcO at very low pO2. ETC complexes activity measurements 
      confirmed that significant reduction in complex IV activity was noticed at higher 
      pO2, but it was unaffected at low pO2 in these cells. This was further extended 
      to heat-shocked cells, where NOS was activated by the induction/activation of 
      (Hsp90) through heat shock at an elevated temperature of 42 degrees C. From these 
      results, we conclude that the entire attenuation of respiration by endogenous NO 
      is due to irreversible inhibition by nitrosation of ETC complexes but not through 
      reversible inhibition by competing with O2 binding at CcO at complex IV.
FAU - Presley, Tennille
AU  - Presley T
AD  - The Center for Biomedical EPR Spectroscopy and Imaging, Biophysics Program, Davis 
      Heart and Lung Research Institute, The Ohio State University, Columbus, OH, USA.
FAU - Vedam, Kaushik
AU  - Vedam K
FAU - Liu, Xiaoping
AU  - Liu X
FAU - Zweier, Jay L
AU  - Zweier JL
FAU - Ilangovan, Govindasamy
AU  - Ilangovan G
LA  - eng
GR  - R01-HL-078796/HL/NHLBI NIH HHS/United States
GR  - R01 HL078796/HL/NHLBI NIH HHS/United States
GR  - F31 GM078772/GM/NIGMS NIH HHS/United States
GR  - R21 EB004658/EB/NIBIB NIH HHS/United States
GR  - F31 GM078772-01/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20090502
PL  - Netherlands
TA  - Cell Stress Chaperones
JT  - Cell stress & chaperones
JID - 9610925
RN  - 0 (HSP90 Heat-Shock Proteins)
RN  - 0 (Nitrates)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - EC 1.14.13.39 (Nitric Oxide Synthase)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Animals
MH  - Aorta
MH  - Binding, Competitive
MH  - Cattle
MH  - Cell Respiration/*physiology
MH  - Electron Transport Complex IV/*metabolism
MH  - Endothelial Cells/*metabolism
MH  - HSP90 Heat-Shock Proteins/*metabolism
MH  - Heat-Shock Response/physiology
MH  - Mitochondria/*metabolism
MH  - *Nitrates
MH  - Nitric Oxide/*metabolism
MH  - Nitric Oxide Synthase/metabolism
MH  - Nitrosation
MH  - Oxygen/*metabolism
PMC - PMC2866951
EDAT- 2009/05/05 09:00
MHDA- 2010/06/19 06:00
PMCR- 2010/05/01
CRDT- 2009/05/05 09:00
PHST- 2009/03/05 00:00 [received]
PHST- 2009/04/02 00:00 [accepted]
PHST- 2009/05/05 09:00 [entrez]
PHST- 2009/05/05 09:00 [pubmed]
PHST- 2010/06/19 06:00 [medline]
PHST- 2010/05/01 00:00 [pmc-release]
AID - S1355-8145(23)01791-1 [pii]
AID - 114 [pii]
AID - 10.1007/s12192-009-0114-0 [doi]
PST - ppublish
SO  - Cell Stress Chaperones. 2009 Nov;14(6):611-27. doi: 10.1007/s12192-009-0114-0. 
      Epub 2009 May 2.