Published ahead of print on November 15, 2002, doi:10.1164/rccm.200206-531OC
Am. J. Respir. Crit. Care Med., Volume 167, Number 3, February 2003, 425-430
A more recent version of this article appeared on February 1, 2003
Submitted on June 9, 2002
Accepted on November 8, 2002
Hydrogen Peroxide Scavenging Properties of Normal Human Airway Secretions
Souheil El-Chemaly1, Matthias Salathe1, Sylvia Baier2, Gregory E Conner3, and Rosanna M Forteza1*
1 Medicine/Pulmonary, University of Miami, Miami, FL, USA,
2 Anesthesiology, University of Miami, Miami, FL, USA,
3 Cell Biology and Anatomy, University of Miami, Miami, FL, USA; Medicine/Pulmonary, University of Miami, Miami, FL, USA
* To whom correspondence should be addressed. E-mail: rforteza{at}miami.edu.
To examine the antioxidant capacity of normal human airway secretions and to characterize its molecular components, tracheal lavages were obtained from 8 patients intubated for elective surgery and free of lung disease. These samples (20 µ]l, ~ 6.8 µg of protein) scavenged 0.57 ± 0.09 nmoles of added 0.96 nmoles H2O2 within 10 minutes at room temperature (n = 8). The scavenging activity was inhibited 60 ± 4% by azide (an inhibitor of heme-containing peroxidases and catalase) and 42 ± 9% by dapsone (an inhibitor of lactoperoxidase). Mercaptosuccinic acid (an inhibitor of glutathione peroxidase) did not significantly inhibit H2O2 scavenging by these secretions. Four-fold diluted secretions showed only non-enzymatic scavenging activity, but addition of thiocyanate to these samples (0.4 mM; substrate for lactoperoxidase) restored their ability to scavenge H2O2. Addition of reduced glutathione (8 µM) only enhanced non-enzymatic scavenging activity. These data provide evidence that multiple enzymatic and non-enzymatic systems coexist in human airway secretions that contribute to H2O2 scavenging. It appears, however, that H2O2 is mainly consumed by the lactoperoxidase system.
Key words: hydrogen peroxide
lactoperoxidase
glutathione peroxidase
oxidants
anti-oxidants
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