Souheil El-Chemaly

Publications (2)16.2 Total impact

• Article: Lactoperoxidase and human airway host defense.

  Corinne Wijkstrom-Frei, Souheil El-Chemaly, Radia Ali-Rachedi, Cynthia Gerson, Miguel A Cobas, Rosanna Forteza, Matthias Salathe, Gregory E Conner
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  ABSTRACT: The lactoperoxidase (LPO) antibiotic system is a well-characterized component of mammary and salivary gland secretions. Because LPO has been shown to function in ovine airways, human airway tissue and secretions were examined for the presence of LPO and its substrate, the anion thiocyanate (SCN-). In addition, human airway secretions were tested for LPO-mediated antibacterial activity, and LPO's activity was assessed against some human airway pathogens. The data showed that normal human airway secretions contained LPO enzyme activity (0.65 +/- 0.09 microg/mg secreted protein; n = 17), and Western blots of secretions demonstrated bands of the expected sizes for LPO. LPO mRNA was detected in trachea by sequencing PCR-amplified cDNA. SCN-, LPO's substrate, was present in undiluted airway secretions at concentrations sufficient for LPO catalysis (0.46 +/- 0.19 mM; n = 8), and diluted secretions contained antibacterial activity with LPO-like properties. Immunocytochemistry localized LPO to submucosal glands in human bronchi. Finally, as expected based on the known antibacterial spectrum of the LPO system, airway secretions showed LPO-dependent activity against Pseudomonas aeruginosa. In addition, the airway LPO system was shown to be effective against Burkholderia cepacia and Haemophilus influenzae. Thus, a functional LPO system exists in human airways and may contribute to airway host defense against infection.
  American Journal of Respiratory Cell and Molecular Biology 09/2003; 29(2):206-12. · 5.13 Impact Factor
• Article: Hydrogen peroxide-scavenging properties of normal human airway secretions.

  Souheil El-Chemaly, Matthias Salathe, Sylvia Baier, Gregory E Conner, Rosanna Forteza
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  ABSTRACT: To examine the antioxidant capacity of normal human airway secretions and to characterize its molecular components, tracheal lavages were obtained from eight patients intubated for elective surgery and free of lung disease. These samples (20 microl, approximately 6.8 microg of protein) scavenged 0.57 +/- 0.09 nmol of added 0.96 nmol hydrogen peroxide (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. Fourfold diluted secretions showed only nonenzymatic scavenging activity, but the addition of thiocyanate to these samples (0.4 mM; substrate for lactoperoxidase) restored their ability to scavenge H2O2. The addition of reduced glutathione (8 microM) only enhanced nonenzymatic scavenging activity. These data provide evidence that multiple enzymatic and nonenzymatic systems coexist in human airway secretions that contribute to H2O2 scavenging. It appears, however, that H2O2 is mainly consumed by the lactoperoxidase system.
  American Journal of Respiratory and Critical Care Medicine 03/2003; 167(3):425-30. · 11.08 Impact Factor