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Trp‐Lys‐Tyr‐Met‐Val‐D‐Met stimulates superoxide generation and killing of Staphylococcus aureus via phospholipase D activation in human monocytes
Author(s) -
Bae YoeSik,
Ju SeongA,
Kim Ji Yung,
Seo Jeong Kon,
Baek Suk Hwan,
Kwak JongYoung,
Kim Byung Sam,
Suh PannGhill,
Ryu Sung Ho
Publication year - 1999
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.65.2.241
Subject(s) - biology , staphylococcus aureus , superoxide , microbiology and biotechnology , phospholipase , phospholipase a , immunology , biochemistry , enzyme , phospholipase a2 , bacteria , genetics
Among the phagocytic leukocytes, monocytes have the important role of clearing out parasitic microorganisms. They accomplish this through production of toxic metabolites of oxygen. Trp‐Lys‐Tyr‐Met‐Val‐D‐Met (WKYMVm), a peptide that stimulates phosphoinositide (PI) hydrolysis in human leukocytes, including monocytes, binds to a unique cell surface receptor and stimulates superoxide generation, killing of Staphylococcus aureus , and activation of phospholipase D (PLD) in human monocytes. Preincubation of the cells with a PI‐specific phospholipase C (PLC) inhibitor (U‐73122), protein kinase C inhibitor (GF109203X), or intracellular Ca 2+ chelator (BAPTA/AM) before the peptide stimulus totally inhibits the peptide‐induced PLD activation and superoxide generation. On the other hand, tyrosine kinase inhibitor genistein only partially inhibits the peptide‐induced processes. The peptide‐induced bacteria killing activity shares regulatory mechanisms for PLD activation with the superoxide generation, which is inhibited in the presence of 1‐butanol. We suggest that the peptide stimulates PLD downstream of PLC activation and PLD activation in turn is essential for the peptide‐induced immunological functions such as the superoxide generation and killing of bacteria by human monocytes. J. Leukoc. Biol. 65:241–248; 1999.