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Am J Physiol Lung Cell Mol Physiol 286: L921-L930, 2004; doi:10.1152/ajplung.00124.2003
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EDITORIAL FOCUS

Lipoteichoic acid-stimulated p42/p44 MAPK activation via Toll-like receptor 2 in tracheal smooth muscle cells

Chiang-Wen Lee,1 Chin-Sung Chien,1 and Chuen-Mao Yang1,2

1Department of Physiology and Pharmacology, 2Graduate Institute of Natural Products, College of Medicine, Chang Gung University, Kwei-San, Tao-Yuan, Taiwan, 3332

Submitted 28 April 2003 ; accepted in final form 24 September 2003

Lipoteichoic acid (LTA), the principal component of the cell wall of gram-positive bacteria, triggers several inflammatory responses. However, the mechanisms underlying its action on human tracheal smooth muscle cells (HTSMCs) were largely unknown. This study was to investigate the mechanisms underlying LTA-stimulated p42/p44 mitogen-activated protein kinase (MAPK) using Western blotting assay. LTA stimulated phosphorylation of p42/p44 MAPK via a Toll-like receptor 2 (TLR2). Pretreatment with pertussis toxin attenuated the LTA-induced responses. LTA-stimulated phosphorylation of p42/p44 MAPK was attenuated by inhibitors of tyrosine kinase (genistein), phosphatidylcholine-phospholipase C (PLC; D609), phosphatidylinositol (PI)-PLC (U-73122), PKC (staurosporine, Gö-6976, rottlerin, or Ro-318220), MEK1/2 (U-0126), PI 3-kinase (LY-294002 and wortmannin), and an intracellular Ca2+ chelator (BAPTA-AM). LTA directly evoked initial transient peak of [Ca2+]i, supporting the involvement of Ca2+ mobilization in LTA-induced responses. These results suggest that in HTSMCs, LTA-stimulated p42/p44 MAPK phosphorylation is mediated through a TLR2 receptor and involves tyrosine kinase, PLC, PKC, Ca2+, MEK, and PI 3-kinase.

calcium; human; phospholipase C; protein kinase C


Address for reprint requests and other correspondence: C.-M. Yang, Dept. of Pharmacology, College of Medicine, Chang Gung Univ., 259 Wen-Hwa 1 Road, Kwei-San, Tao-Yuan, Taiwan, 3332 (E-mail: chuenmao{at}mail.cgu.edu.tw).




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