c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (p38 MAPK) are involved in Mycobacterium tuberculosis-induced expression of Leukotactin-1

• Published in: BMB reports Vol. 45; no. 10; pp. 583 - 588
• Main Authors: Cho, J.E., Daegu Health College, Daegu, Republic of Korea, Park, S.J., Yonsei University, Wonju, Republic of Korea, Cho, S.N., Yonsei University College of Medicine, Seoul, Republic of Korea, Lee, H.Y., Yonsei University, Wonju, Republic of Korea, Kim, Y.S., Yonsei University, Wonju, Republic of Korea
• Format: Journal Article
• Language: English
• Published: Korea (South) Korean Society for Biochemistry and Molecular Biology 01.10.2012; 생화학분자생물학회
• Subjects: Anthracenes - pharmacology; Cell Line, Tumor; Chemokines, CC - metabolism; Humans; Imidazoles - pharmacology; JNK; JNK Mitogen-Activated Protein Kinases - antagonists & inhibitors; JNK Mitogen-Activated Protein Kinases - metabolism; Leukotactin-1; MACROFAGOS; MACROPHAGE; MACROPHAGES; Mycobacterium tuberculosis; Mycobacterium tuberculosis - enzymology; Mycobacterium tuberculosis - metabolism; p38 MAPK; p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors; p38 Mitogen-Activated Protein Kinases - metabolism; Phosphatidylinositol 3-Kinases; Phosphorylation; Proto-Oncogene Proteins c-akt - metabolism; Pyridines - pharmacology; Signal Transduction - drug effects; Tuberculosis - metabolism; Tuberculosis - pathology; Up-Regulation - drug effects; 화학
• ISSN: 1976-6696; 1976-670X
• DOI: 10.5483/BMBRep.2012.45.10.120

Leukotactin(Lkn)-1 is a CC chemokine and is upregulated in macrophages in response to Mycobacterium tuberculosis (MTB) infection. We investigated whether mitogen-activated protein kinases (MAPKs) are involved in MTB-induced expression of Lkn-1. The up-regulation of Lkn-1 by infection with MTB was inhibited in cells treated with inhibitors specific for INK (SP600125) or p38 MAPK (SB202190). Since the up-regulation of Lkn-1 by MTB has been reported to be mediated by the PI3-K/PDK1/Akt signaling, we examined whether INK and/or p38 MAPK are also involved in this signal pathway. MTB-induced Akt phosphorylation was blocked by treatment with JNK- or p38 MAPK-specific inhibitors implying that p38 and INK are upstream of Aid. In addition, treatment with the PI3-K-specific inhibitor inhibited MTB-stimulated activation of INK or p38 MAPK implying that PI3-K is upstream of INK and p38 MAPK. These results collectively suggest that INK and p38 MAPK are involved in the signal pathway responsible for MTB-induced up-regulation of Lkn-1.