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Originally published In Press as doi:10.1074/jbc.M106671200 on November 27, 2001

J. Biol. Chem., Vol. 277, Issue 9, 6830-6837, March 1, 2002
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Surfactant Protein A Inhibits Peptidoglycan-induced Tumor Necrosis Factor-alpha Secretion in U937 Cells and Alveolar Macrophages by Direct Interaction with Toll-like Receptor 2*

Seiji MurakamiDagger §, Daisuke IwakiDagger , Hiroaki MitsuzawaDagger , Hitomi SanoDagger , Hiroki Takahashi§, Dennis R. Voelker, Toyoaki AkinoDagger , and Yoshio KurokiDagger ||

From the Dagger  Department of Biochemistry and § Third Department of Internal Medicine, Sapporo Medical University School of Medicine, Sapporo, 060-8556, Japan and  Department of Medicine, National Jewish Medical and Research Center, Denver, Colorado 80206

Pulmonary surfactant protein A (SP-A) plays an important role in modulation of the innate immune system of the lung. Peptidoglycan (PGN), a cell wall component of Gram-positive bacteria, is known to elicit excessive proinflammatory cytokine production from immune cells. In this study we investigated whether SP-A interacts with PGN and alters PGN-elicited cellular responses. Binding studies demonstrate that PGN is not a ligand for SP-A. However, SP-A significantly reduced PGN-elicited tumor necrosis factor alpha  (TNF-alpha ) secretion by U937 cells and rat alveolar macrophages. The inhibitory effect on TNF-alpha secretion was dependent upon SP-A concentrations in physiological range. Coincubation of SP-A and PGN with human embryonic kidney 293 cells that had been transiently transfected with the cDNA of Toll-like receptor 2 (TLR2), a cell signaling receptor for PGN, significantly attenuated PGN-induced nuclear factor-kappa B activity. SP-A directly bound to a soluble form of the recombinant extracellular TLR2 domain (sTLR2). Coincubation of sTLR2 with SP-A significantly reduced the binding of sTLR2 to PGN. These results indicate that the direct interaction of SP-A with TLR2 alters PGN-induced cell signaling. We propose that SP-A modulates inflammatory responses against the bacterial components by interactions with pattern-recognition receptors.

* This work was supported in part by a grant-in-aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture, Japan and from the Novartis Foundation (Japan).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry, Sapporo Medical University School of Medicine, South-1 West-17, Chuo-ku, Sapporo 060-8556, Japan. Tel.: 81-11-611-2111; Fax: 81-11-611-2236; E-mail: kurokiy@sapmed.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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