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Originally published In Press as doi:10.1074/jbc.M104149200 on June 14, 2001

J. Biol. Chem., Vol. 276, Issue 34, 31510-31514, August 24, 2001
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A Novel Mouse beta -Defensin, mBD-6, Predominantly Expressed in Skeletal Muscle*

Yasuhiro YamaguchiDagger §, Shigetomo Fukuhara§, Takahide NagaseDagger , Tetsuji TomitaDagger , Shigemi Hitomi, Satoshi Kimura||, Hiroki Kurihara§**, and Yasuyoshi OuchiDagger

From the Dagger  Departments of Geriatric Medicine and || Infection Control and Prevention, Graduate School of Medicine, University of Tokyo, Tokyo 113-8655, Japan, the § Division of Integrative Cell Biology, Department of Embryogenesis, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, Japan, and the  Department of Infectious Diseases, Institute of Clinical Medicine, University of Tsukuba, Tsukuba 305-8575, Japan

Defensins comprise a family of cationic antimicrobial peptides that is characterized by the conserved 6 cysteine residues. They are expressed in the epithelial cells of various organs and are identified as key elements in the host defense system at the mucosal surface. We isolated a novel mouse beta -defensin gene from the bacterial artificial chromosome DNA containing the mouse beta -defensin-3 gene. The full-length cDNA was cloned from skeletal muscle cDNA and called mouse beta -defensin-6 (mBD-6). The predicted peptide conserved the 6-cysteine motif and had 59% amino acid sequence identity with mouse beta -defensin-3 and 59% identity with mouse beta -defensin-4. We demonstrated the expression of mBD-6 in skeletal muscle in addition to the esophagus, tongue, and trachea. In animal models of endotoxemia, mBD-6 expression was also induced in the lung. mBD-6 showed potent antimicrobial activity against Escherichia coli and would play an important role in host defense in the esophagus, airways, and skeletal muscle. mBD-6 is the first reported beta -defensin predominantly expressed in skeletal muscle. This unique tissue specificity suggests some novel physiological roles of this peptide family.

* This work was supported by the Japan Society for the Promotion of Science Research for the Future Program, the Research Grant for Cardiovascular Diseases (11C-1) from the Ministry of Health and Welfare, the Program for Promotion of Fundamental Studies in Health Sciences of the Organization for Pharmaceutical Safety and Research (to H. K.), grants-in-aid for Scientific Research from the Ministry of Education, Science and Culture, Japan (to H. K., T. N., and Y. Y.), and the Yamanouchi Foundation for Research on Metabolic Disorders.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: Div. of Integrative Cell Biology, Dept. of Embryogenesis, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto-shi, Kumamoto 860-0811, Japan. Tel.: 096-373-6615; Fax: 096-373-6618; E-mail: kurihara@kaiju.medic.kumamoto-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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