A novel mouse beta-defensin, mBD-6, predominantly expressed in skeletal muscle

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-08, Vol.276 (34), p.31510-31514
Main Authors: Yamaguchi, Y, Fukuhara, S, Nagase, T, Tomita, T, Hitomi, S, Kimura, S, Kurihara, H, Ouchi, Y
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
b-defensin
Base Sequence
Defensins - chemistry
Defensins - genetics
Defensins - metabolism
DNA, Complementary
Escherichia coli
Female
Mice
Mice, Inbred ICR
Molecular Sequence Data
Muscle, Skeletal - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0021-9258
DOI:10.1074/jbc.M104149200