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J. Biol. Chem., Vol. 282, Issue 42, 30878-30888, October 19, 2007

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TM14 Is a New Member of the Fibulin Family (Fibulin-7) That Interacts with Extracellular Matrix Molecules and Is Active for Cell Binding^*

Susana de Vega, Tsutomu Iwamoto¹, Takashi Nakamura, Kentaro Hozumi², Dianalee A. McKnight, Larry W. Fisher, Satoshi Fukumoto^¶, and Yoshihiko Yamada³

From the Laboratory of Cell and Developmental Biology and the Craniofacial and Skeletal Diseases Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892-4370 and the ^¶Department of Pediatric Dentistry, Faculty of Dental Science, Kyushu University, Fukuoka 812-8582, Japan

We identified a new extracellular protein, TM14, by differential hybridization using mouse tooth germ cDNA microarrays. TM14 cDNA encodes 440 amino acids containing a signal peptide. The protein contains 3 EGF modules at the center, a C-terminal domain homologous to the fibulin module, and a unique Sushi domain at the N terminus. In situ hybridization revealed that TM14 mRNA was expressed by preodontoblasts and odontoblasts in developing teeth. TM14 mRNA was also expressed in cartilage, hair follicles, and extraembryonic tissues of the placenta. Immunostaining revealed that TM14 was localized at the apical pericellular regions of preodontoblasts. When the dentin matrix was fully formed and dentin mineralization occurred, TM14 was present in the predentin matrix and along the dentinal tubules. We found that the recombinant TM14 protein was glycosylated with N-linked oligosaccharides and interacted with heparin, fibronectin, fibulin-1, and dentin sialophosphoprotein. We also found that TM14 preferentially bound dental mesenchyme cells and odontoblasts but not dental epithelial cells or nondental cells such as HeLa, COS7, or NIH3T3 cells. Heparin, EDTA, and anti-integrin 1 antibody inhibited TM14 binding to dental mesenchyme cells, suggesting that both a heparan sulfate-containing cell surface receptor and an integrin are involved in TM14 cell binding. Our findings indicate that TM14 is a cell adhesion molecule that interacts with extracellular matrix molecules in teeth and suggest that TM14 plays important roles in both the differentiation and maintenance of odontoblasts as well as in dentin formation. Because of its protein characteristics, TM14 can be classified as a new member of the fibulin family: fibulin-7.

Received for publication, July 16, 2007 , and in revised form, August 13, 2007.

^* This work was supported in part by the Intramural Research Program of the NIDCR, National Institutes of Health, National Institute of Dental and Craniofacial Research (to Y. Y. and L. F.), the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to S. F.), and a Fellowship from the Basque Government, Spain (to S. V.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1.

¹ Present address: Dept. of Pediatric Dentistry, Faculty of Dental Science, Kyushu University, Fukuoka 812-8582, Japan.

² Present address: School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan.

³ To whom correspondence should be addressed: Bldg. 30, Rm. 407, NIDCR, National Institutes of Health, 30 Convent Dr. MSC 4370, Bethesda, MD 20892-4370. Fax: 301-402-0897; E-mail: yoshi.yamada{at}nih.gov.

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