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J. Biol. Chem., Vol. 280, Issue 24, 22596-22605, June 17, 2005

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Endo180 Binds to the C-terminal Region of Type I Collagen^*

Emily K. Thomas, Misa Nakamura, Dirk Wienke¶, Clare M. Isacke¶, Ambra Pozzi||, and Peng Liang**

From the Vanderbilt-Ingram Cancer Center, Department of Cancer Biology, and ^||Department of Nephrology and Hypertension, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and the ^¶Breakthrough Breast Cancer Research Centre, Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, United Kingdom

Type I collagen is a fibril-forming heterotrimer composed of two 1 and one 2 chains and plays a crucial role in cell-matrix adhesion and cell differentiation. Through a comprehensive differential display screening of oncogenic ras target genes, we have shown that the 1 chain of type I collagen (col1a1) is markedly down-regulated by the ras oncogene through the mitogen-activated protein kinase pathway. Although ras-transformed cells are no longer able to produce and secrete endogenous collagen, they can still adhere to exogenous collagen, suggesting that the cells express a collagen binding factor(s) on the cell surface. When the region of col1a1 encompassing the C-terminal glycine repeat and C-prodomain (amino acids 1000–1453) was affinity-labeled with human placental alkaline phosphatase, the secreted trimeric fusion protein could bind to the surface of Ras-transformed cells. Using biochemical purification followed by matrix-assisted laser desorption/ionization mass spectrometry analysis, we identified this collagen binding factor as Endo180 (uPARAP, CD280), a member of the mannose receptor family. Ectopic expression of Endo180 in CosE5 cells followed by in situ staining and quantitative binding assays confirmed that Endo180 indeed recognizes and binds to placental alkaline phosphatase. The interaction between Endo180 and the C-terminal region of type I collagen appears to play an important role in cell-matrix adhesion.

Received for publication, February 1, 2005 , and in revised form, March 25, 2005.

^* This work was supported by the Vanderbilt-Ingram Cancer Center, Multidisciplinary Basic Research Training in Cancer Grant T32CA09592, and NCI, National Institutes of Health, Grant R01 CA94849-01 (to A. P.). 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 nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) DQ058624.

^** To whom correspondence should be addressed: 658 Preston Research Bldg., the Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232. Tel.: 615-936-2182; Fax: 615-936-2183; E-mail: peng.liang{at}vanderbilt.edu.

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