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Originally published In Press as doi:10.1074/jbc.M100861200 on April 5, 2001

J. Biol. Chem., Vol. 276, Issue 26, 24023-24029, June 29, 2001
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Molecular Cloning and Biological Activity of a Novel Lysyl Oxidase-related Gene Expressed in Cartilage*

Hiromu ItoDagger , Haruhiko AkiyamaDagger §, Hiroshi Iguchi, Ken-ichi Iyama||, Masatomo Miyamoto, Kunitaka Ohsawa, and Takashi Nakamura

From the Department of Orthopaedic Surgery, Graduate School of Medicine, Kyoto University, Sakyo, Kyoto 606-8507, the  Department of Hygiene, Hyogo College of Medicine, Nishinomiya, Hyogo 663-8501, and the || Department of Surgical Pathology, Kumamoto University School of Medicine, Kumamoto 860-8556, Japan

We cloned a cDNA encoding a novel lysyl oxidase-related protein, named LOXC, by suppression subtractive hybridization between differentiated and calcified ATDC5 cells, a clonal mouse chondrogenic EC cell line. The deduced amino acid sequence of mouse LOXC consists of 757 amino acids and shows 50% identity with that of mouse lysyl oxidase. Northern blot analysis showed a distinct hybridization band of 5.4 kilobases, and Western blot analysis showed an immunoreactive band at 82 kilodaltons. Expression of LOXC mRNA was detected in osteoblastic MC3T3-E1 cells and embryonic fibroblast C3H10T1/2 cells, whereas none of NIH3T3 fibroblasts and myoblastic C2C12 cells expressed LOXC mRNA in vitro. Moreover, the LOXC mRNA and protein levels dramatically increased throughout a process of chondrogenic differentiation in ATDC5 cells. In vivo, LOXC gene expression was localized in hypertrophic and calcified chondrocytes of growth plates in adult mice. The conditioned media of COS-7 cells transfected with the full-length LOXC cDNA showed the lysyl oxidase activity in both type I and type II collagens derived from chick embryos, and these activities of LOXC were inhibited by beta -aminopropionitrile, a specific inhibitor of lysyl oxidase. Our data indicate that LOXC is expressed in cartilage in vivo and modulates the formation of a collagenous extracellular matrix.

* This work was supported by Grant 0123 from the Japan Orthopaedics and Traumatology Foundation, Inc.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF338440.

Dagger Both authors contributed equally to this work.

§ To whom correspondence should be addressed: Dept. of Orthopaedic Surgery, Graduate School of Medicine, Kyoto University, Sakyo, Kyoto 606-8507, Japan. Tel.: 81-75-751-3652; Fax: 81-75-751-8409; E-mail: akiy@kuhp.kyoto-u.ac.jp.

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