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Originally published In Press as doi:10.1074/jbc.M109665200 on January 22, 2002

J. Biol. Chem., Vol. 277, Issue 14, 12182-12189, April 5, 2002
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Punctin, a Novel ADAMTS-like Molecule, ADAMTSL-1, in Extracellular Matrix*

Satoshi HirohataDagger §, Lauren W. WangDagger §, Masaru Miyagi, Lin Yan, Michael F. Seldin||, Douglas R. Keene**, John W. Crabb, and Suneel S. ApteDagger Dagger Dagger §§

From the Dagger  Department of Biomedical Engineering, Lerner Research Institute, the Dagger Dagger  Department of Orthopaedic Surgery, Cleveland Clinic Foundation, the  Department of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, the || Rowe Program in Genetics, Departments of Biological Chemistry and Medicine, University of California at Davis, Davis, California 956161, and the ** Shriner's Hospital for Children, Portland, Oregon 97201

Punctin (ADAMTSL-1) is a secreted molecule resembling members of the ADAMTS family of proteases. Punctin lacks the pro-metalloprotease and the disintegrin-like domain typical of this family but contains other ADAMTS domains in precise order including four thrombospondin type I repeats. Punctin is the product of a distinct gene on human chromosome 9p21-22 and mouse chromosome 4 that is expressed in adult skeletal muscle. His-tagged punctin expressed in stably transfected High-FiveTM insect cells was purified to apparent homogeneity by Ni-chromatography of conditioned medium. The NH2 terminus is not blocked and has the sequence EEDRD and so forth as determined by Edman degradation, demonstrating signal peptidase processing. Recombinant epitope-tagged punctin has a calculated mass of 59,991 Da but exhibits major molecular species of 61970 ± 6 Da and 62131 ± 5 Da as measured by liquid chromatography electrospray mass spectrometry. Punctin is a glycoprotein based on carbohydrate staining and liquid chromatography electrospray mass spectrometry glycopeptide analysis. Glycosylation occurs at a single N-linked site as demonstrated by altered electrophoretic migration of punctin expressed in the presence of tunicamycin A. Punctin contains disulfide bonds based on antibody accessibility and electrophoretic migration under reducing versus nonreducing conditions. Rotary shadowing demonstrates that punctin is hatchet-shaped having a globular region attached to a short stem. In transfected COS-1 cells, punctin is deposited in the cell substratum in a punctate fashion and is excluded from focal contacts. Punctin is the first member of a novel family of ADAMTS-like proteins that may have important functions in the extracellular matrix.


* This work was supported in part by the Cleveland Clinic Foundation (to S. S. A.), a Yamanouchi USA Foundation Award (to S. S. A.), and National Institutes of Health Grants EY06603 (to J. W. C.) and HGO0734 (to M. F. S.).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/EBI Data Bank with accession number(s) AF176313.

§ Both authors contributed equally to this work.

§§ To whom correspondence should be addressed: Dept. of Biomedical Engineering (ND20), Lerner Research Inst., Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Tel.: 216-445-3278; Fax: 216-445-4383; E-mail: aptes@bme.ri.ccf.org or www.lerner.ccf.org/pi/apte.html.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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