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J. Biol. Chem., Vol. 280, Issue 41, 34796-34804, October 14, 2005

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Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1^*

Nathan V. Lee, Juan Carlos Rodriguez-Manzaneque1, Shelley N.-M. Thai, Waleed O. Twal¶, Alfonso Luque, Karen M. Lyons, W. Scott Argraves¶, and M. Luisa Iruela-Arispe2

From the Department of Molecular, Cell, and Developmental Biology and Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90095 and the ^¶Department of Cell Biology and Anatomy, Medical University of South Carolina, Charleston, South Carolina 29425

ADAMTS-1 is a metalloprotease that has been implicated in the inhibition of angiogenesis and is a mediator of proteolytic cleavage of the hyaluronan binding proteoglycans, aggrecan and versican. In an attempt to further understand the biological function of ADAMTS-1, a yeast two-hybrid screen was performed using the carboxyl-terminal region of ADAMTS-1 as bait. As a result, the extracellular matrix protein fibulin-1 was identified as a potential interacting molecule. Through a series of analyses that included ligand affinity chromatography, co-immunoprecipitation, pulldown assays, and enzyme-linked immunosorbent assay, the ability of these two proteins to interact was substantiated. Additional studies showed that ADAMTS-1 and fibulin-1 colocalized in vivo. Furthermore, fibulin-1 was found to enhance the capacity of ADAMTS-1 to cleave aggrecan, a proteoglycan known to bind to fibulin-1. We confirmed that fibulin-1 was not a proteolytic substrate for ADAMTS-1. Together, these findings indicate that fibulin-1 is a new regulator of ADAMTS-1-mediated proteoglycan proteolysis and thus may play an important role in proteoglycan turnover in tissues where there is overlapping expression.

Received for publication, June 27, 2005 , and in revised form, July 29, 2005.

^* This work was supported by National Institutes of Health Grants CA077420 (to M. L. I.-A.) and HL52813 and HL61873 (to W. S. A), U.S. Public Health Service National Research Service Award GM07185 (to N. V. L.), and American Heart Association Fellowship 0315010Y (to N. V. L.). 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.

¹ Present address: Hospital Universitari Vall d'Hebron, Barcelona, Spain.

² To whom correspondence should be addressed: Paul D. Boyer Hall/Molecular Biology Institute, UCLA, 611 Charles Young Dr. East, Los Angeles, CA 90095. Tel.: 310-794-5763; Fax: 310-794-5766; E-mail: arispe{at}mbi.ucla.edu.

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