Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1

doi:10.1074/jbc.M506980200

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Papers In Press, published online ahead of print August 1, 2005
J. Biol. Chem, 10.1074/jbc.M506980200
Submitted on June 27, 2005
Revised on July 29, 2005
Accepted on August 1, 2005

Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1

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

Molecular, Cell and Dev. Biology, UCLA, Los Angeles, CA 90095

Corresponding Author: arispe{at}mbi.ucla.edu

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 carboxy-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, pull down assays and ELISA, the ability of these two proteins to interact was substantiated. Additional studies showed that ADAMTS-1 and fibulin-1 co-localized 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 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.

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