| First Author | Lee NV | Year | 2005 |
| Journal | J Biol Chem | Volume | 280 |
| Issue | 41 | Pages | 34796-804 |
| PubMed ID | 16061471 | Mgi Jnum | J:102464 |
| Mgi Id | MGI:3607633 | Doi | 10.1074/jbc.M506980200 |
| Citation | Lee NV, et al. (2005) Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1. J Biol Chem 280(41):34796-804 |
| abstractText | 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. |
