Cell-surface processing of pro-adams9 by furin

doi:10.1074/jbc.M511083200

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Papers In Press, published online ahead of print March 14, 2006
J. Biol. Chem, 10.1074/jbc.M511083200
Submitted on October 12, 2005
Revised on March 13, 2006
Accepted on March 14, 2006

Cell-surface processing of pro-adams9 by furin

Bon-Hun Koo, Jean-Michel Longpre, Robert P. T. Somerville, J. Preston Alexander, Richard Leduc, and Suneel S. Apte

Biomedical Engineering, Cleveland Clinic Foundation, ND20, Cleveland, OH 44195

Corresponding Author: aptes{at}ccf.org

Processing of polypeptide precursors by proprotein convertases (PCs) such as furin typically occurs within the trans-Golgi network. Here, we show in a variety of cell types that the propeptide of ADAMTS9 is not excised intracellularly. Pulse-chase analysis in HEK293F cells indicated that the intact zymogen was secreted to the cell-surface and was subsequently processed there before release into the medium. The processing occurred via a furin-dependent mechanism as shown using PC inhibitors, lack of processing in furin-deficient cells, and rescue by furin in these cells. Moreover, down-regulation of furin by siRNA reduced ADAMTS9 processing in HEK293F cells. PC5A could also process proADAMTS9, but similarly to furin, processed forms were absent intracellularly. Cell-surface, furin-dependent processing of proADAMTS9 creates a precedent for extracellular maturation of endogenously produced secreted proproteins. It also indicates the existence of a variety of mechanisms for processing of ADAMTS proteases.

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