Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases

By A. Anders, S. Gilbert, W. Garten, R. Postina, F. Fahrenholz. 2001

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The ADAM metalloproteinases (2008, background): “…the Cys-switch mechanism involved in maintaining latency (Gonzales et al., 2004), and indeed it has been suggested that the main functions of the pro-domain are to act as a chaperone and to protect the enzymes from degradation in the secretory system (Anders et al., 2001; Milla et al., 2006).”
Strategies to improve plasma half life time of peptide and protein drugs (2006, background): “…in the propeptide of collagenase 3, and Asn341-=-Phe, Asp441-=-Leu and Gln354-=-Thr in the aggrecan interglobular domain Cytoplasm, membrane (liver) (Seiki, 2003) 3.4.24.81 endopeptidase of broad specificity Membrane (kidney) (Anders et al., 2001) 3.4.24.86 narrow endopeptidase specificity.”
The ADAMs family of metalloproteases: multidomain proteins with multiple functions. (2003, background): “Thirdly, mutation of PC cleavage sites blocks the processing of ADAM10, ADAM12, and ADAM19 to their mature, active forms (Loechel et al. 1998; Anders et al. 2001; Kang et al. 2002).”
Furin at the cutting edge: From protein traffic to embryogenesis and disease (2002, background): “Characteristic of this protein family, both ADAM10 and ADAM17 contain propeptides that are linked to their catalytic domains by a consensus furin motif, and cleavage at this site is required for their activatio”