ADAM proteases, ErbB pathways and cancer

Bin-Bing S Zhou Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Jordan S Fridman Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Xiangdong Liu Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Steve M Friedman Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Robert C Newton Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Peggy A Scherle Drug Discovery Biology, Incyte Corporation, Experimental Station, Route 141 & Henry Clay Road, Building 400, Wilmington, DE 19880, USA. [email protected]

Abstract

A disintegrin and metalloproteases (ADAMs) are zinc-dependent trans-membrane metalloproteases that shed the extracellular domains of membrane-bound growth factors, cytokines and receptors. Key functions of ADAMs have emerged in ErbB signalling pathways as being sheddases for multiple ErbB ligands. As the ErbB pathway is a validated target for anti-cancer drugs, the upstream activators of ErbB ligands, their sheddases, now enter the spotlight as new drug targets in the ErbB pathway. ADAMs are involved not only in tumour cell proliferation but also in angiogenesis and metastasis. Therefore, strategies targeting ADAMs might be an important complement to existing anti-ErbB approaches.

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ADAM proteases, ErbB pathways and cancer

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