| Literature DB >> 30992230 |
Stefan Düsterhöft1, Juliane Lokau2, Christoph Garbers3.
Abstract
Proteolytic cleavage of transmembrane proteins is an important post-translational modification that regulates the biological function of numerous transmembrane proteins. Among the 560 proteases encoded in the human genome, the metalloprotease A Disintegrin and Metalloprotease 17 (ADAM17) has gained much attention in recent years and has emerged as a central regulatory hub in inflammation, immunity and cancer development. In order to do so, ADAM17 cleaves a variety of substrates, among them the interleukin-6 receptor (IL-6R), the pro-inflammatory cytokine tumor necrosis factor α (TNFα) and most ligands of the epidermal growth factor receptor (EGFR). This review article provides an overview of the functions of ADAM17 with a special focus on its cellular regulation. It highlights the importance of ADAM17 to understand the biology of IL-6 and TNFα and their role in inflammatory diseases. Finally, the role of ADAM17 in the formation and progression of different tumor entities is discussed.Entities:
Keywords: ADAM17; Cancer; IL-6; Inflammation; Proteolysis; TNFα
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Year: 2019 PMID： 30992230 DOI： 10.1016/j.prp.2019.04.002
Source DB: PubMed Journal: Pathol Res Pract ISSN： 0344-0338 Impact factor: 3.250