ADAM and ADAMTS Proteases in Hepatic Disorders
Main Article Content
Keywords
ADAM, ADAMTS, metzincin superfamily, thrombotic thrombocytopenia purpura, von Willebrand Factor
Abstract
Proteolysis is an irreversible post-translational modification that regulates protein function and signal transduction. This includes remodelling of the extracellular matrix, release of membrane-bound cytokines and receptor ectodomains, as well as the initiation of intracellular signalling cues. Members of the adamalysin protease subfamily, in particular the ADAM (a disintegrin and metalloprotease) and ADAMTS (the ADAM containing thrombospondin motif) families, are involved in these processes. This review presents an overview of how ADAM and ADAMTS proteins are involved in liver physiology and pathophysiology.
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2. Köhn-Gaone J, Gogoi-Tiwari J, Ramm GA, Olynyk JK, Tirnitz-Parker JEE. The role of liver progenitor cells during liver regeneration, fibrogenesis, and carcinogenesis. Am J Physiol. 2016;310:G143–54.
3. Ruddell RG, Knight B, Tirnitz-Parker JEE, Akhurst B, Summerville L, Subramaniam VN, et al. Lymphotoxin-beta receptor signaling regulates hepatic stellate cell function and wound healing in a murine model of chronic liver injury. Hepatology. 2009;49:227–39. https://doi.org/10.1002/hep.22597
4. Boulter L, Govaere O, Bird TG, Radulescu S, Ramachandran P, Pellicoro A, et al. Macrophage-derived Wnt opposes Notch signaling to specify hepatic progenitor cell fate in chronic liver disease. Nat Med. 2012;18:572–9. https://doi.org/10.1038/nm.2667
5. Tirnitz-Parker JEE, Olynyk JK, Ramm GA. Role of TWEAK in coregulating liver progenitor cell and fibrogenic responses. Hepatology. 2014;59:1198–201. https://doi.org/10.1002/hep.26701
6. Finkin S, Yuan D, Stein I, Taniguchi K, Weber A, Unger K, et al. Ectopic lymphoid structures function as microniches for tumor progenitor cells in hepatocellular carcinoma. Nat Immunol. 2015;16:1235–44. https://doi.org/10.1038/ni.3290
7. Huxley-Jones J, Clarke T-K, Beck C, Toubaris G, Robertson DL, Boot-Handford RP. The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio. BMC Evol Biol. 2007;7:63. https://doi.org/10.1186/1471-2148-7-63
8. Gomis-Rüth FX. Catalytic domain architecture of metzincin metalloproteases. Biol Chem. 2009;284:15353–7. https://doi.org/10.1074/jbc.R800069200
9. Reiss K, Saftig P. The “a disintegrin and metalloprotease” (ADAM) family of sheddases: Physiological and cellular functions. Semin Cell Dev Biol. 2009;20:126–37. https://doi.org/10.1016/j.semcdb.2008.11.002
10. Seegar TCM, Killingsworth LB, Saha N, Meyer PA, Patra D, Zimmerman B, et al. Structural basis for regulated proteolysis by the ?-secretase ADAM10. Cell. 2017;171:1638–48. https://doi.org/10.1016/j.cell.2017.11.014
11. Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, et al. Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. Protein Sci. 2008;17:16–21. https://doi.org/10.1110/ps.073287008
12. Düsterhöft S, Jung S, Hung C-W, Tholey A, Sönnichsen FD, Grötzinger J, et al. Membrane-proximal domain of a disintegrin and metalloprotease-17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase. J Am Chem Soc. 2013;135:5776–81. https://doi.org/10.1110/ps.073287008
13. Jones JC, Rustagi S, Dempsey PJ. ADAM proteases and gastrointestinal function. Annu Rev Physiol. 2016;78:243–76. https://doi.org/10.1146/annurev-physiol-021014-071720
14. Howard L, Maciewicz RA, Blobel CP. Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem J. 2000;348 Pt 1:21–7. https://doi.org/10.1042/bj3480021
15. Schlomann U, Wildeboer D, Webster A, Antropova O, Zeuschner D, Knight CG, et al. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J Biol Chem. 2002;277:48210–19. https://doi.org/10.1074/jbc.M203355200
16. Wong E, Cohen T, Romi E, Levin M, Peleg Y, Arad U, et al. Harnessing the natural inhibitory domain to control TNF? Converting Enzyme (TACE) activity in vivo. Sci Rep. 2016;6:35598. https://doi.org/10.1038/srep35598
17. Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, et al. Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc Natl Acad Sci U S A. 1998;95:3408–12. https://doi.org/10.1073/pnas.95.7.3408
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Feb 7, 2019
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ADAM and ADAMTS Proteases in Hepatic Disorders. (2019). Journal of Renal and Hepatic Disorders, 3(1), 23-32. https://doi.org/10.15586/jrenhep.2019.47
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