Considerations on inhibition approaches for proinflammatory functions of ADAM proteases

References

• Scheller J, Chalaris A, Garbers C, Rose-John S. ADAM17: a molecular switch to control inflammation and tissue regeneration. Trends Immunol. 2011;32:380–387.
   PubMed Web of Science ®Google Scholar
• Saftig P, Reiss K. The “A Disintegrin And Metalloproteases” ADAM10 and ADAM17: Novel drug targets with therapeutic potential? Eur.J.Cell Biol. 2011;90:527–535
   PubMed Web of Science ®Google Scholar
• Dreymueller D, Uhlig S, Ludwig A. ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets. Am.J.Physiol Lung Cell Mol.Physiol 2015;308:L325–L343.
   PubMed Web of Science ®Google Scholar
• Dreymueller D, Pruessmeyer J, Groth E, Ludwig A. The role of ADAM-mediated shedding in vascular biology. Eur.J.Cell Biol. 2012;91:472–485.
   PubMed Web of Science ®Google Scholar
• Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, Castner BJ, Stocking KL, Reddy P, Srinivasan S et al. A metalloproteinase disintegrin that releases tumour necrosis factor-alpha from cells. Nature 1997;385:729–733.
   PubMed Web of Science ®Google Scholar
• Schulz B, Pruessmeyer J, Maretzky T, Ludwig A, Blobel CP, Saftig P, Reiss K. ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin. Circ.Res. 2008;102:1192–1201.
   PubMed Web of Science ®Google Scholar
• Koenen RR, Pruessmeyer J, Soehnlein O, Fraemohs L, Zernecke A, Schwarz N, Reiss K, Sarabi A, Lindbom L, Hackeng TM et al. Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood. 2009;113:4799–4809.
   PubMed Web of Science ®Google Scholar
• Al-Tamimi M, Tan CW, Qiao J, Pennings GJ, Javadzadegan A, Yong AS, Arthur JF, Davis AK, Jing J, Mu FT et al. Pathologic shear triggers shedding of vascular receptors: a novel mechanism for down-regulation of platelet glycoprotein VI in stenosed coronary vessels. Blood. 2012;119:4311–4320.
   PubMed Web of Science ®Google Scholar
• Gardiner EE, Karunakaran D, Shen Y, Arthur JF, Andrews RK, Berndt MC. Controlled shedding of platelet glycoprotein (GP)VI and GPIb-IX-V by ADAM family metalloproteinases. J Thromb.Haemost. 2007;5:1530–1537.
   PubMed Web of Science ®Google Scholar
• Rabie T, Strehl A, Ludwig A, Nieswandt B. Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V. J Biol.Chem. 2005;280:14462–14468.
   PubMed Web of Science ®Google Scholar
• Pruessmeyer J, Hess FM, Alert H, Groth E, Pasqualon T, Schwarz N, Nyamoya S, Kollert J, van d, V, Donners M et al. Leukocytes require ADAM10 but not ADAM17 for their migration and inflammatory recruitment into the alveolar space. Blood 2014;123:4077–4088.
   PubMed Web of Science ®Google Scholar
• Naus S, Blanchet MR, Gossens K, Zaph C, Bartsch JW, McNagny KM, Ziltener HJ. The metalloprotease-disintegrin ADAM8 is essential for the development of experimental asthma. Am.J.Respir.Crit Care Med. 2010;181:1318–1328.
   PubMed Web of Science ®Google Scholar
• Hartmann D, de Strooper B, Serneels L, Craessaerts K, Herreman A, Annaert W, Umans L, Lubke T, Lena IA, von Figura K et al. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. Hum.Mol.Genet. 2002;11:2615–2624.
   PubMed Web of Science ®Google Scholar
• Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart JW, Kremmer E, Rossner S, Lichtenthaler SF. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J. 2010;29:3020–3032.
   PubMed Web of Science ®Google Scholar
• Sahin U, Weskamp G, Kelly K, Zhou HM, Higashiyama S, Peschon J, Hartmann D, Saftig P, Blobel CP. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol. 2004;164:769–779.
   PubMed Web of Science ®Google Scholar
• Weber S, Niessen MT, Prox J, Lullmann-Rauch R, Schmitz A, Schwanbeck R, Blobel CP, Jorissen E, de Strooper B, Niessen CM et al. The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling. Development. 2011;138:495–505.
   PubMed Web of Science ®Google Scholar
• Chalaris A, Adam N, Sina C, Rosenstiel P, Lehmann-Koch J, Schirmacher P, Hartmann D, Cichy J, Gavrilova O, Schreiber S et al. Critical role of the disintegrin metalloprotease ADAM17 for intestinal inflammation and regeneration in mice. J.Exp.Med. 2010;207:1617–1624.
   PubMed Web of Science ®Google Scholar
• Pasqualon T, Pruessmeyer J, Jankowski V, Babendreyer A, Groth E, Schumacher J, Koenen A, Weidenfeld S, Schwarz N, Denecke B et al. A cytoplasmic C-terminal fragment of Syndecan-1 is generated by sequential proteolysis and antagonizes Syndecan-1 dependent lung tumor cell migration. Oncotarget. 2015;6:31295–31312.
   PubMed Web of Science ®Google Scholar
• Pasqualon T, Pruessmeyer J, Weidenfeld S, Babendreyer A, Groth E, Schumacher J, Schwarz N, Denecke B, Jahr H, Zimmermann P et al. A transmembrane C-terminal fragment of syndecan-1 is generated by the metalloproteinase ADAM17 and promotes lung epithelial tumor cell migration and lung metastasis formation. Cell Mol.Life Sci. 2015;72:3783–3801.
   PubMed Web of Science ®Google Scholar
• Huang Y, Benaich N, Tape C, Kwok HF, Murphy G. Targeting the sheddase activity of ADAM17 by an anti-ADAM17 antibody D1(A12) inhibits head and neck squamous cell carcinoma cell proliferation and motility via blockage of bradykinin induced HERs transactivation. Int.J.Biol.Sci. 2014;10:702–714.
   PubMed Web of Science ®Google Scholar
• Duffy MJ, Mullooly M, O'Donovan N, Sukor S, Crown J, Pierce A, McGowan PM. The ADAMs family of proteases: new biomarkers and therapeutic targets for cancer? Clin.Proteomics. 2011;8:9.
   PubMedGoogle Scholar
• Peschon JJ, Slack JL, Reddy P, Stocking KL, Sunnarborg SW, Lee DC, Russell WE, Castner BJ, Johnson RS, Fitzner JN et al.An essential role for ectodomain shedding in mammalian development. Science 1998;282:1281–1284.
   PubMed Web of Science ®Google Scholar
• Tsai YH, VanDussen KL, Sawey ET, Wade AW, Kasper C, Rakshit S, Bhatt RG, Stoeck A, Maillard I, Crawford HC et al. ADAM10 regulates Notch function in intestinal stem cells of mice. Gastroenterology 2014;147:822–834.
   PubMed Web of Science ®Google Scholar
• Gelling RW, Yan W, Al-Noori S, Pardini A, Morton GJ, Ogimoto K, Schwartz MW, Dempsey PJ. Deficiency of TNFalpha converting enzyme (TACE/ADAM17) causes a lean, hypermetabolic phenotype in mice. Endocrinology 2008;149:6053–6064.
   PubMed Web of Science ®Google Scholar
• Horiuchi K, Kimura T, Miyamoto T, Miyamoto K, Akiyama H, Takaishi H, Morioka H, Nakamura T, Okada Y, Blobel CP et al. Conditional inactivation of TACE by a Sox9 promoter leads to osteoporosis and increased granulopoiesis via dysregulation of IL-17 and G-CSF. J.Immunol. 2009;182:2093–2101.
   PubMed Web of Science ®Google Scholar
• Weskamp G, Mendelson K, Swendeman S, Le Gall S, Ma Y, Lyman S, Hinoki A, Eguchi S, Guaiquil V, Horiuchi K et al. Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes. Circ.Res. 2010;%19;106:932–940.
   PubMed Web of Science ®Google Scholar
• Horiuchi K, Kimura T, Miyamoto T, Takaishi H, Okada Y, Toyama Y, Blobel CP. Cutting edge: TNF-alpha-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock. J Immunol. 2007;179:2686–2689.
   PubMed Web of Science ®Google Scholar
• Dreymueller D, Martin C, Kogel T, Pruessmeyer J, Hess FM, Horiuchi K, Uhlig S, Ludwig A. Lung endothelial ADAM17 regulates the acute inflammatory response to lipopolysaccharide. EMBO Mol.Med. 2012;4:412–423.
   PubMed Web of Science ®Google Scholar
• Jones JC, Rustagi S, Dempsey PJ. ADAM Proteases and Gastrointestinal Function. Annu.Rev.Physiol 2016;78:243–276.
   PubMed Web of Science ®Google Scholar
• Feng Y, Tsai YH, Xiao W, Ralls MW, Stoeck A, Wilson CL, Raines EW, Teitelbaum DH, Dempsey PJ. Loss of ADAM17-Mediated Tumor Necrosis Factor Alpha Signaling in Intestinal Cells Attenuates Mucosal Atrophy in a Mouse Model of Parenteral Nutrition. Mol.Cell Biol. 2015;35:3604–3621.
   PubMed Web of Science ®Google Scholar
• Bender M, Hofmann S, Stegner D, Chalaris A, Bosl M, Braun A, Scheller J, Rose-John S, Nieswandt B. Differentially regulated GPVI ectodomain shedding by multiple platelet-expressed proteinases. Blood. 2010;116:3347–3355.
   PubMed Web of Science ®Google Scholar
• Santos-Martinez MJ, Medina C, Jurasz P, Radomski MW. Role of metalloproteinases in platelet function. Thromb.Res. 2008;121:535–542.
   PubMed Web of Science ®Google Scholar
• Blaydon DC, Biancheri P, Di WL, Plagnol V, Cabral RM, Brooke MA, van Heel DA, Ruschendorf F, Toynbee M, Walne A et al. Inflammatory skin and bowel disease linked to ADAM17 deletion. N.Engl.J.Med. 2011;365:1502–1508.
   PubMed Web of Science ®Google Scholar
• Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, Snellinx A, Craessaerts K, Thathiah A, Tesseur I et al. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J.Neurosci. 2010;30:4833–4844.
   PubMed Web of Science ®Google Scholar
• Fahrenholz F, Gilbert S, Kojro E, Lammich S, Postina R. Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure. Ann.N.Y.Acad.Sci. 2000;920:215–22.:215–222.
   PubMed Web of Science ®Google Scholar
• Postina R, Schroeder A, Dewachter I, Bohl J, Schmitt U, Kojro E, Prinzen C, Endres K, Hiemke C, Blessing M et al.A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin.Invest. 2004;113:1456–1464.
   PubMed Web of Science ®Google Scholar
• Glomski K, Monette S, Manova K, De SB, Saftig P, Blobel CP. Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures. Blood 2011;118:1163–1174.
   PubMed Web of Science ®Google Scholar
• Mathews JA, Ford J, Norton S, Kang D, Dellinger A, Gibb DR, Ford AQ, Massay H, Kepley CL, Scherle P et al. A potential new target for asthma therapy: a disintegrin and metalloprotease 10 (ADAM10) involvement in murine experimental asthma. Allergy 2011;66:1193–1200.
   PubMed Web of Science ®Google Scholar
• Gibb DR, El Shikh M, Kang DJ, Rowe WJ, El Sayed R, Cichy J, Yagita H, Tew JG, Dempsey PJ, Crawford HC et al. ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo. J.Exp.Med. 2010;207:623–635.
   PubMed Web of Science ®Google Scholar
• van der Vorst EP, Jeurissen M, Wolfs IM, Keijbeck A, Theodorou K, Wijnands E, Schurgers L, Weber S, Gijbels MJ, Hamers AA et al. Myeloid A disintegrin and metalloproteinase domain 10 deficiency modulates atherosclerotic plaque composition by shifting the balance from inflammation toward fibrosis. Am.J.Pathol. 2015;185:1145–1155.
   PubMed Web of Science ®Google Scholar
• Inoshima N, Wang Y, Bubeck WJ. Genetic requirement for ADAM10 in severe Staphylococcus aureus skin infection. J.Invest Dermatol. 2012;132:1513–1516.
   PubMed Web of Science ®Google Scholar
• Inoshima I, Inoshima N, Wilke GA, Powers ME, Frank KM, Wang Y, Bubeck WJ. A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice. Nat.Med. 2011;17:1310–1314.
   PubMed Web of Science ®Google Scholar
• Zhang W, Liu S, Liu K, Ji B, Wang Y, Liu Y. Knockout of ADAM10 enhances sorafenib antitumor activity of hepatocellular carcinoma in vitro and in vivo. Oncol.Rep. 2014;32:1913–1922.
   PubMed Web of Science ®Google Scholar
• Tripathy D, Daniele G, Fiorentino TV, Perez-Cadena Z, Chavez-Velasquez A, Kamath S, Fanti P, Jenkinson C, Andreozzi F, Federici M et al. Pioglitazone improves glucose metabolism and modulates skeletal muscle TIMP-3-TACE dyad in type 2 diabetes mellitus: a randomised, double-blind, placebo-controlled, mechanistic study. Diabetologia 2013;56:2153–2163.
   PubMed Web of Science ®Google Scholar
• Schwarz J, Broder C, Helmstetter A, Schmidt S, Yan I, Muller M, Schmidt-Arras D, Becker-Pauly C, Koch-Nolte F, Mittrucker HW et al. Short-term TNFalpha shedding is independent of cytoplasmic phosphorylation or furin cleavage of ADAM17. Biochim.Biophys.Acta 2013;1833:3355–3367.
   PubMed Web of Science ®Google Scholar
• Adrain C, Zettl M, Christova Y, Taylor N, Freeman M. Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science 2012;335:225–228.
   PubMed Web of Science ®Google Scholar
• Maretzky T, McIlwain DR, Issuree PD, Li X, Malapeira J, Amin S, Lang PA, Mak TW, Blobel CP. iRhom2 controls the substrate selectivity of stimulated ADAM17-dependent ectodomain shedding. Proc.Natl.Acad.Sci.U.S.A 2013;110:11433–11438.
   PubMed Web of Science ®Google Scholar
• Li X, Maretzky T, Weskamp G, Monette S, Qing X, Issuree PD, Crawford HC, McIlwain DR, Mak TW, Salmon JE et al. iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling. Proc.Natl.Acad.Sci.U.S.A 2015;112:6080–6085.
   PubMed Web of Science ®Google Scholar
• Jouannet S, Saint-Pol J, Fernandez L, Nguyen V, Charrin S, Boucheix C, Brou C, Milhiet PE, Rubinstein E. TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization. Cell Mol.Life Sci. 2016;73:1895–1915.
   PubMed Web of Science ®Google Scholar
• Noy PJ, Yang J, Reyat JS, Matthews AL, Charlton AE, Furmston J, Rogers DA, Rainger GE, Tomlinson MG. TspanC8 Tetraspanins and A Disintegrin and Metalloprotease 10 (ADAM10) interact via their extracellular regions: Evidence for distinct binding mechanisms for different TspanC8 proteins. J Biol.Chem. 2016;291:3145–3157.
   PubMed Web of Science ®Google Scholar
• Dusterhoft S, Jung S, Hung CW, Tholey A, Sonnichsen FD, Grotzinger J, Lorenzen I. 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;135:5776–5781.
   PubMed Web of Science ®Google Scholar
• Willems SH, Tape CJ, Stanley PL, Taylor NA, Mills IG, Neal DE, McCafferty J, Murphy G. Thiol isomerases negatively regulate the cellular shedding activity of ADAM17. Biochem.J. 2010;428:439–450.
   PubMed Web of Science ®Google Scholar
• Le Gall SM, Maretzky T, Issuree PD, Niu XD, Reiss K, Saftig P, Khokha R, Lundell D, Blobel CP. ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site. J.Cell Sci. 2010;123:3913–3922.
   PubMed Web of Science ®Google Scholar
• Kwok HF, Botkjaer KA, Tape CJ, Huang Y, McCafferty J, Murphy G. Development of a 'mouse and human cross-reactive' affinity-matured exosite inhibitory human antibody specific to TACE (ADAM17) for cancer immunotherapy. Protein Eng Des Sel 2014;27:179–190.
   PubMed Web of Science ®Google Scholar
• Caiazza F, McGowan PM, Mullooly M, Murray A, Synnott N, O'Donovan N, Flanagan L, Tape CJ, Murphy G, Crown J et al. Targeting ADAM-17 with an inhibitory monoclonal antibody has antitumour effects in triple-negative breast cancer cells. Br.J.Cancer 2015;112:1895–1903.
   PubMed Web of Science ®Google Scholar
• Atapattu L, Saha N, Llerena C, Vail ME, Scott AM, Nikolov DB, Lackmann M, Janes PW. Antibodies binding the ADAM10 substrate recognition domain inhibit Eph function. J Cell Sci. 2012;125:6084–6093.
   PubMed Web of Science ®Google Scholar
• Schlomann U, Koller G, Conrad C, Ferdous T, Golfi P, Garcia AM, Hofling S, Parsons M, Costa P, Soper R et al. ADAM8 as a drug target in pancreatic cancer. Nat.Commun. 2015;6:6175.
   PubMed Web of Science ®Google Scholar
• Deng L, Chen J, Jiang X et al. A Synthetic Adam8 Inhibitor Peptide Attenuates Airway Pathologies In Ovalbumin-Sensitized Mice Via Suppression Of Inflammation Mediated By Th2 Cytokines [abstract]. Am J Respir Crit Care Med 2013;A2622.
   PubMed Web of Science ®Google Scholar
• Chen XT, Ghavimi B, Corbett RL, Xue CB, Liu RQ, Covington MB, Qian M, Vaddi KG, Christ DD, Hartman KD et al. A new 4-(2-methylquinolin-4-ylmethyl)phenyl P1' group for the beta-amino hydroxamic acid derived TACE inhibitors. Bioorg.Med.Chem.Lett. 2007;17:1865–1870.
   PubMed Web of Science ®Google Scholar
• Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, Reddy P, Wolfson MF, Rauch CT, Castner BJ et al. Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc.Natl.Acad.Sci.U.S.A 1998;95:3408–3412.
   PubMed Web of Science ®Google Scholar
• Moss ML, Rasmussen FH, Nudelman R, Dempsey PJ, Williams J. Fluorescent substrates useful as high-throughput screening tools for ADAM9. Comb.Chem.High Throughput.Screen. 2010;13:358–365.
   PubMed Web of Science ®Google Scholar
• Ludwig A, Hundhausen C, Lambert MH, Broadway N, Andrews RC, Bickett DM, Leesnitzer MA, Becherer JD. Metalloproteinase inhibitors for the disintegrin-like metalloproteinases ADAM10 and ADAM17 that differentially block constitutive and phorbol ester-inducible shedding of cell surface molecules. Comb.Chem.High Throughput.Screen. 2005;8:161–171.
   PubMed Web of Science ®Google Scholar
• Groves MD, Puduvalli VK, Conrad CA, Gilbert MR, Yung WK, Jaeckle K, Liu V, Hess KR, Aldape KD, Levin VA. Phase II trial of temozolomide plus marimastat for recurrent anaplastic gliomas: a relationship among efficacy, joint toxicity and anticonvulsant status. J.Neurooncol. 2006;80:83–90.
   PubMed Web of Science ®Google Scholar
• Renkiewicz R, Qiu L, Lesch C, Sun X, Devalaraja R, Cody T, Kaldjian E, Welgus H, Baragi V. Broad-spectrum matrix metalloproteinase inhibitor marimastat-induced musculoskeletal side effects in rats. Arthritis Rheum. 2003;48:1742–1749.
   PubMed Web of Science ®Google Scholar
• Morimoto Y, Nishikawa K, Ohashi M. KB-R7785, a novel matrix metalloproteinase inhibitor, exerts its antidiabetic effect by inhibiting tumor necrosis factor-alpha production. Life Sci. 1997;61:795–803.
   PubMed Web of Science ®Google Scholar
• Witters L, Scherle P, Friedman S, Fridman J, Caulder E, Newton R, Lipton A. Synergistic inhibition with a dual epidermal growth factor receptor/HER-2/neu tyrosine kinase inhibitor and a disintegrin and metalloprotease inhibitor. Cancer Res. 2008;68:7083–7089.
   PubMed Web of Science ®Google Scholar
• Merchant NB, Voskresensky I, Rogers CM, Lafleur B, Dempsey PJ, Graves-Deal R, Revetta F, Foutch AC, Rothenberg ML, Washington MK et al. TACE/ADAM-17: a component of the epidermal growth factor receptor axis and a promising therapeutic target in colorectal cancer. Clin.Cancer Res. 2008;14:1182–1191.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Hegen M, Xu J, Keith JC, Jr., Jin G, Du X, Cummons T, Sheppard BJ, Sun L, Zhu Y et al. Characterization of (2R, 3S)-2-([[4-(2-butynyloxy)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide, a potent and selective inhibitor of TNF-alpha converting enzyme. Int.Immunopharmacol. 2004; %20;4:1845–1857.
   Google Scholar
• Qian M, Bai SA, Brogdon B, Wu JT, Liu RQ, Covington MB, Vaddi K, Newton RC, Fossler MJ, Garner CE et al. Pharmacokinetics and pharmacodynamics of DPC 333 ((2R)-2-((3R)-3-amino-3{4-[2-methyl-4-quinolinyl) methoxy] phenyl}-2-oxopyrrolidinyl)-N-hydroxy-4-methylpentanamide)), a potent and selective inhibitor of tumor necrosis factor alpha-converting enzyme in rodents, dogs, chimpanzees, and humans. Drug Metab Dispos. 2007;35:1916–1925.
   PubMed Web of Science ®Google Scholar
• Moss ML, Rasmussen FH. Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening. Anal.Biochem. 2007;366:144–148.
   PubMed Web of Science ®Google Scholar
• Moss ML, Sklair-Tavron L, Nudelman R. Drug insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis. Nat.Clin.Pract.Rheumatol. 2008;4:300–309.
   PubMedGoogle Scholar
• Thabet MM, Huizinga TW. Drug evaluation: apratastat, a novel TACE/MMP inhibitor for rheumatoid arthritis. Curr.Opin.Investig.Drugs 2006;7:1014–1019.
   PubMed Web of Science ®Google Scholar
• Buckley CA, Rouhani FN, Kaler M, Adamik B, Hawari FI, Levine SJ. Amino-terminal TACE prodomain attenuates TNFR2 cleavage independently of the cysteine switch. Am.J Physiol Lung Cell Mol.Physiol. 2005;288:L1132–L1138.
   PubMed Web of Science ®Google Scholar
• Li X, Yan Y, Huang W, Yang Y, Wang H, Chang L. The regulation of TACE catalytic function by its prodomain. Mol.Biol.Rep. 2009;36:641–651.
   PubMed Web of Science ®Google Scholar
• Li X, Yan Y, Huang W, Yang Y. The study of the inhibition of the recombinant TACE prodomain to endotoxemia in mice. Int.J.Mol.Sci. 2009;10:5442–5454.
   PubMed Web of Science ®Google Scholar
• Moss ML, Bomar M, Liu Q, Sage H, Dempsey P, Lenhart PM, Gillispie PA, Stoeck A, Wildeboer D, Bartsch JW et al. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J Biol.Chem. 2007;282:35712–35721.
   PubMed Web of Science ®Google Scholar
• Miller MA, Moss ML, Powell G, Petrovich R, Edwards L, Meyer AS, Griffith LG, Lauffenburger DA. Targeting autocrine HB-EGF signaling with specific ADAM12 inhibition using recombinant ADAM12 prodomain. Sci.Rep. 2015;5:15150.
   PubMed Web of Science ®Google Scholar
• Knapinska AM, Dreymuller D, Ludwig A, Smith L, Golubkov V, Sohail A, Fridman R, Giulianotti M, LaVoi TM, Houghten RA et al. SAR Studies of Exosite-Binding Substrate-Selective Inhibitors of A Disintegrin And Metalloprotease 17 (ADAM17) and Application as Selective in Vitro Probes. J.Med.Chem. 2015;58:5808–5824.
   PubMed Web of Science ®Google Scholar
• Minond D, Cudic M, Bionda N, Giulianotti M, Maida L, Houghten RA, Fields GB. Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates. J.Biol.Chem. 2012;287:36473–36487.
   PubMed Web of Science ®Google Scholar
• Goth CK, Halim A, Khetarpal SA, Rader DJ, Clausen H, Schjoldager KT. A systematic study of modulation of ADAM-mediated ectodomain shedding by site-specific O-glycosylation. Proc.Natl.Acad.Sci.U.S.A 2015;112:14623–14628.
   PubMed Web of Science ®Google Scholar
• Stawikowska R, Cudic M, Giulianotti M, Houghten RA, Fields GB, Minond D. Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates. J.Biol.Chem. 2013;288:22871–22879.
   PubMed Web of Science ®Google Scholar
• Amour A, Slocombe PM, Webster A, Butler M, Knight CG, Smith BJ, Stephens PE, Shelley C, Hutton M, Knauper V et al. TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 1998;435:39–44.
   PubMed Web of Science ®Google Scholar
• Wisniewska M, Goettig P, Maskos K, Belouski E, Winters D, Hecht R, Black R, Bode W. Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex. J.Mol.Biol. 2008;381:1307–1319.
   PubMed Web of Science ®Google Scholar
• Hewing NJ, Weskamp G, Vermaat J, Farage E, Glomski K, Swendeman S, Chan RV, Chiang MF, Khokha R, Anand-Apte B et al. Intravitreal injection of TIMP3 or the EGFR inhibitor erlotinib offers protection from oxygen-induced retinopathy in mice. Invest Ophthalmol.Vis.Sci. 2013;54:864–870.
   PubMed Web of Science ®Google Scholar
• Amour A, Knight CG, Webster A, Slocombe PM, Stephens PE, Knauper V, Docherty AJ, Murphy G. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 2000; %19;473:275–279.
   Google Scholar
• Lee MH, Verma V, Maskos K, Becherer JD, Knauper V, Dodds P, Amour A, Murphy G. The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. FEBS Lett. 2002;520:102–106.
   PubMed Web of Science ®Google Scholar
• Lee MH, Rapti M, Murphy G. Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme. J Biol.Chem. 2005;280:15967–15975.
   PubMed Web of Science ®Google Scholar
• Lee MH, Dodds P, Verma V, Maskos K, Knauper V, Murphy G. Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme. Biochem.J. 2003;371:369–376.
   PubMed Web of Science ®Google Scholar
• Muraguchi T, Takegami Y, Ohtsuka T, Kitajima S, Chandana EP, Omura A, Miki T, Takahashi R, Matsumoto N, Ludwig A et al. RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity. Nat.Neurosci. 2007;10:838–845.
   PubMed Web of Science ®Google Scholar
• Hong KJ, Wu DC, Cheng KH, Chen LT, Hung WC. RECK inhibits stemness gene expression and tumorigenicity of gastric cancer cells by suppressing ADAM-mediated Notch1 activation. J.Cell Physiol 2014;229:191–201.
   PubMed Web of Science ®Google Scholar
• Ludwig A, Martin C, Schumacher J, Hess FM, Uhlig S, Dreymueller D. Endothelial ADAM10 and ADAM17 independently promote endotoxin-induced acute lung injury. Am.J Respir.Crit Care Med. 2012;185:A2630.
   Google Scholar
• Skarja GA, Brown AL, Ho RK, May MH, Sefton MV. The effect of a hydroxamic acid-containing polymer on active matrix metalloproteinases. Biomaterials 2009;30:1890–1897.
   PubMed Web of Science ®Google Scholar
• Nakayama Y, Masuda T. Development of a polymeric matrix metalloproteinase inhibitor as a bioactive stent coating material for prevention of restenosis. J.Biomed.Mater.Res.B Appl.Biomater. 2007;80:260–267.
   PubMed Web of Science ®Google Scholar
• Cobos-Correa A, Trojanek JB, Diemer S, Mall MA, Schultz C. Membrane-bound FRET probe visualizes MMP12 activity in pulmonary inflammation. Nat.Chem.Biol. 2009;5:628–630.
   PubMed Web of Science ®Google Scholar
• Qin Y, Liu XJ, Li L, Liu XJ, Li Y, Gao RJ, Shao RG, Zhen YS. MMP-2/9-oriented combinations enhance antitumor efficacy of EGFR/HER2-targeting fusion proteins and gemcitabine. Oncol.Rep. 2014;32:121–130.
   PubMed Web of Science ®Google Scholar