A disintegrin and metalloprotease 17 in the cardiovascular and central nervous systems

Frontiers in Physiology

Volumn 7, Issue OCT, 2016, Pages

  Xu, Jiaxi ^a   Mukerjee, Snigdha ^a   A Silva Alves, Cristiane R ^b   Carvalho Galvão, Alynne ^b   Cruz, Josiane C ^b   Balarini, Camille M ^b   Braga, Valdir A ^b   Lazartigues, Eric ^a   França Silva, Maria S ^b  

^a LOUISIANA STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b FEDERAL UNIVERSITY OF PARAÍBA   (Brazil)

Author keywords

ACE2; Atherosclerosis; EGFR; Hypertension; Shedding; TACE; TNF

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; NOTCH RECEPTOR; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME INHIBITOR;

ATHEROSCLEROTIC PLAQUE; BRAIN INJURY; BRAIN TUMOR; CARDIOVASCULAR DISEASE; CARDIOVASCULAR SYSTEM; CENTRAL NERVOUS SYSTEM; HUMAN; NONHUMAN; PROTEIN FUNCTION; PROTEIN PROCESSING; RENIN ANGIOTENSIN ALDOSTERONE SYSTEM; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; VASCULAR REMODELING; VASCULARIZATION;

EID: 84995878343     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2016.00469     Document Type: Review

References (171)

1. Adrain, C., and Freeman, M. (2012). New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. Nat. Rev. Mol. Cell Biol. 13, 489-498. doi: 10.1038/nrm3392
2. Akatsu, T., Nakamura, M., Satoh, M., and Hiramori, K. (2003). Increased mRNA expression of tumour necrosis factor-a and its converting enzyme in circulating leucocytes of patients with acute myocardial infarction. Clin. Sci. 105, 39-44. doi: 10.1042/CS20020367
3. Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., et al. (1998). TNF-a converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 435, 39-44.
4. Anders, A., Gilbert, S., Garten, W., Postina, R., and Fahrenholz, F. (2001). Regulation of the a-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J. 15, 1837-1839. doi: 10.1096/fj.01-0007fje
5. Arndt, P. G., Strahan, B., Wang, Y., Long, C., Horiuchi, K., and Walcheck, B. (2011). Leukocyte ADAM17 regulates acute pulmonary inflammation. PLoS ONE 6:e19938. doi: 10.1371/journal.pone.0019938
6. Arribas, J., and Esselens, C. (2009). ADAM17 as a therapeutic target in multiple diseases. Curr. Pharm. Des. 15, 2319-2335. doi: 10.2174/138161209788682398
7. Asai, M., Hattori, C., Szabó, B., Sasagawa, N., Maruyama, K., Tanuma, S., et al. (2003). Putative function of ADAM9, ADAM10, and ADAM17 as APP a-secretase. Biochem. Biophys. Res. Commun. 301, 231-235. doi: 10.1016/S0006-291X(02)02999-6
8. Balarini, C. M., Leal, M. A., Gomes, I. B., Pereira, T. M., Gava, A. L., Meyrelles, S. S., et al. (2013). Sildenafil restores endothelial function in the apolipoprotein E knockout mouse. J. Transl. Med. 11:3 doi: 10.1186/1479-5876-11-3
9. Bandsma, R. H., Van Goor, H., Yourshaw, M., Horlings, R. K., Jonkman, M. F., Schölvinck, E. H., et al. (2015). Loss of ADAM17 is associated with severe multiorgan dysfunction. Hum. Pathol. 46, 923-928. doi: 10.1016/j.humpath.2015.02.010
10. Basu, R., Fan, D., Kandalam, V., Lee, J., Das, S. K., Wang, X., et al. (2012). Loss of Timp3 gene leads to abdominal aortic aneurysm formation in response to angiotensin II. J. Biol. Chem. 287, 44083-44096. doi: 10.1074/jbc.M112.425652
11. Basu, R., Lee, J., Morton, J. S., Takawale, A., Fan, D., Kandalam, V., et al. (2013). TIMP3 is the primary TIMP to regulate agonist-induced vascular remodelling and hypertension. Cardiovasc. Res. 98, 360-371. doi: 10.1093/cvr/cvt067
12. Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., et al. (1997). A metalloproteinase disintegrin that releases tumour-necrosis factor-a from cells. Nature 385, 729-733. doi: 10.1038/385729a0
13. Blobel, C. P. (2005). ADAMs: key components in EGFR signalling and development. Nat. Rev. Mol. Cell Biol. 6, 32-43. doi: 10.1038/nrm1548
14. Bodiga, S., Zhong, J. C., Wang, W., Basu, R., Lo, J., Liu, G. C., et al. (2011). Enhanced susceptibility to biomechanical stress in ACE2 null mice is prevented by loss of the p47(phox) NADPH oxidase subunit. Cardiovasc. Res. 91, 151-161. doi: 10.1093/cvr/cvr036
15. Britsch, S., Li, L., Kirchhoff, S., Theuring, F., Brinkmann, V., Birchmeier, C., et al. (1998). The ErbB2 and ErbB3 receptors and their ligand, neuregulin-1, are essential for development of the sympathetic nervous system. Genes Dev. 12, 1825-1836.
16. Canault, M., Peiretti, F., Kopp, F., Bonardo, B., Bonzi, M. F., Coudeyre, J. C., et al. (2006). The TNFa converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: possible contribution to elevated plasma levels of soluble TNF a receptors. Atherosclerosis 187, 82-91. doi: 10.1016/j.atherosclerosis.2005.08.031
17. Caolo, V., Swennen, G., Chalaris, A., Wagenaar, A., Verbruggen, S., Rose-John, S., et al. (2015). ADAM10 and ADAM17 have opposite roles during sprouting angiogenesis. Angiogenesis 18, 13-22. doi: 10.1007/s10456-014-9443-4
18. Chalaris, A., Rabe, B., Paliga, K., Lange, H., Laskay, T., Fielding, C. A., et al. (2007). Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils. Blood 110, 1748-1755. doi: 10.1182/blood-2007-01-067918
19. Chanthaphavong, R. S., Loughran, P. A., Lee, T. Y., Scott, M. J., and Billiar, T. R. (2012). A role for cGMP in inducible nitric-oxide synthase (iNOS)-induced tumor necrosis factor (TNF) a-converting enzyme (TACE/ADAM17) activation, translocation, and TNF receptor 1 (TNFR1) shedding in hepatocytes. J. Biol. Chem. 287, 35887-35898. doi: 10.1074/jbc.M112.365171
20. Davisson, R. L., Yang, G., Beltz, T. G., Cassell, M. D., Johnson, A. K., and Sigmund, C. D. (1998). The brain renin-angiotensin system contributes to the hypertension in mice containing both the human renin and human angiotensinogen transgenes. Circ. Res. 83, 1047-1058.
21. De Bellard, M. E., Ching, W., Gossler, A., and Bronner-Fraser, M. (2002). Disruption of segmental neural crest migration and ephrin expression in delta-1 null mice. Dev. Biol. 249, 121-130. doi: 10.1006/dbio.2002.0756
22. de Queiroz, T. M., Xia, H., Filipeanu, C. M., Braga, V. A., and Lazartigues, E. (2015). a-Lipoic acid reduces neurogenic hypertension by blunting oxidative stress-mediated increase in ADAM17. Am. J. Physiol. Heart Circ. Physiol. 309, H926-H934. doi: 10.1152/ajpheart.00259.2015
23. Dreymueller, D., Pruessmeyer, J., Groth, E., and Ludwig, A. (2012). The role of ADAM-mediated shedding in vascular biology. Eur. J. Cell Biol. 91, 472-485. doi: 10.1016/j.ejcb.2011.09.003
24. Edwards, D. R., Handsley, M. M., and Pennington, C. J. (2008). The ADAM metalloproteinases. Mol. Aspects Med. 29, 258-289. doi: 10.1016/j.mam.2008.08.001
25. Elliott, K. J., Bourne, A. M., Takayanagi, T., Takaguri, A., Kobayashi, T., Eguchi, K., et al. (2013). ADAM17 silencing by adenovirus encoding miRNA-embedded siRNA revealed essential signal transduction by angiotensin II in vascular smooth muscle cells. J. Mol. Cell. Cardiol. 62, 1-7. doi: 10.1016/j.yjmcc.2013.05.005
26. Fan, H., and Derynck, R. (1999). Ectodomain shedding of TGF-a and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades. EMBO J. 18, 6962-6972. doi: 10.1093/emboj/18.24.6962
27. Fan, H., Turck, C. W., and Derynck, R. (2003). Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-a converting enzyme and of an alternatively translated polypeptide. J. Biol. Chem. 278, 18617-18627. doi: 10.1074/jbc.M300331200
28. Federici, M., Hribal, M. L., Menghini, R., Kanno, H., Marchetti, V., Porzio, O., et al. (2005). Timp3 deficiency in insulin receptor-haploinsufficient mice promotes diabetes and vascular inflammation via increased TNF-a. J. Clin. Invest. 115, 3494-3505. doi: 10.1172/JCI26052
29. Feng, Y., Hans, C., McIlwain, E., Varner, K. J., and Lazartigues, E. (2012). Angiotensin-converting enzyme 2 over-expression in the central nervous system reduces angiotensin-II-mediated cardiac hypertrophy. PLoS ONE 7:e48910. doi: 10.1371/journal.pone.0048910
30. Franzke, C. W., Cobzaru, C., Triantafyllopoulou, A., Löffek, S., Horiuchi, K., Threadgill, D. W., et al. (2012). Epidermal ADAM17 maintains the skin barrier by regulating EGFR ligand-dependent terminal keratinocyte differentiation. J. Exp. Med. 209, 1105-1119. doi: 10.1084/jem.20112258
31. Freimann, S., Ben-Ami, I., Dantes, A., Ron-El, R., and Amsterdam, A. (2004). EGF-like factor epiregulin and amphiregulin expression is regulated by gonadotropins/cAMP in human ovarian follicular cells. Biochem. Biophys. Res. Commun. 324, 829-834. doi: 10.1016/j.bbrc.2004.09.129
32. Freitas Lima, L. C., Braga, V. A., do Socorro de França Silva, M., Cruz, J. C., Sousa Santos, S. H., de Oliveira Monteiro, M. M., et al. (2015). Adipokines, diabetes and atherosclerosis: an inflammatory association. Front. Physiol. 6:304. doi: 10.3389/fphys.2015.00304
33. Fujimori, K. E., Takeuchi, K., Yazaki, T., Uyemura, K., Nojyo, Y., and Tamamki, N. (2000). Expression of L1 and TAG-1 in the corticospinal, callosal, and hippocampal commissural neurons in the developing rat telencephalon as revealed by retrograde and in situ hybridization double labeling. J. Comp. Neurol. 417, 275-288. doi: 10.1002/(SICI)1096-9861(20000214)417:3 < 275::AID-CNE2>3.0.CO;2-7
34. Galazka, G., Windsor, L. J., Birkedal-Hansen, H., and Engler, J. A. (1996). APMA (4-aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cysteine-75 in the propeptide. Biochemistry 35, 11221-11227. doi: 10.1021/bi960618e
35. Garbers, C., Jänner, N., Chalaris, A., Moss, M. L., Floss, D. M., Meyer, D., et al. (2011). Species specificity of ADAM10 and ADAM17 proteins in interleukin-6 (IL-6) trans-signaling and novel role of ADAM10 in inducible IL-6 receptor shedding. J. Biol. Chem. 286, 14804-14811. doi: 10.1074/jbc.M111.229393
36. Gechtman, Z., Alonso, J. L., Raab, G., Ingber, D. E., and Klagsbrun, M. (1999). The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J. Biol. Chem. 274, 28828-28835.
37. Gelling, R. W., Yan, W., Al-Noori, S., Pardini, A., Morton, G. J., Ogimoto, K., et al. (2008). Deficiency of TNFa converting enzyme (TACE/ADAM17) causes a lean, hypermetabolic phenotype in mice. Endocrinology 149, 6053-6064. doi: 10.1210/en.2008-0775
38. Gibb, S. L., Zhao, Y., Potter, D., Hylin, M. J., Bruhn, R., Baimukanova, G., et al. (2015). TIMP3 Attenuates the loss of neural stem cells, mature neurons and neurocognitive dysfunction in traumatic brain injury. Stem Cells 33, 3530-3544. doi: 10.1002/stem.2189
39. Gilles, S., Zahler, S., Welsch, U., Sommerhoff, C. P., and Becker, B. F. (2003). Release of TNF-a during myocardial reperfusion depends on oxidative stress and is prevented by mast cell stabilizers. Cardiovasc. Res. 60, 608-616. doi: 10.1016/j.cardiores.2003.08.016
40. Giricz, O., Calvo, V., Peterson, E. A., Abouzeid, C. M., and Kenny, P. A. (2013). TACE-dependent TGFa shedding drives triple-negative breast cancer cell invasion. Int. J. Cancer 133, 2587-2595. doi: 10.1002/ijc.28295
41. Goddard, D. R., Bunning, R. A., and Woodroofe, M. N. (2001). Astrocyte and endothelial cell expression of ADAM 17 (TACE) in adult human CNS. Glia 34, 267-271. doi: 10.1002/glia.1060
42. Gonzales, P. E., Solomon, A., Miller, A. B., Leesnitzer, M. A., Sagi, I., and Milla, M. E. (2004). Inhibition of the tumor necrosis factor-a-converting enzyme by its pro domain. J. Biol. Chem. 279, 31638-31645. doi: 10.1074/jbc.M401311200
43. Gooz, M. (2010). ADAM-17: the enzyme that does it all. Crit. Rev. Biochem. Mol. Biol. 45, 146-169. doi: 10.3109/10409231003628015
44. Gravano, D. M., McLelland, B. T., Horiuchi, K., and Manilay, J. O. (2010). ADAM17 deletion in thymic epithelial cells alters aire expression without affecting T cell developmental progression. PLoS ONE 5:e13528. doi: 10.1371/journal.pone.0013528
45. Groot, A. J., Cobzaru, C., Weber, S., Saftig, P., Blobel, C. P., Kopan, R., et al. (2013). Epidermal ADAM17 is dispensable for notch activation. J. Invest. Dermatol. 133, 2286-2288. doi: 10.1038/jid.2013.162
46. Guinea-Viniegra, J., Zenz, R., Scheuch, H., Hnisz, D., Holcmann, M., Bakiri, L., et al. (2009). TNFa shedding and epidermal inflammation are controlled by Jun proteins. Genes Dev. 23, 2663-2674. doi: 10.1101/gad.543109
47. Gutiérrez-López, M. D., Gilsanz, A., Yáñez-Mo, M., Ovalle, S., Lafuente, E. M., Dominguez, C., et al. (2011). The sheddase activity of ADAM17/TACE is regulated by the tetraspanin CD9. Cell. Mol. Life Sci. 68, 3275-3292. doi: 10.1007/s00018-011-0639-0
48. Habets, R. A., Groot, A. J., Yahyanejad, S., Tiyanont, K., Blacklow, S. C., and Vooijs, M. (2015). Human NOTCH2 is resistant to ligand-independent activation by metalloprotease ADAM17. J. Biol. Chem. 290, 14705-14716. doi: 10.1074/jbc.M115.643676
49. Hinkle, C. L., Sunnarborg, S. W., Loiselle, D., Parker, C. E., Stevenson, M., Russell, W. E., et al. (2004). Selective roles for tumor necrosis factor a-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: the juxtamembrane stalk determines cleavage efficiency. J. Biol. Chem. 279, 24179-24188. doi: 10.1074/jbc.M312141200
50. Horiuchi, K., Kimura, T., Miyamoto, T., Miyamoto, K., Akiyama, H., Takaishi, H., et al. (2009). Conditional inactivation of TACE by a Sox9 promoter leads to osteoporosis and increased granulopoiesis via dysregulation of IL-17 and G-CSF. J. Immunol. 182, 2093-2101. doi: 10.4049/jimmunol.0802491
51. Horiuchi, K., Kimura, T., Miyamoto, T., Takaishi, H., Okada, Y., Toyama, Y., et al. (2007a). Cutting edge: TNF-a-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock. J. Immunol. 179, 2686-2689. doi: 10.4049/jimmunol.179.5.2686
52. Horiuchi, K., Le Gall, S., Schulte, M., Yamaguchi, T., Reiss, K., Murphy, G., et al. (2007b). Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx. Mol. Biol. Cell 18, 176-188. doi: 10.1091/mbc.E06-01-0014
53. Horiuchi, K., Zhou, H. M., Kelly, K., Manova, K., and Blobel, C. P. (2005). Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2. Dev. Biol. 283, 459-471. doi: 10.1016/j.ydbio.2005.05.004
54. Hurtado, O., Cárdenas, A., Lizasoain, I., Boscá, L., Leza, J. C., Lorenzo, P., et al. (2001). Up-regulation of TNF-a convertase (TACE/ADAM17) after oxygen-glucose deprivation in rat forebrain slices. Neuropharmacology 40, 1094-1102. doi: 10.1016/S0028-3908(01)00035-1
55. Hurtado, O., Lizasoain, I., Fernandez-Tome, P., Alvarez-Barrientos, A., Leza, J. C., Lorenzo, P., et al. (2002). TACE/ADAM17-TNF-a pathway in rat cortical cultures after exposure to oxygen-glucose deprivation or glutamate. J. Cereb. Blood Flow Metab. 22, 576-585. doi: 10.1097/00004647-200205000-00009
56. Itaya, Y., Suzuki, H., Matsukawa, S., Kondo, K., and Saruta, T. (1986). Central renin-angiotensin system and the pathogenesis of DOCA-salt hypertension in rats. Am. J. Physiol. 251, H261-H268.
57. Jackson, L. F., Qiu, T. H., Sunnarborg, S. W., Chang, A., Zhang, C., Patterson, C., et al. (2003). Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J. 22, 2704-2716. doi: 10.1093/emboj/cdg264
58. Jakovcevski, I., Djogo, N., Hölters, L. S., Szpotowicz, E., and Schachner, M. (2013). Transgenic overexpression of the cell adhesion molecule L1 in neurons facilitates recovery after mouse spinal cord injury. Neuroscience 252, 1-12. doi: 10.1016/j.neuroscience.2013.07.067
59. Kahn, J., Walcheck, B., Migaki, G. I., Jutila, M. A., and Kishimoto, T. K. (1998). Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell 92, 809-818.
60. Kalus, I., Bormann, U., Mzoughi, M., Schachner, M., and Kleene, R. (2006). Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth. J. Neurochem. 98, 78-88. doi: 10.1111/j.1471-4159.2006.03847.x
61. Kaneko, H., Anzai, T., Horiuchi, K., Morimoto, K., Anzai, A., Nagai, T., et al. (2011). Tumor necrosis factor-a converting enzyme inactivation ameliorates high-fat diet-induced insulin resistance and altered energy homeostasis. Circ. J. 75, 2482-2490. doi: 10.1253/circj.CJ-11-0182
62. Kärkkäinen, I., Rybnikova, E., Pelto-Huikko, M., and Huovila, A. P. (2000). Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS. Mol. Cell. Neurosci. 15, 547-560. doi: 10.1006/mcne.2000.0848
63. Kishimoto, T. K., Jutila, M. A., Berg, E. L., and Butcher, E. C. (1989). Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 245, 1238-1241.
64. Kleinbongard, P., Heusch, G., and Schulz, R. (2010). TNFa in atherosclerosis, myocardial ischemia/reperfusion and heart failure. Pharmacol. Ther. 127, 295-314. doi: 10.1016/j.pharmthera.2010.05.002
65. Kopan, R., and Ilagan, M. X. (2009). The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137, 216-233. doi: 10.1016/j.cell.2009.03.045
66. Küper, C., Bartels, H., Fraek, M. L., Beck, F. X., and Neuhofer, W. (2007). Ectodomain shedding of pro-TGF-a is required for COX-2 induction and cell survival in renal medullary cells exposed to osmotic stress. Am. J. Physiol. Cell Physiol. 293, C1971-C1982. doi: 10.1152/ajpcell.00404.2007
67. Lakhan, S. E., Kirchgessner, A., and Hofer, M. (2009). Inflammatory mechanisms in ischemic stroke: therapeutic approaches. J. Transl. Med. 7:97. doi: 10.1186/1479-5876-7-97
68. La Marca, R., Cerri, F., Horiuchi, K., Bachi, A., Feltri, M. L., Wrabetz, L., et al. (2011). TACE (ADAM17) inhibits Schwann cell myelination. Nat. Neurosci. 14, 857-865. doi: 10.1038/nn.2849
69. Lambert, D. W., Clarke, N. E., Hooper, N. M., and Turner, A. J. (2008). Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain. FEBS Lett. 582, 385-390. doi: 10.1016/j.febslet.2007.11.085
70. Lambert, D. W., Yarski, M., Warner, F. J., Thornhill, P., Parkin, E. T., Smith, A. I., et al. (2005). Tumor necrosis factor-a convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2). J. Biol. Chem. 280, 30113-30119. doi: 10.1074/jbc.M505111200
71. Lautrette, A., Li, S., Alili, R., Sunnarborg, S. W., Burtin, M., Lee, D. C., et al. (2005). Angiotensin II and EGF receptor cross-talk in chronic kidney diseases: a new therapeutic approach. Nat. Med. 11, 867-874. doi: 10.1038/nm1275
72. Leonard, J. D., Lin, F., and Milla, M. E. (2005). Chaperone-like properties of the prodomain of TNFa-converting enzyme (TACE) and the functional role of its cysteine switch. Biochem. J. 387, 797-805. doi: 10.1042/BJ20041727
73. Li, N., Boyd, K., Dempsey, P. J., and Vignali, D. A. (2007). Non-cell autonomous expression of TNF-a-converting enzyme ADAM17 is required for normal lymphocyte development. J. Immunol. 178, 4214-4221. doi: 10.4049/jimmunol.178.7.4214
74. Li, Q., Zhang, Z., Li, Z., Zhou, M., Liu, B., Pan, L., et al. (2013). ADAM17 is critical for multipolar exit and radial migration of neuronal intermediate progenitor cells in mice cerebral cortex. PLoS ONE 8:e65703. doi: 10.1371/journal.pone.0065703
75. Li, X., and Fan, H. (2004). Loss of ectodomain shedding due to mutations in the metalloprotease and cysteine-rich/disintegrin domains of the tumor necrosis factor-a converting enzyme (TACE). J. Biol. Chem. 279, 27365-27375. doi: 10.1074/jbc.M401690200
76. Li, X., Maretzky, T., Weskamp, G., Monette, S., Qing, X., Issuree, P. D., et al. (2015). iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling. Proc. Natl. Acad. Sci. U.S.A. 112, 6080-6085. doi: 10.1073/pnas.1505649112
77. Li, X., Yan, Y., Huang, W., Yang, Y., Wang, H., and Chang, L. (2009). The regulation of TACE catalytic function by its prodomain. Mol. Biol. Rep. 36, 641-651. doi: 10.1007/s11033-008-9224-5
78. Li, Y., Brazzell, J., Herrera, A., and Walcheck, B. (2006). ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding. Blood 108, 2275-2279. doi: 10.1182/blood-2006-02-005827
79. Limatola, C., and Ransohoff, R. M. (2014). Modulating neurotoxicity through CX3CL1/CX3CR1 signaling. Front. Cell. Neurosci. 8:229. doi: 10.3389/fncel.2014.00229
80. Lin, J., Lemke, C., Redies, C., Yan, X., Mix, E., Rolfs, A., et al. (2011). ADAM17 overexpression promotes angiogenesis by increasing blood vessel sprouting and pericyte number during brain microvessel development. Int. J. Dev. Biol. 55, 961-968. doi: 10.1387/ijdb.103210jl
81. Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R., and Wewer, U. M. (1999). Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch. J. Biol. Chem. 274, 13427-13433.
82. Long, C., Wang, Y., Herrera, A. H., Horiuchi, K., and Walcheck, B. (2010). In vivo role of leukocyte ADAM17 in the inflammatory and host responses during E. coli-mediated peritonitis. J. Leukoc. Biol. 87, 1097-1101. doi: 10.1189/jlb.1109763
83. Lu, Y., Jiang, F., Zheng, X., Katakowski, M., Buller, B., To, S. S., et al. (2011). TGF-β1 promotes motility and invasiveness of glioma cells through activation of ADAM17. Oncol. Rep. 25, 1329-1335. doi: 10.3892/or.2011.1195
84. Madrigal, J. L., García-Bueno, B., Caso, J. R., Pérez-Nievas, B. G., and Leza, J. C. (2006). Stress-induced oxidative changes in brain. CNS Neurol. Disord. Drug Targets 5, 561-568. doi: 10.2174/187152706778559327
85. Madrigal, J. L., Hurtado, O., Moro, M. A., Lizasoain, I., Lorenzo, P., Castrillo, A., et al. (2002). The increase in TNF-a levels is implicated in NF-kappaB activation and inducible nitric oxide synthase expression in brain cortex after immobilization stress. Neuropsychopharmacology 26, 155-163. doi: 10.1016/S0893-133X(01)00292-5
86. Maretzky, T., McIlwain, D. R., Issuree, P. D., Li, X., Malapeira, J., Amin, S., et al. (2013). iRhom2 controls the substrate selectivity of stimulated ADAM17-dependent ectodomain shedding. Proc. Natl. Acad. Sci. U.S.A. 110, 11433-11438. doi: 10.1073/pnas.1302553110
87. Maretzky, T., Schulte, M., Ludwig, A., Rose-John, S., Blobel, C., Hartmann, D., et al. (2005). L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol. Cell. Biol. 25, 9040-9053. doi: 10.1128/MCB.25.20.9040-9053.2005
88. Maskos, K., Fernandez-Catalan, C., Huber, R., Bourenkov, G. P., Bartunik, H., Ellestad, G. A., et al. (1998). Crystal structure of the catalytic domain of human tumor necrosis factor-a-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 95, 3408-3412.
89. Mechtersheimer, S., Gutwein, P., Agmon-Levin, N., Stoeck, A., Oleszewski, M., Riedle, S., et al. (2001). Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins. J. Cell Biol. 155, 661-673. doi: 10.1083/jcb.200101099
90. Menghini, R., Fiorentino, L., Casagrande, V., Lauro, R., and Federici, M. (2013). The role of ADAM17 in metabolic inflammation. Atherosclerosis 228, 12-17. doi: 10.1016/j.atherosclerosis.2013.01.024
91. Merlos-Suárez, A., Ruiz-Paz, S., Baselga, J., and Arribas, J. (2001). Metalloprotease-dependent protransforming growth factor-a ectodomain shedding in the absence of tumor necrosis factor-a-converting enzyme. J. Biol. Chem. 276, 48510-48517. doi: 10.1074/jbc.M103488200
92. Meyer, D., and Birchmeier, C. (1995). Multiple essential functions of neuregulin in development. Nature 378, 386-390. doi: 10.1038/378386a0
93. Meyer, D., Yamaai, T., Garratt, A., Riethmacher-Sonnenberg, E., Kane, D., Theill, L. E., et al. (1997). Isoform-specific expression and function of neuregulin. Development 124, 3575-3586.
94. Milla, M. E., Leesnitzer, M. A., Moss, M. L., Clay, W. C., Carter, H. L., Miller, A. B., et al. (1999). Specific sequence elements are required for the expression of functional tumor necrosis factor-a-converting enzyme (TACE). J. Biol. Chem. 274, 30563-30570.
95. Miller, F. D., and Gauthier, A. S. (2007). Timing is everything: making neurons versus glia in the developing cortex. Neuron 54, 357-369. doi: 10.1016/j.neuron.2007.04.019
96. Moriguchi, Y., Matsubara, H., Mori, Y., Murasawa, S., Masaki, H., Maruyama, K., et al. (1999). Angiotensin II-induced transactivation of epidermal growth factor receptor regulates fibronectin and transforming growth factor-β synthesis via transcriptional and posttranscriptional mechanisms. Circ. Res. 84, 1073-1084.
97. Moss, M. L., Jin, S. L., Milla, M. E., Bickett, D. M., Burkhart, W., Carter, H. L., et al. (1997). Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-a. Nature 385, 733-736. doi: 10.1038/385733a0
98. Mu, Y., Sundar, R., Thakur, N., Ekman, M., Gudey, S. K., Yakymovych, M., et al. (2011). TRAF6 ubiquitinates TGFβ type I receptor to promote its cleavage and nuclear translocation in cancer. Nat. Commun. 2:330. doi: 10.1038/ncomms1332
99. Munhoz, C. D., García-Bueno, B., Madrigal, J. L., Lepsch, L. B., Scavone, C., and Leza, J. C. (2008). Stress-induced neuroinflammation: mechanisms and new pharmacological targets. Braz. J. Med. Biol. Res. 41, 1037-1046. doi: 10.1590/S0100-879X2008001200001
100. Murthy, A., Shao, Y. W., Narala, S. R., Molyneux, S. D., Zúñiga-Pflucker, J. C., and Khokha, R. (2012). Notch activation by the metalloproteinase ADAM17 regulates myeloproliferation and atopic barrier immunity by suppressing epithelial cytokine synthesis. Immunity 36, 105-119. doi: 10.1016/j.immuni.2012.01.005
101. Nikolaidis, N. M., Gray, J. K., Gurusamy, D., Fox, W., Stuart, W. D., Huber, N., et al. (2010). Ron receptor tyrosine kinase negatively regulates TNFa production in alveolar macrophages by inhibiting NF-κB activity and ADAM17 production. Shock 33, 197-204. doi: 10.1097/SHK.0b013e3181ae8155
102. Niu, A., Wang, B., and Li, Y. P. (2015). TNFa shedding in mechanically stressed cardiomyocytes is mediated by Src activation of TACE. J. Cell. Biochem. 116, 559-565. doi: 10.1002/jcb.25006
103. Obama, T., Takayanagi, T., Kobayashi, T., Bourne, A. M., Elliott, K. J., Charbonneau, M., et al. (2015). Vascular induction of a disintegrin and metalloprotease 17 by angiotensin II through hypoxia inducible factor 1a. Am. J. Hypertens. 28, 10-14. doi: 10.1093/ajh/hpu094
104. Odenbach, J., Wang, X., Cooper, S., Chow, F. L., Oka, T., Lopaschuk, G., et al. (2011). MMP-2 mediates angiotensin II-induced hypertension under the transcriptional control of MMP-7 and TACE. Hypertension 57, 123-130. doi: 10.1161/HYPERTENSIONAHA.110.159525
105. Ohtsu, H., Dempsey, P. J., and Eguchi, S. (2006a). ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. Am. J. Physiol. Cell Physiol. 291, C1-10. doi: 10.1152/ajpcell.00620.2005
106. Ohtsu, H., Dempsey, P. J., Frank, G. D., Brailoiu, E., Higuchi, S., Suzuki, H., et al. (2006b). ADAM17 mediates epidermal growth factor receptor transactivation and vascular smooth muscle cell hypertrophy induced by angiotensin II. Arterioscler. Thromb. Vasc. Biol. 26, e133-e137. doi: 10.1161/01.ATV.0000236203.90331.d0
107. Palazuelos, J., Crawford, H. C., Klingener, M., Sun, B., Karelis, J., Raines, E. W., et al. (2014). TACE/ADAM17 is essential for oligodendrocyte development and CNS myelination. J. Neurosci. 34, 11884-11896. doi: 10.1523/JNEUROSCI.1220-14.2014
108. Patel, I. R., Attur, M. G., Patel, R. N., Stuchin, S. A., Abagyan, R. A., Abramson, S. B., et al. (1998). TNF-a convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-a. J. Immunol. 160, 4570-4579.
109. Patel, V. B., Bodiga, S., Basu, R., Das, S. K., Wang, W., Wang, Z., et al. (2012). Loss of angiotensin-converting enzyme-2 exacerbates diabetic cardiovascular complications and leads to systolic and vascular dysfunction: a critical role of the angiotensin II/AT1 receptor axis. Circ. Res. 110, 1322-1335. doi: 10.1161/CIRCRESAHA.112.268029
110. Patel, V. B., Clarke, N., Wang, Z., Fan, D., Parajuli, N., Basu, R., et al. (2014). Angiotensin II induced proteolytic cleavage of myocardial ACE2 is mediated by TACE/ADAM-17: a positive feedback mechanism in the RAS. J. Mol. Cell. Cardiol. 66, 167-176. doi: 10.1016/j.yjmcc.2013.11.017
111. Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., et al. (1998). An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284.
112. Plumb, J., McQuaid, S., Cross, A. K., Surr, J., Haddock, G., Bunning, R. A., et al. (2006). Upregulation of ADAM-17 expression in active lesions in multiple sclerosis. Mult. Scler. 12, 375-385. doi: 10.1191/135248506ms1276oa
113. Pruessmeyer, J., and Ludwig, A. (2009). The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer. Semin. Cell Dev. Biol. 20, 164-174. doi: 10.1016/j.semcdb.2008.09.005
114. Pucadyil, T. J., and Chattopadhyay, A. (2006). Role of cholesterol in the function and organization of G-protein coupled receptors. Prog. Lipid Res. 45, 295-333. doi: 10.1016/j.plipres.2006.02.002
115. Qi, H., Rand, M. D., Wu, X., Sestan, N., Wang, W., Rakic, P., et al. (1999). Processing of the notch ligand delta by the metalloprotease Kuzbanian. Science 283, 91-94.
116. Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., et al. (2000). Functional analysis of the domain structure of tumor necrosis factor-a converting enzyme. J. Biol. Chem. 275, 14608-14614. doi: 10.1074/jbc.275.19.14608
117. Reiss, K., Cornelsen, I., Husmann, M., Gimpl, G., and Bhakdi, S. (2011). Unsaturated fatty acids drive disintegrin and metalloproteinase (ADAM)-dependent cell adhesion, proliferation, and migration by modulating membrane fluidity. J. Biol. Chem. 286, 26931-26942. doi: 10.1074/jbc.M111.243485
118. Reiss, K., and Saftig, P. (2009). The "a disintegrin and metalloprotease" (ADAM) family of sheddases: physiological and cellular functions. Semin. Cell Dev. Biol. 20, 126-137. doi: 10.1016/j.semcdb.2008.11.002
119. Rizza, S., Copetti, M., Cardellini, M., Menghini, R., Pecchioli, C., Luzi, A., et al. (2015). A score including ADAM17 substrates correlates to recurring cardiovascular event in subjects with atherosclerosis. Atherosclerosis 239, 459-464. doi: 10.1016/j.atherosclerosis.2015.01.029
120. Roghani, M., Becherer, J. D., Moss, M. L., Atherton, R. E., Erdjument-Bromage, H., Arribas, J., et al. (1999). Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J. Biol. Chem. 274, 3531-3540.
121. Romera, C., Hurtado, O., Botella, S. H., Lizasoain, I., Cárdenas, A., Fernández-Tomé, P., et al. (2004). In vitro ischemic tolerance involves upregulation of glutamate transport partly mediated by the TACE/ADAM17-tumor necrosis factor-a pathway. J. Neurosci. 24, 1350-1357. doi: 10.1523/JNEUROSCI.1596-03.2004
122. Saftig, P., and Reiss, K. (2011). The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential? Eur. J. Cell Biol. 90, 527-535. doi: 10.1016/j.ejcb.2010.11.005
123. Sahin, U., Weskamp, G., Kelly, K., Zhou, H. M., Higashiyama, S., Peschon, J., et al. (2004). Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J. Cell Biol. 164, 769-779. doi: 10.1083/jcb.200307137
124. Sandgren, E. P., Luetteke, N. C., Palmiter, R. D., Brinster, R. L., and Lee, D. C. (1990). Overexpression of TGFa in transgenic mice: induction of epithelial hyperplasia, pancreatic metaplasia, and carcinoma of the breast. Cell 61, 1121-1135.
125. Satoh, M., Ishikawa, Y., Itoh, T., Minami, Y., Takahashi, Y., and Nakamura, M. (2008). The expression of TNF-a converting enzyme at the site of ruptured plaques in patients with acute myocardial infarction. Eur. J. Clin. Invest. 38, 97-105. doi: 10.1111/j.1365-2362.2007.01912.x
126. Satoh, M., Iwasaka, J., Nakamura, M., Akatsu, T., Shimoda, Y., and Hiramori, K. (2004). Increased expression of tumor necrosis factor-a converting enzyme and tumor necrosis factor-a in peripheral blood mononuclear cells in patients with advanced congestive heart failure. Eur. J. Heart Fail. 6, 869-875. doi: 10.1016/j.ejheart.2004.02.007
127. Satoh, M., Nakamura, M., Saitoh, H., Satoh, H., Maesawa, C., Segawa, I., et al. (1999). Tumor necrosis factor-a-converting enzyme and tumor necrosis factor-a in human dilated cardiomyopathy. Circulation 99, 3260-3265.
128. Scheller, J., Chalaris, A., Garbers, C., and Rose-John, S. (2011). ADAM17: a molecular switch to control inflammation and tissue regeneration. Trends Immunol. 32, 380-387. doi: 10.1016/j.it.2011.05.005
129. Schwarz, J., Schmidt, S., Will, O., Koudelka, T., Köhler, K., Boss, M., et al. (2014). Polo-like kinase 2, a novel ADAM17 signaling component, regulates tumor necrosis factor a ectodomain shedding. J. Biol. Chem. 289, 3080-3093. doi: 10.1074/jbc.M113.536847
130. Seals, D. F., and Courtneidge, S. A. (2003). The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17, 7-30. doi: 10.1101/gad.1039703
131. Serra, H., Chivite, I., Angulo-Urarte, A., Soler, A., Sutherland, J. D., Arruabarrena-Aristorena, A., et al. (2015). PTEN mediates Notch-dependent stalk cell arrest in angiogenesis. Nat. Commun. 6:7935. doi: 10.1038/ncomms8935
132. Shi, W., Chen, H., Sun, J., Buckley, S., Zhao, J., Anderson, K. D., et al. (2003). TACE is required for fetal murine cardiac development and modeling. Dev. Biol. 261, 371-380. doi: 10.1016/S0012-1606(03)00315-4
133. Shimoda, Y., Satoh, M., Nakamura, M., Akatsu, T., and Hiramori, K. (2005). Activated tumour necrosis factor-a shedding process is associated with in-hospital complication in patients with acute myocardial infarction. Clin. Sci. 108, 339-347. doi: 10.1042/CS20040229
134. Skovronsky, D. M., Fath, S., Lee, V. M., and Milla, M. E. (2001). Neuronal localization of the TNFa converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques. J. Neurobiol. 49, 40-46. doi: 10.1002/neu.1064
135. Soond, S. M., Everson, B., Riches, D. W., and Murphy, G. (2005). ERK-mediated phosphorylation of Thr735 in TNFa-converting enzyme and its potential role in TACE protein trafficking. J. Cell Sci. 118, 2371-2380. doi: 10.1242/jcs.02357
136. Srour, N., Lebel, A., McMahon, S., Fournier, I., Fugère, M., Day, R., et al. (2003). TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity. FEBS Lett. 554, 275-283. doi: 10.1016/S0014-5793(03)01159-1
137. Sun, X., Liang, J., Yao, X., Lu, C., Zhong, T., Hong, X., et al. (2015). The activation of EGFR promotes myocardial tumor necrosis factor-a production and cardiac failure in endotoxemia. Oncotarget 6, 35478-35495. doi: 10.18632/oncotarget.6071
138. Suzumura, A. (2013). Neuron-microglia interaction in neuroinflammation. Curr. Protein Pept. Sci. 14, 16-20. doi: 10.2174/1389203711314010004
139. Swendeman, S., Mendelson, K., Weskamp, G., Horiuchi, K., Deutsch, U., Scherle, P., et al. (2008). VEGF-A stimulates ADAM17-dependent shedding of VEGFR2 and crosstalk between VEGFR2 and ERK signaling. Circ. Res. 103, 916-918. doi: 10.1161/CIRCRESAHA.108.184416
140. Takayanagi, T., Kawai, T., Forrester, S. J., Obama, T., Tsuji, T., Fukuda, Y., et al. (2015). Role of epidermal growth factor receptor and endoplasmic reticulum stress in vascular remodeling induced by angiotensin II. Hypertension 65, 1349-1355. doi: 10.1161/HYPERTENSIONAHA.115.05344
141. Tang, J., Zarbock, A., Gomez, I., Wilson, C. L., Lefort, C. T., Stadtmann, A., et al. (2011). ADAM17-dependent shedding limits early neutrophil influx but does not alter early monocyte recruitment to inflammatory sites. Blood 118, 786-794. doi: 10.1182/blood-2010-11-321406
142. Tellier, E., Canault, M., Rebsomen, L., Bonardo, B., Juhan-Vague, I., Nalbone, G., et al. (2006). The shedding activity of ADAM17 is sequestered in lipid rafts. Exp. Cell Res. 312, 3969-3980. doi: 10.1016/j.yexcr.2006.08.027
143. van Hinsbergh, V. W., Eringa, E. C., and Daemen, M. J. (2015). Neovascularization of the atherosclerotic plaque: interplay between atherosclerotic lesion, adventitia-derived microvessels and perivascular fat. Curr. Opin. Lipidol. 26, 405-411. doi: 10.1097/MOL.0000000000000210
144. Van Wart, H. E., and Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. U.S.A. 87, 5578-5582.
145. Vernon, P. J., and Tang, D. (2013). Eat-me: autophagy, phagocytosis, and reactive oxygen species signaling. Antioxid. Redox Signal. 18, 677-691. doi: 10.1089/ars.2012.4810
146. Wakamatsu, Y., Maynard, T. M., Jones, S. U., and Weston, J. A. (1999). NUMB localizes in the basal cortex of mitotic avian neuroepithelial cells and modulates neuronal differentiation by binding to NOTCH-1. Neuron 23, 71-81.
147. Wang, J., Al-Lamki, R. S., Zhang, H., Kirkiles-Smith, N., Gaeta, M. L., Thiru, S., et al. (2003). Histamine antagonizes tumor necrosis factor (TNF) signaling by stimulating TNF receptor shedding from the cell surface and Golgi storage pool. J. Biol. Chem. 278, 21751-21760. doi: 10.1074/jbc.M212662200
148. Wang, L., de Kloet, A. D., Pati, D., Hiller, H., Smith, J. A., Pioquinto, D. J., et al. (2016). Increasing brain angiotensin converting enzyme 2 activity decreases anxiety-like behavior in male mice by activating central Mas receptors. Neuropharmacology 105, 114-123. doi: 10.1016/j.neuropharm.2015.12.026
149. Wang, S. E., Xiang, B., Guix, M., Olivares, M. G., Parker, J., Chung, C. H., et al. (2008). Transforming growth factor β engages TACE and ErbB3 to activate phosphatidylinositol-3 kinase/Akt in ErbB2-overexpressing breast cancer and desensitizes cells to trastuzumab. Mol. Cell. Biol. 28, 5605-5620. doi: 10.1128/MCB.00787-08
150. Wang, X., Oka, T., Chow, F. L., Cooper, S. B., Odenbach, J., Lopaschuk, G. D., et al. (2009). Tumor necrosis factor-a-converting enzyme is a key regulator of agonist-induced cardiac hypertrophy and fibrosis. Hypertension 54, 575-582. doi: 10.1161/HYPERTENSIONAHA.108.127670
151. Weskamp, G., Mendelson, K., Swendeman, S., Le Gall, S., Ma, Y., Lyman, S., et al. (2010). Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes. Circ. Res. 106, 932-940. doi: 10.1161/CIRCRESAHA.109.207415
152. Weskamp, G., Schlöndorff, J., Lum, L., Becherer, J. D., Kim, T. W., Saftig, P., et al. (2004). Evidence for a critical role of the tumor necrosis factor a convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J. Biol. Chem. 279, 4241-4249. doi: 10.1074/jbc.M307974200
153. West, C. M., Joseph, L., and Bhana, S. (2008). Epidermal growth factor receptor-targeted therapy. Br. J. Radiol. 1, S36-S44. doi: 10.1259/bjr/32798755
154. Wilson, C. L., Gough, P. J., Chang, C. A., Chan, C. K., Frey, J. M., Liu, Y., et al. (2013). Endothelial deletion of ADAM17 in mice results in defective remodeling of the semilunar valves and cardiac dysfunction in adults. Mech. Dev. 130, 272-289. doi: 10.1016/j.mod.2013.01.001
155. Wolfsberg, T. G., and White, J. M. (1996). ADAMs in fertilization and development. Dev. Biol. 180, 389-401. doi: 10.1006/dbio.1996.0313
156. Xia, H., and Lazartigues, E. (2008). Angiotensin-converting enzyme 2 in the brain: properties and future directions. J. Neurochem. 107, 1482-1494. doi: 10.1111/j.1471-4159.2008.05723.x
157. Xia, H., Sriramula, S., Chhabra, K. H., and Lazartigues, E. (2013). Brain angiotensin-converting enzyme type 2 shedding contributes to the development of neurogenic hypertension. Circ. Res. 113, 1087-1096. doi: 10.1161/CIRCRESAHA.113.301811
158. Xia, H., Suda, S., Bindom, S., Feng, Y., Gurley, S. B., Seth, D., et al. (2011). ACE2-mediated reduction of oxidative stress in the central nervous system is associated with improvement of autonomic function. PLoS ONE 6:e22682. doi: 10.1371/journal.pone.0022682
159. Xiao, F., Zimpelmann, J., Burger, D., Kennedy, C., Hébert, R. L., and Burns, K. D. (2016). Protein kinase C-delta mediates shedding of angiotensin-converting enzyme 2 from proximal tubular cells. Front. Pharmacol. 7:146. doi: 10.3389/fphar.2016.00146
160. Xu, P., and Derynck, R. (2010). Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation. Mol. Cell 37, 551-566. doi: 10.1016/j.molcel.2010.01.034
161. Xu, P., Liu, J., Sakaki-Yumoto, M., and Derynck, R. (2012). TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association. Sci. Signal. 5, ra34. doi: 10.1126/scisignal.2002689
162. Yemane, H., Busauskas, M., Burris, S. K., and Knuepfer, M. M. (2010). Neurohumoral mechanisms in deoxycorticosterone acetate (DOCA)-salt hypertension in rats. Exp. Physiol. 95, 51-55. doi: 10.1113/expphysiol.2008.046334
163. Zhan, L., Zheng, L., Hosoi, T., Okuma, Y., and Nomura, Y. (2015). Stress-induced neuroprotective effects of epiregulin and amphiregulin. PLoS ONE 10:e0118280. doi: 10.1371/journal.pone.0118280
164. Zhan, M., Jin, B., Chen, S. E., Reecy, J. M., and Li, Y. P. (2007). TACE release of TNF-a mediates mechanotransduction-induced activation of p38 MAPK and myogenesis. J. Cell Sci. 120, 692-701. doi: 10.1242/jcs.03372
165. Zhang, P., Shen, M., Fernandez-Patron, C., and Kassiri, Z. (2016). ADAMs family and relatives in cardiovascular physiology and pathology. J. Mol. Cell. Cardiol. 93, 186-199. doi: 10.1016/j.yjmcc.2015.10.031
166. Zhang, Q., Thomas, S. M., Lui, V. W., Xi, S., Siegfried, J. M., Fan, H., et al. (2006). Phosphorylation of TNF-a converting enzyme by gastrin-releasing peptide induces amphiregulin release and EGF receptor activation. Proc. Natl. Acad. Sci. U.S.A. 103, 6901-6906. doi: 10.1073/pnas.0509719103
167. Zhang, Y., Hegen, M., Xu, J., Keith, J. C. Jr., Jin, G., Du, X., et al. (2004). Characterization of (2R, 3S)-2-([[4-(2-butynyloxy)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide, a potent and selective inhibitor of TNF-a converting enzyme. Int. Immunopharmacol. 4, 1845-1857. doi: 10.1016/j.intimp.2004.08.003
168. Zhang, Z., Kolls, J. K., Oliver, P., Good, D., Schwarzenberger, P. O., Joshi, M. S., et al. (2000). Activation of tumor necrosis factor-a-converting enzyme-mediated ectodomain shedding by nitric oxide. J. Biol. Chem. 275, 15839-15844. doi: 10.1074/jbc.M000604200
169. Zhang, Z., Oliver, P., Lancaster, J. R. Jr., Schwarzenberger, P. O., Joshi, M. S., Cork, J., et al. (2001). Reactive oxygen species mediate tumor necrosis factor a-converting, enzyme-dependent ectodomain shedding induced by phorbol myristate acetate. FASEB J. 15, 303-305. doi: 10.1096/fj.00-0371fje
170. Zheng, D. Y., Zhao, J., Yang, J. M., Wang, M., and Zhang, X. T. (2016). Enhanced ADAM17 expression is associated with cardiac remodeling in rats with acute myocardial infarction. Life Sci. 151, 61-69. doi: 10.1016/j.lfs.2016.02.097
171. Zheng, X., Jiang, F., Katakowski, M., Lu, Y., and Chopp, M. (2012). ADAM17 promotes glioma cell malignant phenotype. Mol. Carcinog. 51, 150-164. doi: 10.1002/mc.20772