ADAMTS-7 promotes vascular smooth muscle cells proliferation in vitro and in vivo

Science China Life Sciences

Volumn 58, Issue 7, 2015, Pages 674-681

  Zhang, Lu ^a,b   Yu, Fang ^a,b   Wang, Li ^a,b   Zheng, JinGang ^c   Du, YaoYao ^a,b   Huang, YaQian ^a,b   Liu, Bo ^a,b   Wang, Xian ^a,b   Kong, Wei ^a,b  

^a PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^b BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

^c CHINA JAPAN FRIENDSHIP HOSPITAL   (China)

Author keywords

ADAMTS 7; proliferation; vascular smooth muscle cell

Indexed keywords

RATTUS;

ADAM PROTEIN; ADAMTS7 PROTEIN, RAT;

ANIMAL; CELL PROLIFERATION; CYTOLOGY; GENE SILENCING; GENETICS; IN VITRO STUDY; MALE; PHYSIOLOGY; RAT; SPRAGUE DAWLEY RAT; VASCULAR SMOOTH MUSCLE;

ADAM PROTEINS; ANIMALS; CELL PROLIFERATION; GENE KNOCKDOWN TECHNIQUES; IN VITRO TECHNIQUES; MALE; MUSCLE, SMOOTH, VASCULAR; RATS; RATS, SPRAGUE-DAWLEY;

EID: 84937816053     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-015-4843-2     Document Type: Article

References (41)

1. Lacolley P, Regnault V, Nicoletti A, Li Z, Michel JB. The vascular smooth muscle cell in arterial pathology: a cell that can take on multiple roles. Cardiovasc Res, 2012, 95: 194–204
2. Rudijanto A. The role of vascular smooth muscle cells on the pathogenesis of atherosclerosis. Acta Med Indones, 2007, 39: 86–93
3. Hao H, Gabbiani G, Bochaton-Piallat ML. Arterial smooth muscle cell heterogeneity: implications for atherosclerosis and restenosis development. Arterioscler Thromb Vasc Biol, 2003, 23: 1510–1520
4. Shi N, Chen SY. Mechanisms simultaneously regulate smooth muscle proliferation and differentiation. J Biomed Res, 2014, 28: 40–46
5. Hu J, Van den Steen PE, Sang QX, Opdenakker G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat Rev Drug Discov, 2007, 6: 480–498
6. Newby AC. Matrix metalloproteinases regulate migration, proliferation, and death of vascular smooth muscle cells by degrading matrix and non-matrix substrates. Cardiovasc Res, 2006, 69: 614–624
7. Sluijter JP, de Kleijn DP, Pasterkamp G. Vascular remodeling and protease inhibition-bench to bedside. Cardiovasc Res, 2006, 69: 595–603
8. Dwivedi A, Slater SC, George SJ. Mmp-9 and -12 cause n-cadherin shedding and thereby beta-catenin signalling and vascular smooth muscle cell proliferation. Cardiovasc Res, 2009, 81: 178–186
9. Liu CJ, Kong W, Ilalov K, Yu S, Xu K, Prazak L, Fajardo M, Sehgal B, Di Cesare PE. Adamts-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein. FASEB J, 2006, 20: 988–990
10. Wang L, Zheng J, Bai X, Liu B, Liu CJ, Xu Q, Zhu Y, Wang N, Kong W, Wang X. Adamts-7 mediates vascular smooth muscle cell migration and neointima formation in balloon-injured rat arteries. Circ Res, 2009, 104: 688–698
11. Wang L, Zheng J, Du Y, Huang Y, Li J, Liu B, Liu CJ, Zhu Y, Gao Y, Xu Q, Kong W, Wang X. Cartilage oligomeric matrix protein maintains the contractile phenotype of vascular smooth muscle cells by interacting with alpha(7)beta(1) integrin. Circ Res, 106: 514–525
12. Du Y, Gao C, Liu Z, Wang L, Liu B, He F, Zhang T, Wang Y, Wang X, Xu M, Luo GZ, Zhu Y, Xu Q, Wang X, Kong W. Upregulation of a disintegrin and metalloproteinase with thrombospondin motifs-7 by mir-29 repression mediates vascular smooth muscle calcification. Arterioscler Thromb Vasc Biol, 2012, 32: 2580–2588
13. Du Y, Wang Y, Wang L, Liu B, Tian Q, Liu CJ, Zhang T, Xu Q, Zhu Y, Ake O, Qi Y, Tang C, Kong W, Wang X. Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2 novelty and significance. Circ Res, 2011, 108: 917–928
14. Schunkert H, Konig IR, Kathiresan S, Reilly MP, Assimes TL, Holm H, Preuss M, Stewart AF, Barbalic M, Gieger C, Absher D, Aherrahrou Z, Allayee H, Altshuler D, Anand SS, Andersen K, Anderson JL, Ardissino D, Ball SG, Balmforth AJ, Barnes TA, Becker DM, Becker LC, Berger K, Bis JC, Boekholdt SM, Boerwinkle E, Braund PS, Brown MJ, Burnett MS, Buysschaert I, Cardiogenics, Carlquist JF, Chen L, Cichon S, Codd V, Davies RW, Dedoussis G, Dehghan A, Demissie S, Devaney JM, Diemert P, Do R, Doering A, Eifert S, Mokhtari NE, Ellis SG, Elosua R, Engert JC, Epstein SE, de Faire U, Fischer M, Folsom AR, Freyer J, Gigante B, Girelli D, Gretarsdottir S, Gudnason V, Gulcher JR, Halperin E, Hammond N, Hazen SL, Hofman A, Horne BD, Illig T, Iribarren C, Jones GT, Jukema JW, Kaiser MA, Kaplan LM, Kastelein JJ, Khaw KT, Knowles JW, Kolovou G, Kong A, Laaksonen R, Lambrechts D, Leander K, Lettre G, Li M, Lieb W, Loley C, Lotery AJ, Mannucci PM, Maouche S, Martinelli N, McKeown PP, Meisinger C, Meitinger T, Melander O, Merlini PA, Mooser V, Morgan T, Muhleisen TW, Muhlestein JB, Munzel T, Musunuru K, Nahrstaedt J, Nelson CP, Nothen MM, Olivieri O, Patel RS, Patterson CC, Peters A, Peyvandi F, Qu L, Quyyumi AA, Rader DJ, Rallidis LS, Rice C, Rosendaal FR, Rubin D, Salomaa V, Sampietro ML, Sandhu MS, Schadt E, Schafer A, Schillert A, Schreiber S, Schrezenmeir J, Schwartz SM, Siscovick DS, Sivananthan M, Sivapalaratnam S, Smith A, Smith TB, Snoep JD, Soranzo N, Spertus JA, Stark K, Stirrups K, Stoll M, Tang WH, Tennstedt S, Thorgeirsson G, Thorleifsson G, Tomaszewski M, Uitterlinden AG, van Rij AM, Voight BF, Wareham NJ, Wells GA, Wichmann HE, Wild PS, Willenborg C, Witteman JC, Wright BJ, Ye S, Zeller T, Ziegler A, Cambien F, Goodall AH, Cupples LA, Quertermous T, Marz W, Hengstenberg C, Blankenberg S, Ouwehand WH, Hall AS, Deloukas P, Thompson JR, Stefansson K, Roberts R, Thorsteinsdottir U, O’Donnell CJ, McPherson R, Erdmann J, Consortium CA, Samani NJ. Large-scale association analysis identifies 13 new susceptibility loci for coronary artery disease. Nat Genet, 2011, 43: 333–338
15. Reilly MP, Li M, He J, Ferguson JF, Stylianou IM, Mehta NN, Burnett MS, Devaney JM, Knouff CW, Thompson JR, Horne BD, Stewart AF, Assimes TL, Wild PS, Allayee H, Nitschke PL, Patel RS, Consortium MIG, Consortium WTCC, Martinelli N, Girelli D, Quyyumi AA, Anderson JL, Erdmann J, Hall AS, Schunkert H, Quertermous T, Blankenberg S, Hazen SL, Roberts R, Kathiresan S, Samani NJ, Epstein SE, Rader DJ. Identification of adamts7 as a novel locus for coronary atherosclerosis and association of abo with myocardial infarction in the presence of coronary atherosclerosis: two genome-wide association studies. Lancet, 2011, 377: 383–392
16. Consortium CADCDG. A genome-wide association study in europeans and south asians identifies five new loci for coronary artery disease. Nat Genet, 2011, 43: 339–344
17. Pu X, Xiao Q, Kiechl S, Chan K, Ng FL, Gor S, Poston RN, Fang C, Patel A, Senver EC, Shaw-Hawkins S, Willeit J, Liu C, Zhu J, Tucker AT, Xu Q, Caulfield MJ, Ye S. Adamts7 cleavage and vascular smooth muscle cell migration is affected by a coronary-artery-disease-associated variant. Am J Hum Genet, 2013, 92: 366–374
18. Apte SS. A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (adamts) superfamily: functions and mechanisms. J Biol Chem, 2009, 284: 31493–31497
19. Luque A, Carpizo DR, Iruela-Arispe ML. Adamts1/meth1 inhibits endothelial cell proliferation by direct binding and sequestration of vegf165. J Biol Chem, 2003, 278: 23656–23665
20. Rocks N, Paulissen G, Quesada-Calvo F, Munaut C, Gonzalez ML, Gueders M, Hacha J, Gilles C, Foidart JM, Noel A, Cataldo DD. Adamts-1 metalloproteinase promotes tumor development through the induction of a stromal reaction in vivo. Cancer Res, 2008, 68: 9541–9550
21. Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, Little CB, Last K, Farmer PJ, Campbell IK, Fourie AM, Fosang AJ. Adamts5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature, 2005, 434: 648–652
22. Glasson SS, Askew R, Sheppard B, Carito B, Blanchet T, Ma HL, Flannery CR, Peluso D, Kanki K, Yang Z, Majumdar MK, Morris EA. Deletion of active adamts5 prevents cartilage degradation in a murine model of osteoarthritis. Nature, 2005, 434: 644–648
23. Tortorella MD, Burn TC, Pratta MA, Abbaszade I, Hollis JM, Liu R, Rosenfeld SA, Copeland RA, Decicco CP, Wynn R, Rockwell A, Yang F, Duke JL, Solomon K, George H, Bruckner R, Nagase H, Itoh Y, Ellis DM, Ross H, Wiswall BH, Murphy K, Hillman MC, Jr., Hollis GF, Newton RC, Magolda RL, Trzaskos JM, Arner EC. Purification and cloning of aggrecanase-1: a member of the adamts family of proteins. Science, 1999, 284: 1664–1666
24. Furlan M, Robles R, Solenthaler M, Lammle B. Acquired deficiency of von willebrand factor-cleaving protease in a patient with thrombotic thrombocytopenic purpura. Blood, 1998, 91: 2839–2846
25. Salter RC, Ashlin TG, Kwan AP, Ramji DP. Adamts proteases: key roles in atherosclerosis? J Mol Med (Berl), 2010, 88: 1203–1211
26. Jonsson-Rylander AC, Nilsson T, Fritsche-Danielson R, Hammarstrom A, Behrendt M, Andersson JO, Lindgren K, Andersson AK, Wallbrandt P, Rosengren B, Brodin P, Thelin A, Westin A, Hurt-Camejo E, Lee-Sogaard CH. Role of adamts-1 in atherosclerosis: Remodeling of carotid artery, immunohistochemistry, and proteolysis of versican. Arterioscler Thromb Vasc Biol, 2005, 25: 180–185
27. Sabatine MS, Ploughman L, Simonsen KL, Iakoubova OA, Kirchgessner TG, Ranade K, Tsuchihashi Z, Zerba KE, Long DU, Tong CH, Packard CJ, Pfeffer MA, Devlin JJ, Shepherd J, Campos H, Sacks FM, Braunwald E. Association between adamts1 matrix metalloproteinase gene variation, coronary heart disease, and benefit of statin therapy. Arterioscler Thromb Vasc Biol, 2008, 28: 562–567
28. Wagsater D, Bjork H, Zhu C, Bjorkegren J, Valen G, Hamsten A, Eriksson P. Adamts-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques. Atherosclerosis, 2008, 196: 514–522
29. Didangelos A, Mayr U, Monaco C, Mayr M. Novel role of adamts-5 protein in proteoglycan turnover and lipoprotein retention in atherosclerosis. J Biol Chem, 2012, 287: 19341–19345
30. Lindner V, Reidy MA. Proliferation of smooth muscle cells after vascular injury is inhibited by an antibody against basic fibroblast growth factor. Proc Natl Acad Sci USA, 1991, 88: 3739–3743
31. Ferns GA, Raines EW, Sprugel KH, Motani AS, Reidy MA, Ross R. Inhibition of neointimal smooth muscle accumulation after angioplasty by an antibody to PDGF. Science, 1991, 253: 1129–1132
32. Tsai S, Hollenbeck ST, Ryer EJ, Edlin R, Yamanouchi D, Kundi R, Wang C, Liu B, Kent KC. Tgf-beta through smad3 signaling stimulates vascular smooth muscle cell proliferation and neointimal formation. Am J Physiol Heart Circ Physiol, 2009, 297: H540–549
33. Min LJ, Mogi M, Li JM, Iwanami J, Iwai M, Horiuchi M. Aldosterone and angiotensin II synergistically induce mitogenic response in vascular smooth muscle cells. Circ Res, 2005, 97: 434–442
34. Grant MB, Wargovich TJ, Ellis EA, Caballero S, Mansour M, Pepine CJ. Localization of insulin-like growth factor I and inhibition of coronary smooth muscle cell growth by somatostatin analogues in human coronary smooth muscle cells. A potential treatment for restenosis? Circulation, 1994, 89: 1511–1517
35. Elledge SJ. Cell cycle checkpoints: preventing an identity crisis. Science, 1996, 274: 1664–1672
36. Koepp DM, Harper JW, Elledge SJ. How the cyclin became a cyclin: regulated proteolysis in the cell cycle. Cell, 1999, 97: 431–434
37. Vidal A, Koff A. Cell-cycle inhibitors: three families united by a common cause. Gene, 2000, 247: 1–15
38. Bendeck MP, Conte M, Zhang M, Nili N, Strauss BH, Farwell SM. Doxycycline modulates smooth muscle cell growth, migration, and matrix remodeling after arterial injury. Am J Pathol, 2002, 160: 1089–1095
39. Islam MM, Franco CD, Courtman DW, Bendeck MP. A nonantibiotic chemically modified tetracycline (CMT-3) inhibits intimal thickening. Am J Pathol, 2003, 163: 1557–1566
40. Cho A, Reidy MA. Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury. Circ Res, 2002, 91: 845–851
41. Galis ZS, Johnson C, Godin D, Magid R, Shipley JM, Senior RM, Ivan E. Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling. Circ Res, 2002, 91: 852–859