SEARCH

SEARCH BY CITATION

References

  • 1
    Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002; 2: 16174.
  • 2
    Shiomi T, Okada Y. MT1-MMP and MMP-7 in invasion and metastasis of human cancers. Cancer Metastasis Rev 2003; 22: 14552.
  • 3
    Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003; 17: 730.
  • 4
    Iba K, Albrechtsen R, Gilpin B et al. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to β1 integrin-dependent cell spreading. J Cell Biol 2000; 149: 114356.
  • 5
    Gaultier A, Cousin H, Darribere T, Alfandari D. ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J Biol Chem 2000; 277: 23 336–44.
  • 6
    Huovila AP, Turner AJ, Pelto-Huikko M, Karkkainen I, Ortiz RM. Shedding light on ADAM metalloproteinases. Trends Biochem Sci 2005; 30: 41322.
  • 7
    Izumi Y, Hirata M, Hasuwa H et al. A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J 1998; 17: 726072.
  • 8
    Asakura M, Kitakaze M, Takashima S et al. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat Med 2002; 8: 3540.
  • 9
    Mochizuki S, Shimoda M, Shiomi T, Fujii Y, Okada Y. ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3. Biochem Biophys Res Commun 2004; 315: 7984.
  • 10
    Millichip MI, Dallas DJ, Wu E, Dale S, McKie N. The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem Biophys Res Commun 1998; 245: 5948.
  • 11
    Roy R, Wewer UM, Zurakowski D, Pories SE, Moses MA. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. J Biol Chem 2004; 279: 51 323–30.
  • 12
    Martin J, Eynstone LV, Davies M, Williams JD, Steadman R. The role of ADAM 15 in glomerular mesangial cell migration. J Biol Chem 2002; 277: 33 683–9.
  • 13
    Russel DL, Doyle KM, Ochsner SA, Sandy JD, Richards JS. Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation. J Biol Chem 2003; 278: 42 330–9.
  • 14
    Somerville RP, Longpre JM, Jungers KA et al. Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1. J Biol Chem 2003; 278: 950313.
  • 15
    Tortorella MD, Burn TC, Pratta MA et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999; 284: 16646.
  • 16
    Tortorella MD, Pratta M, Liu RQ et al. Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4). J Biol Chem 2000; 275: 18 566–73.
  • 17
    Sandy JD, Westling J, Kenagy RD et al. Versican V1 proteolysis in human aorta in vivo occurs at the Glu441–Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4. J Biol Chem 2001; 276: 13 372–8.
  • 18
    Nakamura H, Fujii Y, Inoki I et al. Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. J Biol Chem 2000; 275: 38 885–90.
  • 19
    Levy GG, Nichols WC, Lian EC et al. Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature 2001; 413: 48894.
  • 20
    Kim IM, Ramakrishna S, Gusarova GA et al. The forkhead box m1 transcription factor is essential for embryonic development of pulmonary vasculature. J Biol Chem 2005; 280: 22 278–86.
  • 21
    Schlomann U, Rathke-Hartlieb S, Yamamoto S, Jockusch H, Bartsch JW. Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron–glia interactions during neurodegeneration. J Neurosci 2000; 20: 796471.
  • 22
    Sung SY, Kubo H, Shigemura K et al. Oxidative stress induces ADAM9 protein expression in human prostate cancer cells. Cancer Res 2006; 66: 951926.
  • 23
    Le Pabic H, Bonnier D, Wewer UM et al. ADAM12 in human liver cancers: TGF-β-regulated expression in stellate cells is associated with matrix remodeling. Hepatology 2003; 37: 105666.
  • 24
    Diaz-Rodriguez E, Montero JC, Esparis-Ogando A, Yuste L, Pandiella A. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-converting enzyme at threonine 735: a potential role in regulated shedding. Mol Biol Cell 2002; 13: 203144.
  • 25
    Sundberg C, Thodeti CK, Kveiborg M et al. Regulation of ADAM12 cell-surface expression by protein kinase C epsilon. J Biol Chem 2004; 279: 51 601–11.
  • 26
    Soond S, Everson B, Riches DW, Murphy G. ERK-mediated phosphorylation of Thr735 in TNFα-converting enzyme and its potential role in TACE protein trafficking. J Cell Sci 2005; 118: 237180.
  • 27
    Loechel F, Gilpin BJ, Engvall E, Albrechtsen R, Wewer UM. Human ADAM 12 (meltrin alpha) is an active metalloprotease. J Biol Chem 1998; 273: 16 993–7.
  • 28
    Gao G, Plaas A, Thompson VP et al. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. J Biol Chem 2004; 279: 10 042–51.
  • 29
    Rodriguez-Manzaneque JC, Milchanowski AB, Dufour EK, Leduc R, Iruela-Arispe ML. Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms. J Biol Chem 2004; 275: 33 471–9.
  • 30
    Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci 2002; 115: 371927.
  • 31
    Amour A, Knight CG, Webster A et al. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett 2000; 473: 2759.
  • 32
    Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem Biophys Res Commun 2000; 278: 51115.
  • 33
    Zou J, Zhu F, Liu J et al. Catalytic activity of human ADAM33. J Biol Chem 2000; 279: 981830.
  • 34
    Kashiwagi M, Enghild JJ, Gendron C et al. Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing. J Biol Chem 2004; 279: 10 109–19.
  • 35
    Wei S, Kashiwagi M, Kota S et al. Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not tumor necrosis factor-alpha-converting enzyme. J Biol Chem 2004; 280: 32 877–82.
  • 36
    Amour A, Knight CG, English WR et al. The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs. FEBS Lett 2002; 524: 1548.
  • 37
    Chesneau V, Becherer JD, Zheng Y et al. Catalytic properties of ADAM19. J Biol Chem 2003; 278: 22 331–40.
  • 38
    Hashimoto G, Shimoda M, Okada Y. ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan. J Biol Chem 2004; 279: 32 483–91.
  • 39
    Schlomann U, Wildeboer D, Webster A et al. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J Biol Chem 2002; 277: 48 210–19.
  • 40
    Roghani M, Becherer JD, Moss M et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J Biol Chem 1999; 274: 353140.
  • 41
    Ludwig A, Hundhausen C, Lambert MH et al. 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: 16171.
  • 42
    Zhou BB, Peyton M, He B et al. Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell 2006; 10: 3950.
  • 43
    Ishikawa N, Daigo Y, Yasui W et al. ADAM8 as a novel serological and histochemical marker for lung cancer. Clin Cancer Res 2006; 10: 836370.
  • 44
    Wildeboer D, Naus S, Amy Sang QX, Bartsch JW, Pagenstecher A. Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness. J Neuropathol Exp Neurol 2006; 65: 51627.
  • 45
    O'Shea C, McKie N, Buggy Y et al. Expression of ADAM-9 mRNA and protein in human breast cancer. Int J Cancer 2003; 105: 75461.
  • 46
    Peduto L, Reuter VE, Shaffer DR et al. Critical function for ADAM9 in mouse prostate cancer. Cancer Res 2005; 65: 931219.
  • 47
    Mazzocca A, Coppari R, De Franco R et al. A secreted form of ADAM9 promotes carcinoma invasion through tumor–stromal interactions. Cancer Res 2005; 65: 472838.
  • 48
    Shintani Y, Higashiyama S, Ohta M et al. Overexpression of ADAM9 in non-small cell lung cancer correlates with brain metastasis. Cancer Res 2004; 64: 41906.
  • 49
    Ko SY, Lin SC, Wong YK et al. Increase of disintergin metalloprotease 10 (ADAM10) expression in oral squamous cell carcinoma. Cancer Lett 2007; 245: 3343.
  • 50
    Carl-McGrath S, Lendeckel U, Ebert M, Roessner A, Rocken C. The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer. Int J Oncol 2005; 26: 1724.
  • 51
    Fogel M, Gutwein P, Mechtersheimer S et al. L1 expression as a predictor of progression and survival in patients with uterine and ovarian carcinomas. Lancet 2003; 362: 86975.
  • 52
    Gutwein P, Oleszewski M, Mechtersheimer S et al. Role of Src kinases in the ADAM-mediated release of L1 adhesion molecule from human tumor cells. J Biol Chem 2000; 275: 15 490–7.
  • 53
    Mechtersheimer S, Gutwein P, Agmon-Levin N et al. Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins. J Cell Biol 2001; 155: 66173.
  • 54
    Kodama T, Ikeda E, Okada A et al. ADAM12 is selectively overexpressed in human glioblastomas and is associated with glioblastoma cell proliferation and shedding of heparin-binding epidermal growth factor. Am J Pathol 2004; 165: 174353.
  • 55
    Iba K, Albrechtsen R, Gilpin BJ, Loechel F, Wewer UM. Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion. Am J Pathol 1999; 154: 1489501.
  • 56
    Kveiborg M, Frohlich C, Albrechtsen R et al. A role for ADAM12 in breast tumor progression and stromal cell apoptosis. Cancer Res 2005; 65: 475461.
  • 57
    Schutz A, Hartig W, Wobus M et al. Expression of ADAM15 in lung carcinomas. Virchows Arch 2005; 446: 4219.
  • 58
    Lendeckel U, Kohl J, Arndt M et al. Increased expression of ADAM family members in human breast cancer and breast cancer cell lines. J Cancer Res Clin Oncol 2005; 131: 418.
  • 59
    Trochon-Joseph V, Martel-Renoir D, Mir LM et al. Evidence of antiangiogenic and antimetastatic activities of the recombinant disintegrin domain of metargidin. Cancer Res 2005; 64: 20629.
  • 60
    Beck V, Herold H, Benge A et al. ADAM15 decreases integrin αvβ3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion. Int J Biochem Cell Biol 2005; 37: 590603.
  • 61
    Borrell-Pages M, Rojo F, Albanell J, Baselga J, Arribas J. TACE is required for the activation of the EGFR by TGF-α in tumors. EMBO J 2005; 22: 111424.
  • 62
    Ohtsuka T, Shiomi T, Shimoda M et al. ADAM28 is overexpressed in human non-small cell lung carcinomas and correlates with cell proliferation and lymph node metastasis. Int J Cancer 2006; 118: 26373.
  • 63
    Mitsui Y, Mochizuki S, Kodama T et al. ADAM28 is overexpressed in human breast carcinomas: implications for carcinoma cell proliferation through cleavage of insulin-like growth factor binding protein-3. Cancer Res 2006; 66: 991320.
  • 64
    Dimitroff CJ, Descheny L, Trujillo N et al. Identification of leukocyte E-selectin ligands, P-selectin glycoprotein ligand-1 and E-selectin ligand-1, on human metastatic prostate tumor cells. Cancer Res 2005; 65: 575060.
  • 65
    Liu YJ, Xu Y, Yu Q. Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively. Oncogene 2006; 25: 245267.
  • 66
    Held-Feindt J, Paredes EB, Blomer U et al. Matrix-degrading proteases ADAMTS4 and ADAMTS5 (disintegrins and metalloproteinases with thrombospondin motifs 4 and 5) are expressed in human glioblastomas. Int J Cancer 2006; 118: 5561.
  • 67
    Nakada M, Miyamori H, Kita D et al. Human glioblastomas overexpress ADAMTS-5 that degrades brevican. Acta Neuropathol (Berl) 2005; 110: 23946.
  • 68
    Roemer A, Schwettmann L, Jung M et al. Increased mRNA expression of ADAMs in renal cell carcinoma and their association with clinical outcome. Oncol Rep 2004; 11: 52936.
  • 69
    Grutzmann R, Luttges J, Sipos B et al. ADAM9 expression in pancreatic cancer is associated with tumor type and is a prognostic factor in ductal adenocarcinoma. Br J Cancer 2004; 90: 10538.
  • 70
    Zigrino P, Mauch C, Fox JW, Nischt R. ADAM9 expression and regulation in human skin melanoma and melanoma cell lines. Int J Cancer 2005; 116: 8539.
  • 71
    Tannapfel A, Anhalt K, Hausermann P et al. Identification of novel proteins associated with hepatocellular carcinomas using protein microarrays. J Pathol 2003; 201: 23849.
  • 72
    Yoshimura T, Tomita T, Dixon MF et al. ADAM (a disintegrin and metalloproteinase) messenger RNA expression in Helicobacter pylori-infected, normal, and neoplastic gastric mucosa. J Infect Dis 2002; 185: 33240.
  • 73
    Gavert N, Conacci-Sorrell M, Gast D et al. L1, a novel target of beta-catenin signaling, transforms cells and is expressed at the invasive front of colon cancers. J Cell Biol 2005; 168: 63342.
  • 74
    Wu E, Croucher PI, Mckie N. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem Biophys Res Commun 1997; 235: 43742.
  • 75
    McCulloch DR, Akl P, Samaratunga H, Herington AC, Odorico DM. Expression of the disintegrin metalloproteinase, ADAM-10, in prostate cancer and its regulation by dihydrotestosterone, insulin-like growth factor I, and epidermal growth factor in the prostate cancer cell model LNCaP. Clin Cancer Res 2004; 10: 31423.
  • 76
    Kuefer R, Day KC, Kleer CG et al. ADAM15 disintegrin is associated with aggressive prostate and breast cancer diseases. Neoplasia 2006; 8: 31929.
  • 77
    Tanaka Y, Miyamoto S, Suzuki SO et al. Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloproteinase 17 expression in human ovarian cancer. Clin Cancer Res 2005; 11: 478392.
  • 78
    Blanchot-Jossic F, Jarry A, Masson D et al. Up-regulated expression of ADAM17 in human colon carcinoma: Co-expression with EGFR in neoplastic and endothelial cells. J Pathol 2005; 207: 15663.
  • 79
    Karan D, Lin FC, Bryan M et al. Expression of ADAMs (a disintegrin and metalloprotease) and TIMP-3 (tissue inhibitor of metalloproteinase-3) in human prostatic adenocarcinomas. Int J Oncol 2003; 23: 136571.
  • 80
    Minn AJ, Kang Y, Serganova I et al. Distinct organ-specific metastatic potential of individual breast cancer cells and primary tumors. J Clin Invest 2005; 115: 4455.