Recombinant disintegrin domain of human ADAM9 inhibits migration and invasion of DU145 prostate tumor cells

References

• Maximum androgen blockade in advanced prostate cancer: an overview of the randomised trials. Prostate Cancer Trialists' Collaborative Group. Lancet 2000; 355:1491-8; PMID:10801170; http://dx.doi.org/10.1016/S0140-6736(00)02163-2
   PubMed Web of Science ®Google Scholar
• Stone AL, Kroeger M, Sang QX. Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review). J Protein Chem 1999; 18:447-65; PMID:10449042; http://dx.doi.org/10.1023/A:1020692710029
   PubMedGoogle Scholar
• Klein T, Bischoff R. Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: biological function and structure. J Proteome Res 2011; 10:17-33; PMID:20849079; http://dx.doi.org/10.1021/pr100556z
   PubMed Web of Science ®Google Scholar
• Blobel CP. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 2005; 6:32-43; PMID:15688065; http://dx.doi.org/10.1038/nrm1548
   PubMed Web of Science ®Google Scholar
• Nath D, Slocombe PM, Webster A, Stephens PE, Docherty AJ, Murphy G. Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility. J Cell Sci 2000; 113 ( Pt 12):2319-28; PMID:10825303
   PubMed Web of Science ®Google Scholar
• Zhou M, Graham R, Russell G, Croucher PI. MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin. Biochem Biophys Res Commun 2001; 280:574-80; PMID:11162558; http://dx.doi.org/10.1006/bbrc.2000.4155
   PubMedGoogle Scholar
• Karadag A, Zhou M, Croucher PI. ADAM-9 (MDC-9/meltrin-gamma), a member of the a disintegrin and metalloproteinase family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the alpha(v)beta5 integrin. Blood 2006; 107:3271-8; PMID:16373656; http://dx.doi.org/10.1182/blood-2005-09-3830
   PubMedGoogle Scholar
• Mazzocca A, Coppari R, De Franco R, Cho JY, Libermann TA, Pinzani M, et al. A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions. Cancer Res 2005; 65:4728-38; PMID:15930291; http://dx.doi.org/10.1158/0008-5472.CAN-04-4449
   PubMed Web of Science ®Google Scholar
• Cominetti MR, Martin AC, Ribeiro JU, Djaafri I, Fauvel-Lafeve F, Crepin M, et al. Inhibition of platelets and tumor cell adhesion by the disintegrin domain of human ADAM9 to collagen I under dynamic flow conditions. Biochimie 2009; 91:1045-52; PMID:19505527; http://dx.doi.org/10.1016/j.biochi.2009.05.012
   PubMed Web of Science ®Google Scholar
• Zigrino P, Steiger J, Fox JW, Loffek S, Schild A, Nischt R, et al. Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration. JBiol Chem 2007; 282:30785-93; PMID:17704059; http://dx.doi.org/10.1074/jbc.M701658200
   PubMedGoogle Scholar
• Takeda S, Igarashi T, Mori H, Araki S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J 2006; 25:2388-96; PMID:16688218; http://dx.doi.org/10.1038/sj.emboj.7601131
   PubMedGoogle Scholar
• Fritzsche FR, Jung M, Tolle A, Wild P, Hartmann A, Wassermann K, et al. ADAM9 expression is a significant and independent prognostic marker of PSA relapse in prostate cancer. Euro Urol 2008; 54:1097-106; PMID:18061337; http://dx.doi.org/10.1016/j.eururo.2007.11.034
   PubMedGoogle Scholar
• Carl-McGrath S, Lendeckel U, Ebert M, Roessner A, Rocken C. The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer. Int JOncol 2005; 26:17-24; PMID:15586220
   PubMed Web of Science ®Google Scholar
• Peduto L, Reuter VE, Shaffer DR, Scher HI, Blobel CP. Critical function for ADAM9 in mouse prostate cancer. Cancer research 2005; 65:9312-9; PMID:16230393; http://dx.doi.org/10.1158/0008-5472.CAN-05-1063
   PubMedGoogle Scholar
• Li J, Ji Z, Qiao C, Qi Y, Shi W. Overexpression of ADAM9 Promotes Colon Cancer Cells Invasion. J Invest Surg 2013; 26; PMID:23514059; http://dx.doi.org/10.3109/08941939.2012.728682
   PubMedGoogle Scholar
• Josson S, Anderson CS, Sung SY, Johnstone PA, Kubo H, Hsieh CL, et al. Inhibition of ADAM9 expression induces epithelial phenotypic alterations and sensitizes human prostate cancer cells to radiation and chemotherapy. Prostate 2011; 71:232-40; PMID:20672324; http://dx.doi.org/10.1002/pros.21237
   PubMed Web of Science ®Google Scholar
• Peduto L. ADAM9 as a potential target molecule in cancer. Curr Pharm Des 2009; 15:2282-7; PMID:19601830; http://dx.doi.org/10.2174/138161209788682415
   PubMed Web of Science ®Google Scholar
• Zhang J, Chen N, Qi J, Zhou B, Qiu X. HDGF and ADAM9 are novel molecular staging biomarkers, prognostic biomarkers and predictive biomarkers for adjuvant chemotherapy in surgically resected stage I non-small cell lung cancer. JCancer ResClin Oncol 2014; 140:1441-9; PMID:24770635; http://dx.doi.org/10.1007/s00432-014-1687-2
   PubMedGoogle Scholar
• Hood JD, Cheresh DA. Role of integrins in cell invasion and migration. Nat Rev Cancer 2002; 2:91-100; PMID:12635172; http://dx.doi.org/10.1038/nrc727
   PubMed Web of Science ®Google Scholar
• Pontier SM, Muller WJ. Integrins in breast cancer dormancy. APMIS 2008; 116:677-84; PMID: 18834411; http://dx.doi.org/10.1111/j.1600-0463.2008.01026.x
   PubMedGoogle Scholar
• Van den Eynden GG, Majeed AW, Illemann M, Vermeulen PB, Bird NC, Hoyer-Hansen G, et al. The multifaceted role of the microenvironment in liver metastasis: biology and clinical implications. Cancer Res 2013; 73:2031-43; PMID:23536564; http://dx.doi.org/10.1158/0008-5472.CAN-12-3931
   PubMed Web of Science ®Google Scholar
• Sakamoto S, Kyprianou N. Targeting anoikis resistance in prostate cancer metastasis. Mol Aspects Med 2010; 31:205-14; PMID:20153362; http://dx.doi.org/10.1016/j.mam.2010.02.001
   PubMed Web of Science ®Google Scholar
• Belkin AM, Stepp MA. Integrins as receptors for laminins. Microsc Res Techniq 2000; 51:280-301; PMID:NOT_FOUND; http://dx.doi.org/10.1002/1097-0029(20001101)51:3%3c280::AID-JEMT7%3e3.0.CO;2-O
   PubMed Web of Science ®Google Scholar
• Skogseth H, Holt RU, Larsson E, Halgunset J. Tyrosine kinase inhibitors alter adhesivity of prostatic cancer cells to extracellular matrix components. APMIS 2006; 114:225-33; PMID:16643189; http://dx.doi.org/10.1111/j.1600-0463.2006.apm_365.x
   PubMedGoogle Scholar
• Witkowski CM, Rabinovitz I, Nagle RB, Affinito KS, Cress AE. Characterization of integrin subunits, cellular adhesion and tumorgenicity of four human prostate cell lines. J Cancer Res Clin Oncol 1993; 119:637-44; PMID:7688749; http://dx.doi.org/10.1007/BF01215981
   PubMed Web of Science ®Google Scholar
• Fry JL, Toker A. Secreted and membrane-bound isoforms of protease ADAM9 have opposing effects on breast cancer cell migration. Cancer Res 2010; 70:8187-98; PMID:20736367; http://dx.doi.org/10.1158/0008-5472.CAN-09-4231
   PubMed Web of Science ®Google Scholar
• Roghani M, Becherer JD, Moss ML, Atherton RE, Erdjument-Bromage H, Arribas J, et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J Biol Chem 1999; 274:3531-40; PMID:9920899; http://dx.doi.org/10.1074/jbc.274.6.3531
   PubMed Web of Science ®Google Scholar
• Yue PY, Leung EP, Mak NK, Wong RN. A simplified method for quantifying cell migration/wound healing in 96-well plates. J Biomol Screen 2010; 15:427-33; PMID:20208035; http://dx.doi.org/10.1177/1087057110361772
   PubMed Web of Science ®Google Scholar