Structure, regulatory factors and cancer-related physiological effects of ADAM9

References

• Wolfsberg TG, Primakoff P, Myles DG, et al. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J Cell Biol. 1995;131(2):275–278.
   PubMed Web of Science ®Google Scholar
• Wolfsberg TG, Straight PD, Gerena RL, et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol. 1995;169:378–383.
   PubMed Web of Science ®Google Scholar
• Weskamp G, Kratzschmar J, Reid MS, et al. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J Cell Biol. 1996;132:717–726.
   PubMed Web of Science ®Google Scholar
• Nath D, Slocombe PM, Webster A, et al. 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)):2319–2328.
   PubMed Web of Science ®Google Scholar
• Primakoff P, Myles DG. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 2000;16:83–87.
   PubMed Web of Science ®Google Scholar
• Zhang C, Zhang Y, Ding W, et al. MiR-33a suppresses breast cancer cell proliferation and metastasis by targeting ADAM9 and ROS1. Protein Cell. 2015;6(12):881–889
   PubMed Web of Science ®Google Scholar
• Roghani M, Becherer JD, Moss ML, et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J Biol Chem. 1999;274(6):3531–3540
   PubMed Web of Science ®Google Scholar
• Niewiarowski S, McLane MA, Kloczewiak M, et al. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin Hematol. 1994;31:289–300.
   PubMed Web of Science ®Google Scholar
• White JM. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr Opin Cell Biol. 2003;15:598–606.
   PubMed Web of Science ®Google Scholar
• Porter S, Clark IM, Kevorkian L, et al. The ADAMTS metalloproteinases. Biochem J. 2005;386:15–27.
   PubMed Web of Science ®Google Scholar
• Janes PW, Saha N, Barton WA, et al. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell. 2005;123(2):291–304
   PubMed Web of Science ®Google Scholar
• Hotoda N, Koike H, Sasagawa N, et al. A secreted form of human ADAM9 has an alpha-secretase activity for APP. Biochem Biophys Res Commun. 2002;293:800–805.
   PubMed Web of Science ®Google Scholar
• Kerlavage A, Bonazzi V, di Tommaso M, et al. The celera discovery system. Nucleic Acids Res. 2002;30:129–136.
   PubMed Web of Science ®Google Scholar
• Duffy MJ, Mullooly M, O’Donovan N, et al. The ADAMs family of proteases: new biomarkers and therapeutic targets for cancer? Clin Proteomics. 2011;8(1):9
   PubMedGoogle Scholar
• Black RA, White JM. ADAMs: focus on the protease domain. Curr Opin Cell Biol. 1998;10:654–659.
   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;18:447–465.
   PubMedGoogle Scholar
• 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;17:7260–7272.
   PubMed Web of Science ®Google Scholar
• Mahimkar RM, Baricos WH, Visaya O, et al. Identification, cellular distribution and potential function of the metalloprotease-disintegrin MDC9 in the kidney. J Am Soc Nephrol. 2000;11:595–603.
   PubMed Web of Science ®Google Scholar
• Overall CM, Kleifeld O. Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer. 2006;6:227–239.
   PubMed Web of Science ®Google Scholar
• Cauwe B, Van den Steen PE, Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol. 2007;42:113–185.
   PubMed Web of Science ®Google Scholar
• Sanderson MP, Dempsey PJ, Dunbar AJ. Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGF-like factors. Growth Factors. 2006;24:121–136.
   PubMed Web of Science ®Google Scholar
• Perry AC, Jones R, Hall L. Analysis of transcripts encoding novel members of the mammalian metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family and their expression in reproductive and non-reproductive monkey tissues. Biochem J. 1995;312((Pt 1)):239–244.
   PubMedGoogle Scholar
• Sarkar S, Zemp FJ, Senger D, et al. ADAM-9 is a novel mediator of tenascin-C-stimulated invasiveness of brain tumor-initiating cells. Neuro Oncol. 2015;17:1095–1105.
   PubMed Web of Science ®Google Scholar
• Kenny PA, Bissell MJ. Tumor reversion: correction of malignant behavior by microenvironmental cues. Int J Cancer. 2003;107:688–695.
   PubMed Web of Science ®Google Scholar
• Albelda SM. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab Invest. 1993;68:4–17.
   PubMed Web of Science ®Google Scholar
• Nicolson GL. Tumor and host molecules important in the organ preference of metastasis. Semin Cancer Biol. 1991;2:143–154.
   PubMedGoogle Scholar
• Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100:57–70.
   PubMed Web of Science ®Google Scholar
• Koike H, TOMIOKA S, SORIMACHI H, et al. Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein. Biochem J. 1999;343(Pt 2):371–375
   PubMed Web of Science ®Google Scholar
• Dyczynska E, Sun D, Yi H, et al. Proteolytic processing of delta-like 1 by ADAM proteases. J Biol Chem. 2007;282:436–444.
   PubMed Web of Science ®Google Scholar
• Mohan S, Thompson GR, Amaar YG, et al. ADAM-9 is an insulin-like growth factor binding protein-5 protease produced and secreted by human osteoblasts. Biochemistry. 2002;41:15394–15403.
   PubMed Web of Science ®Google Scholar
• Cisse MA, Sunyach C, Lefranc-Jullien S, et al. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J Biol Chem. 2005;280(49):40624–40631
   PubMed Web of Science ®Google Scholar
• Franzke CW, Tasanen K, Borradori L, et al. Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface. J Biol Chem. 2004;279:24521–24529.
   PubMed Web of Science ®Google Scholar
• 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(11):4728–4738
   PubMed Web of Science ®Google Scholar
• Peduto L, Reuter VE, Shaffer DR, et al. Critical function for ADAM9 in mouse prostate cancer. Cancer Res. 2005;65:9312–9319.
   PubMedGoogle Scholar
• Coussens LM, Werb Z. Inflammation and cancer. Nature. 2002;420:860–867.
   PubMed Web of Science ®Google Scholar
• Bode W, Gomis-Ruth FX, Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’. FEBS Lett. 1993;331:134–140.
   PubMed Web of Science ®Google Scholar
• Arribas J, Bech-Serra JJ, Santiago-Josefat B. ADAMs, cell migration and cancer. Cancer Metastasis Rev. 2006;25:57–68.
   PubMed Web of Science ®Google Scholar
• Eto K, Huet C, Tarui T, et al. Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. J Biol Chem. 2002;277:17804–17810.
   PubMed Web of Science ®Google Scholar
• Wolfsberg TG, White JM. ADAMs in fertilization and development. Dev Biol. 1996;180:389–401.
   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;70:8187–8198.
   PubMed Web of Science ®Google Scholar
• Aleckovic M, Kang Y. Regulation of cancer metastasis by cell-free miRNAs. Biochim Biophys Acta. 2015;1855:24–42.
   PubMed Web of Science ®Google Scholar
• Ruan K, Fang X, Ouyang G. MicroRNAs: novel regulators in the hallmarks of human cancer. Cancer Lett. 2009;285:116–126.
   PubMed Web of Science ®Google Scholar
• Volinia S, Galasso M, Sana ME, et al. Breast cancer signatures for invasiveness and prognosis defined by deep sequencing of microRNA. Proc Natl Acad Sci U S A. 2012;109:3024–3029.
   PubMed Web of Science ®Google Scholar
• Khella HWZ, Scorilas A, Mozes R, et al. Low expression of miR-126 is a prognostic marker for metastatic clear cell renal cell carcinoma. Am J Pathol. 2015;185(3):693–703
   PubMed Web of Science ®Google Scholar
• Yang Y, Song KL, Chang H, et al. Decreased expression of microRNA-126 is associated with poor prognosis in patients with cervical cancer. Diagn Pathol. 2014;9:220.
   PubMed Web of Science ®Google Scholar
• Liu Y, Zhou Y, Feng X, et al. Low expression of microRNA-126 is associated with poor prognosis in colorectal cancer. Genes Chromosomes Cancer. 2014;53(4):358–365
   PubMed Web of Science ®Google Scholar
• Tavazoie SF, Alarcón C, Oskarsson T, et al. Endogenous human microRNAs that suppress breast cancer metastasis. Nature. 2008;451:147–152.
   PubMed Web of Science ®Google Scholar
• Hamada S, Satoh K, Fujibuchi W, et al. MiR-126 acts as a tumor suppressor in pancreatic cancer cells via the regulation of ADAM9. Mol Cancer Res. 2012;10(1):3–10
   PubMed Web of Science ®Google Scholar
• Chen H, Miao R, Fan J, et al. Decreased expression of miR-126 correlates with metastatic recurrence of hepatocellular carcinoma. Clin Exp Metastasis. 2013;30(5):651–658
   PubMed Web of Science ®Google Scholar
• Sasahira T, Kurihara M, Bhawal UK, et al. Downregulation of miR-126 induces angiogenesis and lymphangiogenesis by activation of VEGF-A in oral cancer. Br J Cancer. 2012;107:700–706.
   PubMed Web of Science ®Google Scholar
• 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(3):275–279
   PubMed Web of Science ®Google Scholar
• Kashiwagi M, Tortorella M, Nagase H, et al. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem. 2001;276:12501–12504.
   PubMed Web of Science ®Google Scholar
• Murphy G, Knauper V, Lee MH, et al. Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail. Biochem Soc Symp. 2003;70:65–80.
   PubMedGoogle Scholar
• Nagase H, Brew K. Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Biochem Soc Symp. 2003;70:201–212.
   PubMedGoogle Scholar
• Amour A, Knight CG, English WR, et al. The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs. FEBS Lett. 2002;524:154–158.
   PubMed Web of Science ®Google Scholar
• Chen C-M, Hsieh Y-H, Hwang J-M, et al. Fisetin suppresses ADAM9 expression and inhibits invasion of glioma cancer cells through increased phosphorylation of ERK1/2. Tumour Biol. 2015;36(5):3407–3415
   PubMedGoogle Scholar
• Hong W, Dong E. The past, present and future of breast cancer research in China. Cancer Lett. 2014;351:1–5.
   PubMed Web of Science ®Google Scholar
• Bray F, Ferlay J, Soerjomataram I, et al. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin. 2018;68:394–424.
   PubMed Web of Science ®Google Scholar
• Porter S, Scott SD, Sassoon EM, et al. Dysregulated expression of adamalysin-thrombospondin genes in human breast carcinoma. Clin Cancer Res. 2004;10:2429–2440.
   PubMed Web of Science ®Google Scholar
• 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(6):754–761
   PubMed Web of Science ®Google Scholar
• Hanemaaijer R, Verheijen JH, Maguire TM, et al. Increased gelatinase-A and gelatinase-B activities in malignant vs. benign breast tumors. Int J Cancer. 2000;86:204–207.
   PubMed Web of Science ®Google Scholar
• Chenard M-P, O’Siorain L, Shering S, et al. High levels of stromelysin-3 correlate with poor prognosis in patients with breast carcinoma. Int J Cancer. 1996;69(6):448–451
   PubMed Web of Science ®Google Scholar
• Duffy MJ, Blaser J, Duggan C, et al. Assay of matrix metalloproteases types 8 and 9 by ELISA in human breast cancer. Br J Cancer. 1995;71(5):1025–1028
   PubMed Web of Science ®Google Scholar
• Remacle AG, Noël A, Duggan C, et al. Assay of matrix metalloproteinases types 1, 2, 3 and 9 in breast cancer. Br J Cancer. 1998;77(6):926–931
   PubMed Web of Science ®Google Scholar
• Elston CW, Ellis IO, Pinder SE. Pathological prognostic factors in breast cancer. Crit Rev Oncol Hematol. 1999;31:209–223.
   PubMed Web of Science ®Google Scholar
• Tabar L, Fagerberg G, Chen HH, et al. Tumour development, histology and grade of breast cancers: prognosis and progression. Int J Cancer. 1996;66:413–419.
   PubMed Web of Science ®Google Scholar
• Isaacs C, Stearns V, Hayes DF. New prognostic factors for breast cancer recurrence. Semin Oncol. 2001;28:53–67.
   PubMed Web of Science ®Google Scholar
• Slamon DJ, Clark G, Wong S, et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science. 1987;235(4785):177–182
   PubMed Web of Science ®Google Scholar
• Zhu N, Zhang D, Xie H, et al. Endothelial-specific intron-derived miR-126 is down-regulated in human breast cancer and targets both VEGFA and PIK3R2. Mol Cell Biochem. 2011;351(1–2):157–164
   PubMed Web of Science ®Google Scholar
• Wang CZ, Yuan P, Li Y. MiR-126 regulated breast cancer cell invasion by targeting ADAM9. Int J Clin Exp Pathol. 2015;8:6547–6553.
   PubMed Web of Science ®Google Scholar
• Blenkiron C, Goldstein LD, Thorne NP, et al. MicroRNA expression profiling of human breast cancer identifies new markers of tumor subtype. Genome Biol. 2007;8(10):R214
   PubMed Web of Science ®Google Scholar
• Holmes RS, Vaughan TL. Epidemiology and pathogenesis of esophageal cancer. Semin Radiat Oncol. 2007;17:2–9.
   PubMed Web of Science ®Google Scholar
• Liu R, Gu J, Jiang P, et al. DNMT1-microRNA126 epigenetic circuit contributes to esophageal squamous cell carcinoma growth via ADAM9-EGFR-AKT signaling. Clin Cancer Res. 2015;21(4):854–863
   PubMed Web of Science ®Google Scholar
• Siegel R, Naishadham D, Jemal A. Cancer statistics, 2013. CA Cancer J Clin. 2013;63:11–30.
   PubMed Web of Science ®Google Scholar
• Reungwetwattana T, Weroha SJ, Molina JR. Oncogenic pathways, molecularly targeted therapies, and highlighted clinical trials in non-small-cell lung cancer (NSCLC). Clin Lung Cancer. 2012;13:252–266.
   PubMed Web of Science ®Google Scholar
• Jemal A, Siegel R, Xu J, et al. Cancer statistics, 2010. CA Cancer J Clin. 2010;60:277–300.
   PubMed Web of Science ®Google Scholar
• 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(12):4190–4196
   PubMed Web of Science ®Google Scholar
• Chang L, Gong F, Cui Y. RNAi-mediated A disintegrin and metalloproteinase 9 gene silencing inhibits the tumor growth of non-small lung cancer in vitro and in vivo. Mol Med Rep. 2015;12:1197–1204.
   PubMed Web of Science ®Google Scholar
• Hirao T, Nanba D, Tanaka M, et al. Overexpression of ADAM9 enhances growth factor-mediated recycling of E-cadherin in human colon cancer cell line HT29 cells. Exp Cell Res. 2006;312:331–339.
   PubMed Web of Science ®Google Scholar
• Fu Q, Cheng J, Zhang J, et al. miR-20b reduces 5-FU resistance by suppressing the ADAM9/EGFR signaling pathway in colon cancer. Oncol Rep. 2017;37(1):123–130
   PubMed Web of Science ®Google Scholar
• Cordon-Cardo C. Molecular alterations associated with bladder cancer initiation and progression. Scand J Urol Nephrol Suppl. 2008;42(sup218):154–165.
   Google Scholar
• Jia AY, Castillo-Martin M, Bonal DM, et al. MicroRNA-126 inhibits invasion in bladder cancer via regulation of ADAM9. Br J Cancer. 2014;110(12):2945–2954
   PubMed Web of Science ®Google Scholar
• Fritzsche FR, Jung M, Tolle A, et al. ADAM9 is highly expressed in renal cell cancer and is associated with tumour progression. BMC Cancer. 2008;8:179.
   PubMed Web of Science ®Google Scholar
• Min KJ, Nam JO, Kwon TK. Fisetin induces apoptosis through p53-mediated up-regulation of dr5 expression in human renalcarcinoma caki cells. Molecules. 2017;22. DOI:10.3390/molecules22081285
   Web of Science ®Google Scholar
• 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;11:529–536.
   PubMed Web of Science ®Google Scholar
• Bertram J, Peacock JW, Fazli L, et al. Loss of PTEN is associated with progression to androgen independence. Prostate. 2006;66(9):895–902
   PubMed Web of Science ®Google Scholar
• Ichikawa T, Suzuki H, Ueda T, et al. Hormone treatment for prostate cancer: current issues and future directions. Cancer Chemother Pharmacol. 2005;56(Suppl S1):58–63
   PubMedGoogle Scholar
• Shigemura K, Sung S-Y, Kubo H, et al. Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells. Prostate. 2007;67(7):722–731
   PubMed Web of Science ®Google Scholar
• Singh SK, Hawkins C, Clarke ID, et al. Identification of human brain tumour initiating cells. Nature. 2004;432:396–401.
   PubMed Web of Science ®Google Scholar
• Choi SA, Lee JY, Phi JH, et al. Identification of brain tumour initiating cells using the stem cell marker aldehyde dehydrogenase. Eur J Cancer. 2014;50(1):137–149
   PubMed Web of Science ®Google Scholar
• Modrek AS, Bayin NS, Placantonakis DG. Brain stem cells as the cell of origin in glioma. World J Stem Cells. 2014;6:43–52.
   PubMedGoogle Scholar
• Leins A, Riva P, Lindstedt R, et al. Expression of tenascin-C in various human brain tumors and its relevance for survival in patients with astrocytoma. Cancer. 2003;98(11):2430–2439
   PubMed Web of Science ®Google Scholar
• Deryugina EI, Bourdon MA. Tenascin mediates human glioma cell migration and modulates cell migration on fibronectin. J Cell Sci. 1996;109((Pt 3)):643–652.
   PubMedGoogle Scholar
• Wang H, Sun T, Hu J, et al. miR-33a promotes glioma-initiating cell self-renewal via PKA and NOTCH pathways. J Clin Invest. 2014;124(10):4489–4502
   PubMed Web of Science ®Google Scholar
• Carl-McGrath S, Lendeckel U, Ebert M, et al. The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer. Int J Oncol. 2005;26:17–24.
   PubMed Web of Science ®Google Scholar
• Yoshimura T, Tomita T, Dixon M, et al. ADAMs (a disintegrin and metalloproteinase) messenger RNA expression in helicobacter pylori–infected, normal, and neoplastic gastric mucosa. J Infect Dis. 2002;185:332–340.
   PubMed Web of Science ®Google Scholar
• Kim JM, Jeung H-C, Rha SY, et al. The effect of disintegrin-metalloproteinase ADAM9 in gastric cancer progression. Mol Cancer Ther. 2014;13:3074–3085.
   PubMed Web of Science ®Google Scholar
• Rocks N, Paulissen G, El Hour M, et al. Emerging roles of ADAM and ADAMTS metalloproteinases in cancer. Biochimie. 2008;90(2):369–379
   PubMed Web of Science ®Google Scholar
• Zigrino P, Mauch C, Fox JW, et al. Adam-9expression and regulation in human skin melanoma and melanoma cell lines. Int J Cancer. 2005;116:853–859.
   PubMed Web of Science ®Google Scholar
• Franzke C-W, Tasanen K, Schäcke H, et al. Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs. Embo J. 2002;21(19):5026–5035
   PubMed Web of Science ®Google Scholar
• Kurschat P, Zigrino P, Nischt R, et al. Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines. J Biol Chem. 1999;274(30):21056–21062
   PubMed Web of Science ®Google Scholar
• Philip S, Kundu GC. Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase-2 activation through I kappa B alpha/IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways. J Biol Chem. 2003;278:14487–14497.
   PubMed Web of Science ®Google Scholar
• Rumpler G, Becker B, Hafner C, et al. Identification of differentially expressed genes in models of melanoma progression by cDNA array analysis: SPARC, MIF and a novel cathepsin protease characterize aggressive phenotypes. Exp Dermatol. 2003;12(6):761–771
   PubMed Web of Science ®Google Scholar
• Hornebeck W, Emonard H, Monboisse JC, et al. Matrix-directed regulation of pericellular proteolysis and tumor progression. Semin Cancer Biol. 2002;12:231–241.
   PubMed Web of Science ®Google Scholar
• Cairns RA, Khokha R, Hill RP. Molecular mechanisms of tumor invasion and metastasis: an integrated view. Curr Mol Med. 2003;3:659–671.
   PubMed Web of Science ®Google Scholar
• Yamada D, Ohuchida K, Mizumoto K, et al. Increased expression of ADAM 9 and ADAM 15 mRNA in pancreatic cancer. Anticancer Res. 2007;27:793–799.
   PubMed Web of Science ®Google Scholar
• Allinson TM, Parkin ET, Turner AJ, et al. ADAMs family members as amyloid precursor protein alpha-secretases. J Neurosci Res. 2003;74:342–352.
   PubMed Web of Science ®Google Scholar
• Al-Fakhri N, Wilhelm J, Hahn M, et al. Increased expression of disintegrin-metalloproteinases ADAM-15 and ADAM-9 following upregulation of integrins alpha5beta1 and alphavbeta3 in atherosclerosis. J Cell Biochem. 2003;89(4):808–823
   PubMed Web of Science ®Google Scholar
• Valkovskaya N, Kayed H, Felix K, et al. ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer. J Cell Mol Med. 2007;11(5):1162–1174
   PubMed Web of Science ®Google Scholar
• Arima T, Enokida H, Kubo H, et al. Nuclear translocation of ADAM-10 contributes to the pathogenesis and progression of human prostate cancer. Cancer Sci. 2007;98(11):1720–1726
   PubMed Web of Science ®Google Scholar
• Roy R, Wewer UM, Zurakowski D, et al. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. J Biol Chem. 2004;279:51323–51330.
   PubMed Web of Science ®Google Scholar
• Zhong JL, Poghosyan Z, Pennington CJ, et al. Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma. Mol Cancer Res. 2008;6:383–394.
   PubMed Web of Science ®Google Scholar
• Sjoblom T, Jones S, Wood LD, et al. The consensus coding sequences of human breast and colorectal cancers. Science. 2006;314(5797):268–274
   PubMed Web of Science ®Google Scholar
• Gomez-Gaviro M, Domínguez-Luis M, Canchado J, et al. Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding. J Immunol. 2007;178(12):8053–8063
   PubMed Web of Science ®Google Scholar
• Weskamp G, Ford JW, Sturgill J, et al. ADAM10 is a principal ‘sheddase’ of the low-affinity immunoglobulin E receptor CD23. Nat Immunol. 2006;7(12):1293–1298
   PubMed Web of Science ®Google Scholar
• Laigaard J, Sørensen T, Fröhlich C, et al. ADAM12: a novel first-trimester maternal serum marker for Down syndrome. Prenat Diagn. 2003;23(13):1086–1091
   PubMed Web of Science ®Google Scholar
• Butler CA, Darragh KM, Currie GP, et al. Variation in lung cancer survival rates between countries: do differences in data reporting contribute? Respir Med. 2006;100:1642–1646.
   PubMed Web of Science ®Google Scholar
• Shibuya K, Inoue M, Lopez AD. Statistical modeling and projections of lung cancer mortality in 4 industrialized countries. Int J Cancer. 2005;117:476–485.
   PubMed Web of Science ®Google Scholar
• Ferlay J, Autier P, Boniol M, et al. Estimates of the cancer incidence and mortality in Europe in 2006. Ann Oncol. 2007;18:581–592.
   PubMed Web of Science ®Google Scholar
• Zheng X, Chopp M, Lu Y, et al. MiR-15b and miR-152 reduce glioma cell invasion and angiogenesis via NRP-2 and MMP-3. Cancer Lett. 2013;329:146–154.
   PubMed Web of Science ®Google Scholar
• Tian L, Zhang Y, Chen Yet al. EMMPRIN is an independent negative prognostic factor for patients with astrocytic glioma. PLoS One. 2013;8:e58069.
   PubMed Web of Science ®Google 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.
   PubMed Web of Science ®Google Scholar
• Sahin U, Weskamp G, Kelly K, et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol. 2004;164(5):769–779
   PubMed Web of Science ®Google Scholar
• Nishimura H, Kim E, Nakanishi T, et al. Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem. 2004;279:34957–34962.
   PubMed Web of Science ®Google Scholar
• Sagane K, Hayakawa K, Kai J, et al. Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice. BMC Neurosci. 2005;6:33.
   PubMed Web of Science ®Google Scholar
• Nishimura H, Cho C, Branciforte DR, et al. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol. 2001;233:204–213.
   PubMed Web of Science ®Google Scholar
• Kelly K, Hutchinson G, Nebenius-Oosthuizen D, et al. Metalloprotease-disintegrin ADAM8: expression analysis and targeted deletion in mice. Dev Dyn. 2005;232:221–231.
   PubMed Web of Science ®Google Scholar
• Namba K, Nishio M, Mori K, et al. Involvement of ADAM9 in multinucleated giant cell formation of blood monocytes. Cell Immunol. 2001;213(2):104–113
   PubMed Web of Science ®Google Scholar
• Zigrino P, Nischt R, Mauch C. The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts. J Biol Chem. 2011;286:6801–6807.
   PubMed Web of Science ®Google Scholar
• Mahimkar RM, Visaya O, Pollock AS, et al. The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins. Biochem J. 2005;385:461–468.
   PubMed Web of Science ®Google Scholar
• Mauch C, Zamek J, Abety AN, et al. Accelerated wound repair in ADAM-9 knockout animals. J Invest Dermatol. 2010;130(8):2120–2130
   PubMed Web of Science ®Google Scholar
• Blobel CP. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch. Cell. 1997;90:589–592.
   PubMed Web of Science ®Google Scholar