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Cancer Cell Biology

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Adam-9 expression and regulation in human skin melanoma and melanoma cell lines

  1. Paola Zigrino1,†,*,
  2. Cornelia Mauch1,
  3. Jay W. Fox2,
  4. Roswitha Nischt1

Article first published online: 26 APR 2005

DOI: 10.1002/ijc.21087

Issue

International Journal of Cancer

International Journal of Cancer

Volume 116, Issue 6, pages 853–859, 10 October 2005

Additional Information

How to Cite

Zigrino, P., Mauch, C., Fox, J. W. and Nischt, R. (2005), Adam-9 expression and regulation in human skin melanoma and melanoma cell lines. Int. J. Cancer, 116: 853–859. doi: 10.1002/ijc.21087

Author Information

  1. 1

    Department of Dermatology, University of Cologne, Cologne, Germany

  2. 2

    Department of Microbiology, University of Virginia, Charlottesville, VA, USA

  1. †

    Fax: +49 221 4785949.

*Department of Dermatology, University of Cologne, Joseph Stelzmann Str 9, 50931 Cologne, Germany

  1. †

    Fax: +49 221 4785949.

Publication History

  1. Issue published online: 28 JUL 2005
  2. Article first published online: 26 APR 2005
  3. Manuscript Accepted: 7 JAN 2005
  4. Manuscript Received: 15 APR 2004

Funded by

  • Wilhelm Sander-Stiftung. Grant Number: 1999.093.2
  • Deutsche Forschungsgemeinschaft. Grant Number: SFB 589 (University of Cologne)
  • National Institutes of Health. Grant Number: U54 GM64346
  • University of Virginia Cancer Center
  • Polifarma, Ltd

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References

  • 1
    Somerville RP, Oblander SA, Apte SS. Matrix metalloproteinases: old dogs with new tricks. Genome Biol 2003; 4: 216.
  • 2
    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: 33683–9.
  • 3
    Alfandari D, Cousin H, Gaultier A, Smith K, White JM, Darribere T, DeSimone DW Xenopus ADAM 13 is a metalloprotease required for cranial neural crest-cell migration. Curr Biol 2001; 11: 918–30.
  • 4
    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: 594–8.
  • 5
    Schwettmann L, Tschesche H. Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin. Protein Expr Purif 2001; 21: 65–70.
  • 6
    Franzke CW, Tasanen K, Schacke H, Zhou Z, Tryggvason K, Mauch C, Zigrino P, Sunnarborg S, Lee DC, Fahrenholz F, Bruckner-Tuderman L. Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs. EMBO J 2002; 21: 5026–35.
  • 7
    Schlondorff J, Blobel CP. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J Cell Sci 1999; 112: 3603–17.
  • 8
    Roghani M, Becherer JD, Moss ML, Atherton RE, Erdjument-Bromage H, Arribas J, Blackburn RK, Weskamp G, Tempst P, Blobel CP. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J Biol Chem 1999; 274: 3531–40.
  • 9
    Loechel F, Gilpin BJ, Engvall E, Albrechtsen R, Wewer UM. Human ADAM 12 (meltrin alpha) is an active metalloprotease. J Biol Chem 1998; 273: 16993–7.
  • 10
    Peschon JJ, Slack JL, Reddy P, Stocking KL, Sunnarborg SW, Lee DC, Russell WE, Castner BJ, Johnson RS, Fitzner JN, Boyce RW, Nelson N, et al. An essential role for ectodomain shedding in mammalian development. Science 1998; 282: 1281–4.
  • 11
    Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR, Cumano A, Roux P, Black RA, Israel A. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 2000; 5: 207–16.
  • 12
    Howard L, Nelson KK, Maciewicz RA, Blobel CP. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J Biol Chem 1999; 274: 31693–9.
  • 13
    Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003; 17: 7–30.
  • 14
    Nath D, Slocombe PM, Stephens PE, Warn A, Hutchinson GR, Yamada KM, Docherty AJ, Murphy G. Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells. J Cell Sci 1999; 112: 579–87.
  • 15
    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: 2319–28.
  • 16
    Almeida EA, Huovila AP, Sutherland AE, Stephens LE, Calarco PG, Shaw LM, Mercurio AM, Sonnenberg A, Primakoff P, Myles DG, White JM. Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor. Cell 1995; 81: 1095–104.
  • 17
    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.
  • 18
    Weskamp G, Kratzschmar J, Reid MS, Blobel CP. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J Cell Biol 1996; 132: 717–26.
  • 19
    Hotoda N, Koike H, Sasagawa N, Ishiura S. A secreted form of human ADAM9 has an alpha-secretase activity for APP. Biochem Biophys Res Commun 2002; 293: 800–5.
  • 20
    Weskamp G, Cai H, Brodie TA, Higashyama S, Manova K, Ludwig T, Blobel CP. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol Cell Biol 2002; 22: 1537–44.
  • 21
    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: 437–42.
  • 22
    McCulloch DR, Harvey M, Herington AC. The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone. Mol Cell Endocrinol 2000; 167: 11–21.
  • 23
    O'Shea C, McKie N, Buggy Y, Duggan C, Hill AD, McDermott E, O'Higgins N, Duffy MJ. Expression of ADAM-9 mRNA and protein in human breast cancer. Int J Cancer 2003; 105: 754–61.
    Direct Link:
  • 24
    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: 1489–501.
  • 25
    Yavari R, Adida C, Bray-Ward P, Brines M, Xu T. Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. Hum Mol Genet 1998; 7: 1161–7.
  • 26
    Carey TE, Takahashi T, Resnick LA, Oettgen HF, Old LJ. Cell surface antigens of human malignant melanoma: mixed hemadsorption assays for humoral immunity to cultured autologous melanoma cells. Proc Natl Acad Sci USA 1976; 73: 3278–82.
  • 27
    Herlyn D, Adachi K, Koprowski H, Herlyn M. Experimental model of human melanoma metastases. Cancer Treat Res 1991; 54: 105–18.
  • 28
    Luca M, Hunt B, Bucana CD, Johnson JP, Fidler IJ, Bar-Eli M. Direct correlation between MUC18 expression and metastatic potential of human melanoma cells. Melanoma Res 1993; 3: 35–41.
  • 29
    van Muijen GN, Jansen KF, Cornelissen IM, Smeets DF, Beck JL, Ruiter DJ. Establishment and characterization of a human melanoma cell line (MV3) which is highly metastatic in nude mice. Int J Cancer 1991; 48: 85–91.
    Direct Link:
  • 30
    Welch DR, Bisi JE, Miller BE, Conaway D, Seftor EA, Yohem KH, Gilmore LB, Seftor RE, Nakajima M, Hendrix MJ. Characterization of a highly invasive and spontaneously metastatic human malignant melanoma cell line. Int J Cancer 1991; 47: 227–37.
    Direct Link:
  • 31
    Zigrino P, Drescher C, Mauch C. Collagen-induced proMMP-2 activation by MT1-MMP in human dermal fibroblasts and the possible role of alpha2beta1 integrins. Eur J Cell Biol 2001; 80: 68–77.
  • 32
    Sudbeck BD, Parks WC, Welgus HG, Pentland AP. Collagen-stimulated induction of keratinocyte collagenase is mediated via tyrosine kinase and protein kinase C activities. J Biol Chem 1994; 269: 30022–9.
  • 33
    Pantazis P, Bonner WM. Specific alterations in the pattern of histone-3 synthesis during conversion of human leukemic cells to terminally differentiated cells in culture. Differentiation 1984; 28: 186–90.
    Direct Link:
  • 34
    Carlson RO, Martin DM, Feldman EL, Agranoff BW. PKC activity and PKC-alpha mRNA content are reduced in serum-derived human neuroblastoma cells without concomitant induction of differentiation. Exp Cell Res 1993; 207: 340–7.
  • 35
    Cordell JL, Falini B, Erber WN, Ghosh AK, Abdulaziz Z, MacDonald S, Pulford KA, Stein H, Mason DY. Immunoenzymatic labeling of monoclonal antibodies using immune complexes of alkaline phosphatase and monoclonal anti-alkaline phosphatase (APAAP complexes). J Histochem Cytochem 1984; 32: 219–29.
  • 36
    Rosenwald IB, Setkov NA, Kazakov VN, Chen JJ, Ryazanov AG, London IM, Epifanova OI. Transient inhibition of protein synthesis induces expression of proto-oncogenes and stimulates resting cells to enter the cell cycle. Cell Prolif 1995; 28: 631–44.
    Direct Link:
  • 37
    Kurschat P, Zigrino P, Nischt R, Breitkopf K, Steurer P, Klein CE, Krieg T, Mauch C. 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: 21056–62.
  • 38
    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: 14487–97.
  • 39
    Rumpler G, Becker B, Hafner C, McClelland M, Stolz W, Landthaler M, Schmitt R, Bosserhoff A, Vogt T. 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: 761–71.
    Direct Link:
  • 40
    Hornebeck W, Emonard H, Monboisse JC, Bellon G. Matrix-directed regulation of pericellular proteolysis and tumor progression. Semin Cancer Biol 2002; 12: 231–41.
  • 41
    Kenny PA, Bissell MJ. Tumor reversion: correction of malignant behavior by microenvironmental cues. Int J Cancer 2003; 107: 688–95.
    Direct Link:
  • 42
    Kurschat P, Wickenhauser C, Groth W, Krieg T, Mauch C. Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography. J Pathol 2002; 197: 179–87.
    Direct Link:
  • 43
    Fiore E, Fusco C, Romero P, Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene 2002; 21: 5213–23.
  • 44
    Hofmann UB, Westphal JR, Waas ET, Zendman AJ, Cornelissen IM, Ruiter DJ, van Muijen GN. Matrix metalloproteinases in human melanoma cell lines and xenografts: increased expression of activated matrix metalloproteinase-2 (MMP-2) correlates with melanoma progression. Br J Cancer 1999; 81: 774–82.
  • 45
    Karan D, Lin FC, Bryan M, Ringel J, Moniaux N, Lin MF, Batra SK. Expression of ADAMs (a disintegrin and metalloproteases) and TIMP-3 (tissue inhibitor of metalloproteinase-3) in human prostatic adenocarcinomas. Int J Oncol 2003; 23: 1365–71.
  • 46
    Le Pabic H, Bonnier D, Wewer UM, Coutand A, Musso O, Baffet G, Clement B, Theret N. ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling. Hepatology 2003; 37: 1056–66.
    Direct Link:
  • 47
    Nelson KK, Schlondorff J, Blobel CP. Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta. Biochem J 1999; 343: 673–80.
  • 48
    Cairns RA, Khokha R, Hill RP. Molecular mechanisms of tumor invasion and metastasis: an integrated view. Curr Mol Med 2003; 3: 659–71.
  • 49
    McGary EC, Lev DC, Bar-Eli M. Cellular adhesion pathways and metastatic potential of human melanoma. Cancer Biol Ther 2002; 1: 459–65.
  • 50
    Kurschat P, Mauch C. Mechanisms of metastasis. Clin Exp Dermatol 2000; 25: 482–9.
    Direct Link:
  • 51
    Coussens LM, Werb Z. Inflammation and cancer. Nature 2002; 420: 860–7.
  • 52
    Wong WR, Kossodo S, Kochevar IE. Influence of cytokines on matrix metalloproteinases produced by fibroblasts cultured in monolayer and collagen gels. J Formos Med Assoc 2001; 100: 377–82.
  • 53
    Fowlkes JL, Winkler MK. Exploring the interface between metallo-proteinase activity and growth factor and cytokine bioavailability. Cytokine Growth Factor Rev 2002; 13: 277–87.
  • 54
    Flannery CR, Little CB, Caterson B, Hughes CE. Effects of culture conditions and exposure to catabolic stimulators (IL-1 and retinoic acid) on the expression of matrix metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs) by articular cartilage chondrocytes. Matrix Biol 1999; 18: 225–37.
  • 55
    Chang C, Werb Z. The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol 2001; 11: S37–43.
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