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Original Article

ADAM-9, ADAM-15, and ADAM-17 are upregulated in macrophages in advanced human atherosclerotic plaques in aorta and carotid and femoral arteries—Tampere vascular study

, PhD , MD, , , , , , , , , , , , , , , & show all
Pages 279-290 | Received 23 Feb 2008, Published online: 08 Jul 2009

References

  • Herren B, Raines EW, Ross R. Expression of a disintegrin-like protein in cultured human vascular cells and in vivo. FASEB J. 1997; 11: 173–80
  • Stary HC, Chandler AB, Dinsmore RE, Fuster V, Glagov S, Insull W, Jr, et al. A definition of advanced types of atherosclerotic lesions and a histological classification of atherosclerosis. A report from the Committee on Vascular Lesions of the Council on Arteriosclerosis, American Heart Association. Circulation. 1995; 92: 1355–74
  • Wolfsberg TG, Straight PD, Gerena RL, Huovila AP, Primakoff P, Myles DG, et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol. 1995; 169: 378–83
  • Blobel CP. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol. 2005; 6: 32–43
  • Huovila AP, Turner AJ, Pelto-Huikko M, Karkkainen I, Ortiz RM. Shedding light on ADAM metalloproteases. Trends Biochem Sci. 2005; 30: 413–22
  • Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 2003; 17: 7–30
  • Dreux AC, Lamb DJ, Modjtahedi H, Ferns GA. The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis. Atherosclerosis. 2006; 186: 38–53
  • Popa C, Netea MG, van Riel PL, van der Meer JW, Stalenhoef AF. The role of TNF-alpha in chronic inflammatory conditions, intermediary metabolism, and cardiovascular risk. J Lipid Res. 2007; 48: 751–62
  • 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
  • Karadag A, Zhou M, Croucher PI. ADAM-9 (MDC-9/meltrin-gamma), a member of the a disintegrin and metalloprotease family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the alpha(v)beta5 integrin. Blood. 2006; 107: 3271–8
  • Jasiulionis MG, Chammas R, Ventura AM, Travassos LR, Brentani RR. alpha6beta1-Integrin, a major cell surface carrier of beta1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state. Cancer Res. 1996; 56: 1682–9
  • Gimond C, Baudoin C, van der Neut R, Kramer D, Calafat J, Sonnenberg A. Cre-loxP-mediated inactivation of the alpha6A integrin splice variant in vivo: evidence for a specific functional role of alpha6A in lymphocyte migration but not in heart development. J Cell Biol. 1998; 143: 253–66
  • Shaw LM, Mercurio AM. Regulation of cellular interactions with laminin by integrin cytoplasmic domains: the A and B structural variants of the alpha 6 beta 1 integrin differentially modulate the adhesive strength, morphology, and migration of macrophages. Mol Biol Cell. 1994; 5: 679–90
  • Al-Fakhri N, Wilhelm J, Hahn M, Heidt M, Hehrlein FW, Endisch AM, et al. Increased expression of disintegrin-metalloproteases ADAM-15 and ADAM-9 following upregulation of integrins alpha5beta1 and alphavbeta3 in atherosclerosis. J Cell Biochem. 2003; 89: 808–23
  • Zhang XP, Kamata T, Yokoyama K, Puzon-McLaughlin W, Takada Y. Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3. J Biol Chem. 1998; 273: 7345–50
  • Langer H, May AE, Bultmann A, Gawaz M. ADAM 15 is an adhesion receptor for platelet GPIIb-IIIa and induces platelet activation. Thromb Haemost. 2005; 94: 555–61
  • Horiuchi K, Weskamp G, Lum L, Hammes HP, Cai H, Brodie TA, et al. Potential role for ADAM15 in pathological neovascularization in mice. Mol Cell Biol. 2003; 23: 5614–24
  • Charrier-Hisamuddin L, Laboisse CL, Merlin D. ADAM-15: a metalloprotease that mediates inflammation. FASEB J. 2008; 22: 641–53
  • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, et al. A metalloprotease disintegrin that releases tumour-necrosis factor-alpha from cells. Nature. 1997; 385: 729–33
  • Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, et al. Cloning of a disintegrin metalloprotease that processes precursor tumour-necrosis factor-alpha. Nature. 1997; 385: 733–6
  • Canault M, Peiretti F, Kopp F, Bonardo B, Bonzi MF, Coudeyre JC, et al. The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: possible contribution to elevated plasma levels of soluble TNF alpha receptors. Atherosclerosis. 2006; 187: 82–91
  • Canault M, Leroyer AS, Peiretti F, Leseche G, Tedgui A, Bonardo B, et al. Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1. Am J Pathol. 2007; 171: 1713–23
  • Condon TP, Flournoy S, Sawyer GJ, Baker BF, Kishimoto TK, Bennett CF. ADAM17 but not ADAM10 mediates tumor necrosis factor-alpha and L-selectin shedding from leukocyte membranes. Antisense Nucleic Acid Drug Dev. 2001; 11: 107–16
  • Gomez-Gaviro M, Dominguez-Luis M, Canchado J, Calafat J, Janssen H, Lara-Pezzi E, et al. Expression and regulation of the metalloprotease ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding. J Immunol. 2007; 178: 8053–63
  • Rovida E, Paccagnini A, Del Rosso M, Peschon J, Dello Sbarba P. TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation. J Immunol. 2001; 166: 1583–9
  • Laaksonen R, Katajamaa M, Paiva H, Sysi-Aho M, Saarinen L, Junni P, et al. A systems biology strategy reveals biological pathways and plasma biomarker candidates for potentially toxic statin-induced changes in muscle. PLoS ONE. 2006; 1: e97
  • Huovila AP, Eder AM, Fuller SD. Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment. J Cell Biol. 1992; 118: 1305–20
  • Shi SR, Key ME, Kalra KL. Antigen retrieval in formalin-fixed, paraffin-embedded tissues: an enhancement method for immunohistochemical staining based on microwave oven heating of tissue sections. J Histochem Cytochem. 1991; 39: 741–8
  • Izumi Y, Hirata M, Hasuwa H, Iwamoto R, Umata T, Miyado K, 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: 7260–72
  • Miyamoto S, Yagi H, Yotsumoto F, Kawarabayashi T, Mekada E. Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy. Cancer Sci. 2006; 97: 341–7
  • Nath D, Slocombe PM, Stephens PE, Warn A, Hutchinson GR, Yamada KM, et al. Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells. J Cell Sci. 1999; 112(Pt 4)579–87
  • Moiseeva EP. Adhesion receptors of vascular smooth muscle cells and their functions. Cardiovasc Res. 2001; 52: 372–86
  • Mosnier JF, Jarry A, Bou-Hanna C, Denis MG, Merlin D, Laboisse CL. ADAM15 upregulation and interaction with multiple binding partners in inflammatory bowel disease. Lab Invest. 2006; 86: 1064–73
  • Maury CP, Teppo AM. Circulating tumour necrosis factor-alpha (cachectin) in myocardial infarction. J Intern Med. 1989; 225: 333–6
  • Heinisch RH, Zanetti CR, Comin F, Fernandes JL, Ramires JA, Serrano CV, Jr. Serial changes in plasma levels of cytokines in patients with coronary artery disease. Vasc Health Risk Manag. 2005; 1: 245–50
  • Barath P, Fishbein MC, Cao J, Berenson J, Helfant RH, Forrester JS. Detection and localization of tumor necrosis factor in human atheroma. Am J Cardiol. 1990; 65: 297–302
  • Moss ML, Bartsch JW. Therapeutic benefits from targeting of ADAM family members. Biochemistry. 2004; 43: 7227–35

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