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Gene Review

ADAM8  -  ADAM metallopeptidase domain 8

Homo sapiens

Synonyms: ADAM 8, CD156, CD156a, Cell surface antigen MS2, Disintegrin and metalloproteinase domain-containing protein 8, ...
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Disease relevance of ADAM8


Psychiatry related information on ADAM8

  • Sorption of MS2 bacteriophage to layered double hydroxides: effects of reaction time, pH, and competing anions [6].

High impact information on ADAM8

  • Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function [7].
  • Among amino acid codons that require a third-position pyrimidine, there is a significant bias favoring the use of cytidine over uracil in MS2 phage RNA [8].
  • Hybrid proteins containing RS domains fused to the MS2 RNA binding protein were tested in vitro with RNA substrates bearing an MS2 recognition sequence [9].
  • The thermodynamic contribution of a stacking interaction between Tyr85 in MS2 coat protein and a single-stranded pyrimidine in its RNA binding site has been examined [10].
  • Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex [10].

Chemical compound and disease context of ADAM8


Biological context of ADAM8


Anatomical context of ADAM8

  • The ADAM8-dependent release of sCD23 and the endogenous release from B cell lines could be similarly inhibited by a hydroxamic acid, metalloprotease inhibitor compound [21].
  • Here we demonstrate for the first time ADAM8 protein expression on B cells and dendritic cells, and its higher expression on CD14(2+)CD16(-) monocytes compared to CD14(+)CD16(+) cells [16].
  • ADAM8 mRNA and protein are found at low levels throughout the normal mouse CNS, in neurons and oligodendrocytes [22].
  • In the WR CNS regions in which neurodegeneration occurs, ADAM8 is induced in neurons, reactive astrocytes, and activated microglia [22].
  • RT-PCR using ADAM-specific primers enabled us to identify the expression of ADAM 8, 9, 10, 15, 17, and 28 in both osteoclasts and osteoblasts [23].

Associations of ADAM8 with chemical compounds

  • Materials and Methods: Chinese hamster ovary cells (CHO) expressing different integrin subunits were tested for their capacity to bind the disintegrin domain of ADAM8 [24].
  • Addition of antisense (AS) S-oligonucleotides for ADAM8 (1-10 nM) to mouse bone marrow cultures treated with 10(-9) M 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] significantly inhibited OCL formation compared with treatment with the control S-oligonucleotide [25].
  • Electron microscopy studies revealed that MS2 affinity-selected B complexes exhibit a rhombic shape with a maximum dimension of 420 A and are structurally more homogeneous than B complexes treated with heparin [26].
  • Two adducts (MS1 and MS2) bound to the immobilized boronate column indicating the presence of cis-vicinal hydroxyl groups, a configuration which would result from reaction of 7 beta, 8 alpha-dihydroxy-9 alpha, 10 alpha-epoxy-7,8,9,10-tetrahydroBaP (anti-BaPDE) with DNA [27].
  • Chain elongation studies utilizing an MS2 RNA template showed that (-)-carbovir 5'-triphosphate terminated transcription at positions identical to those where dideoxy-GTP terminated [28].

Enzymatic interactions of ADAM8

  • In this report we demonstrate that soluble ADAM8 is an active metalloprotease in vitro and is able to hydrolyse myelin basic protein and a variety of peptide substrates based on the cleavage sites of membrane-bound cytokines, growth factors and receptors which are known to be processed by metalloproteinases [29].

Regulatory relationships of ADAM8

  • The in vivo relevance of the ProteaseSpot method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP [2].

Other interactions of ADAM8

  • The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs [29].
  • The lack of TIMP inhibition of ADAM8 and 9 contrasts with other membrane-associated metalloproteinases characterised to date in this respect (ADAM10, 12, 17, and the membrane-type metalloproteinases) which have been implicated in protein processing at the cell surface [29].
  • We conclude that ADAM8 could contribute to ectodomain shedding of CD23 and may thus be a potential target for therapeutic intervention in allergy and inflammation [21].
  • From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the beta-amyloid precursor protein (APP) [2].
  • The proportion of the serum ADAM8-positive cases defined by our criteria was 63% and that for carcinoembryonic antigen was 57%, indicating equivalent diagnostic power of these two markers [1].

Analytical, diagnostic and therapeutic context of ADAM8


  1. ADAM8 as a novel serological and histochemical marker for lung cancer. Ishikawa, N., Daigo, Y., Yasui, W., Inai, K., Nishimura, H., Tsuchiya, E., Kohno, N., Nakamura, Y. Clin. Cancer Res. (2004) [Pubmed]
  2. Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8. Naus, S., Reipschläger, S., Wildeboer, D., Lichtenthaler, S.F., Mitterreiter, S., Guan, Z., Moss, M.L., Bartsch, J.W. Biol. Chem. (2006) [Pubmed]
  3. Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness. Wildeboer, D., Naus, S., Amy Sang, Q.X., Bartsch, J.W., Pagenstecher, A. J. Neuropathol. Exp. Neurol. (2006) [Pubmed]
  4. Increased expression of a novel osteoclast-stimulating factor, ADAM8, in interface tissue around loosened hip prostheses. Mandelin, J., Li, T.F., Hukkanen, M.V., Liljeström, M., Chen, Z.K., Santavirta, S., Kitti, U., Konttinen, Y.T. J. Rheumatol. (2003) [Pubmed]
  5. ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer. Valkovskaya, N., Kayed, H., Felix, K., Hartmann, D., Giese, N.A., Osinsky, S.P., Friess, H., Kleeff, J. J. Cell. Mol. Med. (2007) [Pubmed]
  6. Sorption of MS2 bacteriophage to layered double hydroxides: effects of reaction time, pH, and competing anions. You, Y., Vance, G.F., Sparks, D.L., Zhuang, J., Jin, Y. J. Environ. Qual. (2003) [Pubmed]
  7. Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function. Atkins, J.F., Steitz, J.A., Anderson, C.W., Model, P. Cell (1979) [Pubmed]
  8. Is there selection against wobble in codon-anticodon pairing? Fitch, W.M. Science (1976) [Pubmed]
  9. Arginine/serine-rich domains of SR proteins can function as activators of pre-mRNA splicing. Graveley, B.R., Maniatis, T. Mol. Cell (1998) [Pubmed]
  10. Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex. LeCuyer, K.A., Behlen, L.S., Uhlenbeck, O.C. EMBO J. (1996) [Pubmed]
  11. Sequence of the A-protein of coliphage MS2. I. Isolation of A-protein, determination of the NH2- and COOH-terminal sequences, isolation and amino acid sequence of the tryptic peptides. Nolf, F.A., Vandekerckhove, J.S., Lenaerts, A.K., Van Montagu, M.C. J. Biol. Chem. (1977) [Pubmed]
  12. Sequence of the A-protein of coliphage MS2. III. Isolation and sequence determination of thermolytic peptides and soluble cyanogen bromide fragments: alignment of 363 amino acid residues of a total of 393. Vandekerckhove, J.S., Van Montagu, M.C. J. Biol. Chem. (1977) [Pubmed]
  13. Crystal structures of MS2 capsids with mutations in the subunit FG loop. Stonehouse, N.J., Valegård, K., Golmohammadi, R., van den Worm, S., Walton, C., Stockley, P.G., Liljas, L. J. Mol. Biol. (1996) [Pubmed]
  14. Bacteriophage inactivation at the air-water-solid interface in dynamic batch systems. Thompson, S.S., Yates, M.V. Appl. Environ. Microbiol. (1999) [Pubmed]
  15. Use of modified diatomaceous earth for removal and recovery of viruses in water. Farrah, S.R., Preston, D.R., Toranzos, G.A., Girard, M., Erdos, G.A., Vasuhdivan, V. Appl. Environ. Microbiol. (1991) [Pubmed]
  16. The detection of ADAM8 protein on cells of the human immune system and the demonstration of its expression on peripheral blood B cells, dendritic cells and monocyte subsets. Richens, J., Fairclough, L., Ghaemmaghami, A.M., Mahdavi, J., Shakib, F., Sewell, H.F. Immunobiology (2007) [Pubmed]
  17. CD156 (human ADAM8): expression, primary amino acid sequence, and gene location. Yoshiyama, K., Higuchi, Y., Kataoka, M., Matsuura, K., Yamamoto, S. Genomics (1997) [Pubmed]
  18. ADAM8 expression in prostate cancer is associated with parameters of unfavorable prognosis. Fritzsche, F.R., Jung, M., Xu, C., Rabien, A., Schicktanz, H., Stephan, C., Dietel, M., Jung, K., Kristiansen, G. Virchows Arch. (2006) [Pubmed]
  19. Expression of ADAMs and Their Inhibitors in Sputum from Patients with Asthma. Paulissen, G., Rocks, N., Quesada-Calvo, F., Gosset, P., Foidart, J.M., Noel, A., Louis, R., Cataldo, D.D. Mol. Med. (2006) [Pubmed]
  20. Leeway and constraints in the forced evolution of a regulatory RNA helix. Olsthoorn, R.C., Licis, N., van Duin, J. EMBO J. (1994) [Pubmed]
  21. Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. Fourie, A.M., Coles, F., Moreno, V., Karlsson, L. J. Biol. Chem. (2003) [Pubmed]
  22. Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration. Schlomann, U., Rathke-Hartlieb, S., Yamamoto, S., Jockusch, H., Bartsch, J.W. J. Neurosci. (2000) [Pubmed]
  23. ADAM gene expression and regulation during human osteoclast formation. Verrier, S., Hogan, A., McKie, N., Horton, M. Bone (2004) [Pubmed]
  24. alpha(9)beta(1): A Novel Osteoclast Integrin That Regulates Osteoclast Formation and Function. Rao, H., Lu, G., Kajiya, H., Garcia-Palacios, V., Kurihara, N., Anderson, J., Patrene, K., Sheppard, D., Blair, H.C., Windle, J.J., Choi, S.J., Roodman, G.D. J. Bone Miner. Res. (2006) [Pubmed]
  25. ADAM8: a novel osteoclast stimulating factor. Choi, S.J., Han, J.H., Roodman, G.D. J. Bone Miner. Res. (2001) [Pubmed]
  26. Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions. Deckert, J., Hartmuth, K., Boehringer, D., Behzadnia, N., Will, C.L., Kastner, B., Stark, H., Urlaub, H., Lührmann, R. Mol. Cell. Biol. (2006) [Pubmed]
  27. Benzo(a)pyrene:DNA adduct formation in normal human mammary epithelial cell cultures and the human mammary carcinoma T47D cell line. Pruess-Schwartz, D., Baird, W.M., Nikbakht, A., Merrick, B.A., Selkirk, J.K. Cancer Res. (1986) [Pubmed]
  28. DNA chain termination activity and inhibition of human immunodeficiency virus reverse transcriptase by carbocyclic 2',3'-didehydro-2',3'-dideoxyguanosine triphosphate. Orr, D.C., Figueiredo, H.T., Mo, C.L., Penn, C.R., Cameron, J.M. J. Biol. Chem. (1992) [Pubmed]
  29. The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs. Amour, A., Knight, C.G., English, W.R., Webster, A., Slocombe, P.M., Knäuper, V., Docherty, A.J., Becherer, J.D., Blobel, C.P., Murphy, G. FEBS Lett. (2002) [Pubmed]
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