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ADAM33  -  ADAM metallopeptidase domain 33

Homo sapiens

Synonyms: ADAM 33, C20orf153, DJ964F7.1, DKFZp434K0521, Disintegrin and metalloproteinase domain-containing protein 33, ...
 
 
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Disease relevance of ADAM33

  • OBJECTIVES: To assess whether SNPs in ADAM33 are associated with accelerated lung function loss in the general population and with chronic obstructive pulmonary disease (COPD) [1].
  • The potential for therapeutic intervention with ADAM 33 is extremely attractive and further work will not only focus on the specific domains of ADAM 33, but also the mechanisms by which they lead to bronchial hyperreactivity [2].
  • OBJECTIVE: The purpose of this study was to test the association between ADAM33 polymorphisms and Japanese cedar pollinosis (JCPsis), a most common seasonal allergic rhinitis in Japan. METHODS: We conducted a case-control association study among a Japanese population, involving 95 adult individuals with JCPsis and 95 normal healthy controls [3].
  • CONCLUSION: These findings suggest that a variant in ADAM33 is not only important in the development of asthma but also in disease progression, possibly related to enhanced airway remodelling [4].
  • OBJECTIVE: To assess whether genetic functional variants of ADAM33 relate to the susceptibility or some phenotypes in adult patients with bronchial asthma in a Japanese population [5].
 

High impact information on ADAM33

  • A survey of 135 polymorphisms in 23 genes identified the ADAM33 gene as being significantly associated with asthma using case-control, transmission disequilibrium and haplotype analyses (P = 0.04 0.000003) [6].
  • Linkage to the short arm of chromosome 20 in a genome screen was followed by positive tests of association that centre on the gene for a membrane-anchored zinc-dependent metalloproteinase known as ADAM33 [7].
  • The domain structure of the ADAM33 protein gives capabilities of proteolysis, adhesion, cell fusion and intracellular signalling [7].
  • We identified five single nucleotide polymorphisms on three genes previously associated with asthma [interleukin (IL)-4RA, IL-13, ADAM33] and one gene associated with inflammation (cyclooxygenase-2) [8].
  • Of many synthetic peptides tested as potential substrates, four peptides derived from beta-amyloid precursor protein (APP), Kit-ligand-1 (KL-1), tumor necrosis factor-related activation-induced cytokine, and insulin B chain were cleaved by ADAM33; mutation at the catalytic site, E346A, inactivated catalytic activity [9].
 

Chemical compound and disease context of ADAM33

  • In addition, associations were found between ADAM33 polymorphisms and various cedar pollinosis phenotypes including clinical severity, eosinophil counts in nasal secretion and allergen-specific IgE levels in sera, but not total serum IgE levels [3].
 

Biological context of ADAM33

  • METHODS: Children were genotyped for 17 SNPs in ADAM33 [10].
  • OBJECTIVE: We sought to determine whether polymorphisms in ADAM33 are associated with asthma or closely related phenotypes in 4 different asthma populations [11].
  • The occurrence of ADAM33 in embryonic mesenchymal cells suggests that it may be involved in airway wall "modeling" that contributes to the early life origins of asthma [12].
  • OBJECTIVE AND METHODS: To study the role of ADAM33 in asthma, we investigated its expression in normal, asthmatic, and embryonic airways using reverse transcriptase-quantitative polymerase chain reaction and immunochemistry [12].
  • ADAM33 enzyme properties and substrate specificity [13].
 

Anatomical context of ADAM33

  • ADAM33 is expressed in airway smooth muscle (ASM) cells and is suggested to play a role in the function of these cells [14].
  • CONCLUSIONS: Several ADAM33 protein isoforms occur in adult bronchial smooth muscle and in human embryonic bronchi and surrounding mesenchyme, strongly suggesting its importance in smooth muscle development and/or function, which could explain its genetic association with bronchial hyperresponsiveness [12].
  • The splicing and fate of ADAM33 transcripts in primary human airways fibroblasts [15].
  • ADAM33 was expressed in the smooth muscles and basement membranes of almost all the patients with asthma, but was absent in the normal control subjects [16].
  • Our proposals are supported by the recent identification of ADAM33 as an asthma susceptibility gene, the expression of which is abundant in airway fibroblasts and smooth muscle but absent from T lymphocytes or inflammatory cells that infiltrate the airway wall in patients with asthma [17].
 

Associations of ADAM33 with chemical compounds

 

Other interactions of ADAM33

  • CONCLUSION: The expression of ADAM33 by ASM cells is increased in patients with asthma, and its expression may be regulated by IFN-gamma [14].
  • OBJECTIVE: To investigate whether ADAM33 is more highly expressed in ASM cells of patients with asthma than in those of normal subjects, and whether there is any inflammatory mediator (asthma-related cytokine/chemokine) that could modulate the expression of ADAM33 in ASM cells [14].
  • To understand the function of the gene product, the recombinant metalloproteinase domain of human ADAM33 was purified and tested for its substrate cleavage specificity using peptides derived from beta-amyloid precursor protein (APP) [13].
  • Cell-adhesion assays demonstrated that, similar to ADAM28, the ADAM7 disintegrin domain supported alpha4beta1-dependent Jurkat cell adhesion, whereas the ADAM33 disintegrin domain did not [20].
  • Polymorphisms in ADAM33 are associated with allergic rhinitis due to Japanese cedar pollen [3].
 

Analytical, diagnostic and therapeutic context of ADAM33

References

  1. A disintegrin and metalloprotease 33 polymorphisms and lung function decline in the general population. van Diemen, C.C., Postma, D.S., Vonk, J.M., Bruinenberg, M., Schouten, J.P., Boezen, H.M. Am. J. Respir. Crit. Care Med. (2005) [Pubmed]
  2. ADAM 33 and its association with airway remodeling and hyperresponsiveness in asthma. Holgate, S.T., Davies, D.E., Rorke, S., Cakebread, J., Murphy, G., Powell, R.M., Holloway, J.W. Clinical reviews in allergy & immunology. (2004) [Pubmed]
  3. Polymorphisms in ADAM33 are associated with allergic rhinitis due to Japanese cedar pollen. Cheng, L., Enomoto, T., Hirota, T., Shimizu, M., Takahashi, N., Akahoshi, M., Matsuda, A., Dake, Y., Doi, S., Enomoto, K., Yamasaki, A., Fukuda, S., Mao, X.Q., Hopkin, J.M., Tamari, M., Shirakawa, T. Clin. Exp. Allergy (2004) [Pubmed]
  4. Polymorphisms of the ADAM33 gene are associated with accelerated lung function decline in asthma. Jongepier, H., Boezen, H.M., Dijkstra, A., Howard, T.D., Vonk, J.M., Koppelman, G.H., Zheng, S.L., Meyers, D.A., Bleecker, E.R., Postma, D.S. Clin. Exp. Allergy (2004) [Pubmed]
  5. Association between ADAM33 polymorphisms and adult asthma in the Japanese population. Hirota, T., Hasegawa, K., Obara, K., Matsuda, A., Akahoshi, M., Nakashima, K., Shirakawa, T., Doi, S., Fujita, K., Suzuki, Y., Nakamura, Y., Tamari, M. Clin. Exp. Allergy (2006) [Pubmed]
  6. Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness. Van Eerdewegh, P., Little, R.D., Dupuis, J., Del Mastro, R.G., Falls, K., Simon, J., Torrey, D., Pandit, S., McKenny, J., Braunschweiger, K., Walsh, A., Liu, Z., Hayward, B., Folz, C., Manning, S.P., Bawa, A., Saracino, L., Thackston, M., Benchekroun, Y., Capparell, N., Wang, M., Adair, R., Feng, Y., Dubois, J., FitzGerald, M.G., Huang, H., Gibson, R., Allen, K.M., Pedan, A., Danzig, M.R., Umland, S.P., Egan, R.W., Cuss, F.M., Rorke, S., Clough, J.B., Holloway, J.W., Holgate, S.T., Keith, T.P. Nature (2002) [Pubmed]
  7. A new gene for asthma: would you ADAM and Eve it? Cookson, W. Trends Genet. (2003) [Pubmed]
  8. Polymorphisms associated with asthma are inversely related to glioblastoma multiforme. Schwartzbaum, J., Ahlbom, A., Malmer, B., Lönn, S., Brookes, A.J., Doss, H., Debinski, W., Henriksson, R., Feychting, M. Cancer Res. (2005) [Pubmed]
  9. Catalytic activity of human ADAM33. Zou, J., Zhu, F., Liu, J., Wang, W., Zhang, R., Garlisi, C.G., Liu, Y.H., Wang, S., Shah, H., Wan, Y., Umland, S.P. J. Biol. Chem. (2004) [Pubmed]
  10. Polymorphisms in a disintegrin and metalloprotease 33 (ADAM33) predict impaired early-life lung function. Simpson, A., Maniatis, N., Jury, F., Cakebread, J.A., Lowe, L.A., Holgate, S.T., Woodcock, A., Ollier, W.E., Collins, A., Custovic, A., Holloway, J.W., John, S.L. Am. J. Respir. Crit. Care Med. (2005) [Pubmed]
  11. Association of a disintegrin and metalloprotease 33 (ADAM33) gene with asthma in ethnically diverse populations. Howard, T.D., Postma, D.S., Jongepier, H., Moore, W.C., Koppelman, G.H., Zheng, S.L., Xu, J., Bleecker, E.R., Meyers, D.A. J. Allergy Clin. Immunol. (2003) [Pubmed]
  12. ADAM33 expression in asthmatic airways and human embryonic lungs. Haitchi, H.M., Powell, R.M., Shaw, T.J., Howarth, P.H., Wilson, S.J., Wilson, D.I., Holgate, S.T., Davies, D.E. Am. J. Respir. Crit. Care Med. (2005) [Pubmed]
  13. ADAM33 enzyme properties and substrate specificity. Zou, J., Zhang, R., Zhu, F., Liu, J., Madison, V., Umland, S.P. Biochemistry (2005) [Pubmed]
  14. Downregulation of a disintegrin and metalloproteinase 33 by IFN-gamma in human airway smooth muscle cells. Ito, I., Laporte, J.D., Fiset, P.O., Asai, K., Yamauchi, Y., Martin, J.G., Hamid, Q. J. Allergy Clin. Immunol. (2007) [Pubmed]
  15. The splicing and fate of ADAM33 transcripts in primary human airways fibroblasts. Powell, R.M., Wicks, J., Holloway, J.W., Holgate, S.T., Davies, D.E. Am. J. Respir. Cell Mol. Biol. (2004) [Pubmed]
  16. A disintegrin and metalloproteinase 33 protein in patients with asthma: relevance to airflow limitation. Lee, J.Y., Park, S.W., Chang, H.K., Kim, H.Y., Rhim, T., Lee, J.H., Jang, A.S., Koh, E.S., Park, C.S. Am. J. Respir. Crit. Care Med. (2006) [Pubmed]
  17. Airway remodeling in asthma: new insights. Davies, D.E., Wicks, J., Powell, R.M., Puddicombe, S.M., Holgate, S.T. J. Allergy Clin. Immunol. (2003) [Pubmed]
  18. Crystal structure of the catalytic domain of human ADAM33. Orth, P., Reichert, P., Wang, W., Prosise, W.W., Yarosh-Tomaine, T., Hammond, G., Ingram, R.N., Xiao, L., Mirza, U.A., Zou, J., Strickland, C., Taremi, S.S., Le, H.V., Madison, V. J. Mol. Biol. (2004) [Pubmed]
  19. A genome-wide search for quantitative trait loci contributing to variation in seasonal pollen reactivity. Blumenthal, M.N., Langefeld, C.D., Barnes, K.C., Ober, C., Meyers, D.A., King, R.A., Beaty, T.H., Beck, S.R., Bleecker, E.R., Rich, S.S. J. Allergy Clin. Immunol. (2006) [Pubmed]
  20. ADAM disintegrin-like domain recognition by the lymphocyte integrins alpha4beta1 and alpha4beta7. Bridges, L.C., Sheppard, D., Bowditch, R.D. Biochem. J. (2005) [Pubmed]
 
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