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Gene Review

ADAM19  -  ADAM metallopeptidase domain 19

Homo sapiens

Synonyms: ADAM 19, Disintegrin and metalloproteinase domain-containing protein 19, FKSG34, MADDAM, MLTNB, ...
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Disease relevance of ADAM19

  • In brain tumor tissue, ADAM8 and ADAM19 undergo activation by prodomain removal resulting in active proteases [1].
  • ADAM19 in proximal tubules and in peritubular capillaries was associated with interstitial fibrosis (P<0.05) [2].
  • To determine whether ADAM19 is specifically related to CAN, we studied transplant biopsies with and without CAN, acute rejection and non-transplant-related kidney diseases: interstitial fibrosis (IF), interstitial atrophy, glomerular fibrosis and interstitial inflammation [3].

Psychiatry related information on ADAM19


High impact information on ADAM19

  • Essential role for ADAM19 in cardiovascular morphogenesis [5].
  • These findings raise the possibility that mutations in ADAM19 may contribute to human congenital heart valve and septal defects [5].
  • ADAM19 is also highly expressed in osteoblast-like cells in the bone, yet it does not appear to be essential for bone growth and skeletal development [5].
  • In contrast, MADDAM expression was maintained in MOs differentiated along the dendritic cell (DC) pathway and induced in CD34(+)-derived DCs [6].
  • Long-term culture (more than 20 hours) of MOs during macrophage (MAC) differentiation led to a rapid and complete down-regulation of MADDAM expression [6].

Biological context of ADAM19


Anatomical context of ADAM19

  • Adamalysin 19 (a disintegrin and metalloproteinase 19, ADAM19, or meltrin beta) is a plasma membrane metalloproteinase [7].
  • Meltrin beta/ADAM19 is a member of ADAMs (a disintegrin and metalloproteases), which are a family of membrane-anchored glycoproteins that play important roles in fertilization, myoblast fusion, neurogenesis, and proteolytic processing of several membrane-anchored proteins [10].
  • Human ADAM19 (MADDAM) is a molecular marker for human dendritic cells and not expressed in macrophages [11].
  • The ADAM8 and ADAM19 proteins were mainly located in tumor cells and in some tumors in endothelia of blood vessels [1].
  • Normal human kidneys showed constitutive ADAM19 expression in distal tubules and endothelial cells, whereas proximal tubules were negative [2].

Associations of ADAM19 with chemical compounds


Regulatory relationships of ADAM19

  • This report is the first thorough investigation of the intracellular activation of adamalysin 19, demonstrating that furin activated pro-hADAM19 in the secretory pathway via one of the two consecutive furin recognition sites [7].

Other interactions of ADAM19

  • The human protein shows homology with Xenopus ADAM13 (44%), human ADAM19 (40%), and human ADAM12 (39%) [14].
  • ArgBP1 may be the key protein, which accounts for the physiological function of ADAM19 [15].
  • Anti-metalloproteinase and anti-disintegrin domain IgG molecules inhibited the alpha-2-macroglobulin cleavage by hADAM19; however, their pre-immune and anti-pro-domain IgG molecules did not [16].
  • These data suggest that the ADAM19 may be involved in the key processes of glandular secretion, trophoblast invasion and degradation of extracellular matrix during early pregnancy [12].

Analytical, diagnostic and therapeutic context of ADAM19


  1. 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]
  2. ADAM19 expression in human nephrogenesis and renal disease: Associations with clinical and structural deterioration. Melenhorst, W.B., van den Heuvel, M.C., Timmer, A., Huitema, S., Bulthuis, M., Timens, W., van Goor, H. Kidney Int. (2006) [Pubmed]
  3. Upregulation of ADAM19 in chronic allograft nephropathy. Melenhorst, W.B., van den Heuvel, M.C., Stegeman, C.A., van der Leij, J., Huitema, S., van den Berg, A., van Goor, H. American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons. (2006) [Pubmed]
  4. ADAM19 is tightly associated with constitutive Alzheimer's disease APP alpha-secretase in A172 cells. Tanabe, C., Hotoda, N., Sasagawa, N., Sehara-Fujisawa, A., Maruyama, K., Ishiura, S. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  5. Essential role for ADAM19 in cardiovascular morphogenesis. Zhou, H.M., Weskamp, G., Chesneau, V., Sahin, U., Vortkamp, A., Horiuchi, K., Chiusaroli, R., Hahn, R., Wilkes, D., Fisher, P., Baron, R., Manova, K., Basson, C.T., Hempstead, B., Blobel, C.P. Mol. Cell. Biol. (2004) [Pubmed]
  6. Molecular cloning and characterization of a human metalloprotease disintegrin--a novel marker for dendritic cell differentiation. Fritsche, J., Moser, M., Faust, S., Peuker, A., Büttner, R., Andreesen, R., Kreutz, M. Blood (2000) [Pubmed]
  7. Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites. Kang, T., Zhao, Y.G., Pei, D., Sucic, J.F., Sang, Q.X. J. Biol. Chem. (2002) [Pubmed]
  8. Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta. Wei, P., Zhao, Y.G., Zhuang, L., Ruben, S., Sang, Q.X. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  9. Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity. Kang, T., Park, H.I., Suh, Y., Zhao, Y.G., Tschesche, H., Sang, Q.X. J. Biol. Chem. (2002) [Pubmed]
  10. Roles of Meltrin beta /ADAM19 in the processing of neuregulin. Shirakabe, K., Wakatsuki, S., Kurisaki, T., Fujisawa-Sehara, A. J. Biol. Chem. (2001) [Pubmed]
  11. Epigenetic regulation of the dendritic cell-marker gene ADAM19. Ehrnsperger, A., Rehli, M., Thu-Hang, P., Kreutz, M. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  12. Expression of adamalysin 19/ADAM19 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy. Wang, H.X., Zhao, Y.G., Wang, H.M., Yang, Q., Lin, H.Y., Sang, Q.X., Zhu, C. Mol. Hum. Reprod. (2005) [Pubmed]
  13. Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19. Kang, T., Tschesche, H., Amy Sang, Q.X. Exp. Cell Res. (2004) [Pubmed]
  14. Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity. Yoshinaka, T., Nishii, K., Yamada, K., Sawada, H., Nishiwaki, E., Smith, K., Yoshino, K., Ishiguro, H., Higashiyama, S. Gene (2002) [Pubmed]
  15. Screen and identification of proteins interacting with ADAM19 cytoplasmic tail. Huang, L., Feng, L., Yang, L., Zhou, W., Zhao, S., Li, C. Mol. Biol. Rep. (2002) [Pubmed]
  16. Inhibitory antibodies against endopeptidase activity of human adamalysin 19. Zhao, Y.G., Wei, P., Sang, Q.X. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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