The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ADAM11  -  ADAM metallopeptidase domain 11

Homo sapiens

Synonyms: ADAM 11, Disintegrin and metalloproteinase domain-containing protein 11, MDC, Metalloproteinase-like, disintegrin-like, and cysteine-rich protein
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ADAM11

  • A related protein, ADAM11, has only a minor effect on cell growth, and its expression is unchanged in low- and high-grade gliomas [1].
  • CONCLUSIONS: Our results show that especially for primary tumors containing stromal elements, the assessment of mRNA expression levels of ADAM-9 and ADAM-11 could be useful to identify patients with recurrent breast cancer who are likely to benefit or fail from tamoxifen therapy [2].
  • By contrast, the absolute number and median frequency of MDC in HIV-infected individuals were similar to those observed in uninfected controls, while a significant decrease was present in subjects with >5000 HIV-1 copies/ml [3].
  • Myeloid, CD1a-sorted dendritic cells (MDC) productively replicated human immunodeficiency virus strains encoding envelope genes of either primary X4R5 or R5 strains for up to 45 days [4].
  • The gene locus for congenital muscular dystrophy 1B, MDC 1B, on chromosome 1q42 was also excluded [5].

Psychiatry related information on ADAM11

  • However, since all abnormal ultrasound scans were found in children with a mitochondrial disorder, and no significant correlation with the MDC score was found, muscle ultrasound can be used complementary to this scoring system to facilitate the decision-making in pursuing further invasive diagnostics [6].

High impact information on ADAM11

  • Rearrangements in both tumours involve multiple exons and disrupt the coding region of the new MDC [7].
  • Such stimulation depended on the presence of low levels of primary agonists such as adenosine diphosphate (ADP) and thrombin, or others like epinephrine (EPI) and macrophage-derived chemokine (MDC, CCL22) [8].
  • We report here the identification of MDC-L (ADAM 23), a novel member of the MDC protein family [9].
  • Metalloprotease disintegrins (a disintegrin and metalloprotease (ADAM) and metalloprotease, disintegrin, cysteine-rich proteins (MDC)) are a family of membrane-anchored glycoproteins that function in diverse biological processes, including fertilization, neurogenesis, myogenesis, and ectodomain processing of cytokines and other proteins [10].
  • To identify MDC proteins expressed in human lymph node, a polymerase chain reaction-based strategy combined with degenerate oligonucleotide primers was employed [9].

Chemical compound and disease context of ADAM11


Biological context of ADAM11

  • The putative tumour suppressor gene MDC (ADAM11) is expressed at very low levels in all cells examined [11].
  • Similarly analyzed were the effects on cell proliferation of bacterially expressed glutathione S-transferase fusion proteins with the disintegrin domain of ADAM11 and ADAM22 [1].
  • The metalloprotease disintegrin cysteine-rich (MDC) proteins are a recently identified family of transmembrane proteins that function in proteolytic processing of cell surface molecules and in cell adhesion [9].
  • A recently identified gene encoding a metalloprotease-like, disintegrin-like, cysteine-rich protein (MDC) represents a candidate tumor suppressor gene for human breast cancer based on its location within a minimal region of chromosome 17q21 previously defined by tumor deletion mapping [12].
  • Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing [12].

Anatomical context of ADAM11

  • Since lymphocytes must interact with a constantly changing environment, we hypothesized that lymphocytes would express unique MDC proteins [9].
  • Cell-free supernatant collected from long-term infected MDC, which had been exposed to an X4R5 virus 45 days earlier, was still infectious when placed over activated T cells [4].
  • The rate of sequestration was never slower than that of controls, indicating that MDC did not decrease the ability of Sertoli cells to sequester 125I-hFSH [13].
  • METHODS: The MDC system is composed of a light source, a colposcope, and a video rate color CCD camera with a frame grabber and takes approximately less than 1 min to make images of the cervix [14].
  • We now describe the cloning, sequence determination and characterization of transcripts encoding the human and macaque (Macaca fascicularis) orthologues of a novel member of the MDC family (eMDC II) which is abundantly-expressed in the epididymis [15].

Associations of ADAM11 with chemical compounds

  • Pooled data from several minor controlled trials performed during the last 13 years which have shown consistent improvement of myocardial function, specifically in patients with idiopathic dilated cardiomyopathy, have recently been confirmed by two major trials using the selective beta-blockers metoprolol (MDC trial) and bisoprolol (CIBIS trial) [16].
  • The C-terminal 10 residues of the MDC peptide behave in solution in a manner identical to that of a 10-residue peptide with the same sequence; a highly specific local interaction between an aromatic ring and a glycine amide proton appears to be retained in the longer peptide [17].
  • The effect of replacement of a cysteine residue in the middle of the sequence with an alanine was explored by the comparison of the MDC peptide and a 16-residue peptide representing the sequence of the D-helix alone, both containing the change Cys99Ala [17].
  • The CD spectrum in TFE shows an increase in the proportion of helix, to an overall maximum of approximately 55% helix at 50% v/v TFE, corresponding to approximately 100% helix in the D-helix sequence of the peptide, since the N and C termini of the MDC peptide are not helical according to the NMR spectra [17].
  • The evolution of the Metalloproteinase Disintegrin Cysteine-rich (MDC) gene family and that of the mammalian Matrix-degrading Metalloproteinases (MMPs) are compared [18].

Other interactions of ADAM11


Analytical, diagnostic and therapeutic context of ADAM11

  • ADAM-11 transcript was not detected by Northern blotting possibly due to low levels of ADAM-11 mRNA expression [21].
  • METHODS: Specimens of low- and high-grade gliomas and normal brain were analyzed for ADAM11 and ADAM22 expression using Western blotting [1].
  • There was a decrease of 34% in the combined number of deaths and patients needing a heart transplantation (P = 0.058) in the MDC trial [16].
  • The frequencies of plasmacytoid DC (PDC) and myeloid DC (MDC) were estimated in 63 patients with CHC and 34 normal controls using four-colour flow cytometry [22].
  • CONCLUSION: In the absence of Neuroform stent support, aneurysms embolized with the MDC system demonstrated a significant rate of recanalization [23].


  1. ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain. D'Abaco, G.M., Ng, K., Paradiso, L., Godde, N.J., Kaye, A., Novak, U. Neurosurgery (2006) [Pubmed]
  2. How ADAM-9 and ADAM-11 differentially from estrogen receptor predict response to tamoxifen treatment in patients with recurrent breast cancer: a retrospective study. Sieuwerts, A.M., Meijer-van Gelder, M.E., Timmermans, M., Trapman, A.M., Garcia, R.R., Arnold, M., Goedheer, A.J., Portengen, H., Klijn, J.G., Foekens, J.A. Clin. Cancer Res. (2005) [Pubmed]
  3. Persistent decreases in blood plasmacytoid dendritic cell number and function despite effective highly active antiretroviral therapy and increased blood myeloid dendritic cells in HIV-infected individuals. Chehimi, J., Campbell, D.E., Azzoni, L., Bacheller, D., Papasavvas, E., Jerandi, G., Mounzer, K., Kostman, J., Trinchieri, G., Montaner, L.J. J. Immunol. (2002) [Pubmed]
  4. Long-term productive human immunodeficiency virus infection of CD1a-sorted myeloid dendritic cells. Popov, S., Chenine, A.L., Gruber, A., Li, P.L., Ruprecht, R.M. J. Virol. (2005) [Pubmed]
  5. Congenital muscular dystrophy with adducted thumbs, ptosis, external ophthalmoplegia, mental retardation and cerebellar hypoplasia: a novel form of CMD. Voit, T., Parano, E., Straub, V., Schröder, J.M., Schaper, J., Pavone, P., Falsaperla, R., Pavone, L., Herrmann, R. Neuromuscul. Disord. (2002) [Pubmed]
  6. Skeletal muscle ultrasonography in children with a dysfunction in the oxidative phosphorylation system. Pillen, S., Morava, E., Van Keimpema, M., Ter Laak, H.J., De Vries, M.C., Rodenburg, R.J., Zwarts, M.J. Neuropediatrics. (2006) [Pubmed]
  7. A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. Emi, M., Katagiri, T., Harada, Y., Saito, H., Inazawa, J., Ito, I., Kasumi, F., Nakamura, Y. Nat. Genet. (1993) [Pubmed]
  8. LDL oxidized by hypochlorous acid causes irreversible platelet aggregation when combined with low levels of ADP, thrombin, epinephrine, or macrophage-derived chemokine (CCL22). Coleman, L.G., Polanowska-Grabowska, R.K., Marcinkiewicz, M., Gear, A.R. Blood (2004) [Pubmed]
  9. MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. Roberts, C.M., Tani, P.H., Bridges, L.C., Laszik, Z., Bowditch, R.D. J. Biol. Chem. (1999) [Pubmed]
  10. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. Howard, L., Nelson, K.K., Maciewicz, R.A., Blobel, C.P. J. Biol. Chem. (1999) [Pubmed]
  11. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Wu, E., Croucher, P.I., McKie, N. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  12. Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing. Katagiri, T., Harada, Y., Emi, M., Nakamura, Y. Cytogenet. Cell Genet. (1995) [Pubmed]
  13. Effect of transglutaminase substrates and polyamines on the cellular sequestration and processing of follicle-stimulating hormone by rat Sertoli cells. Dias, J.A. Biol. Reprod. (1986) [Pubmed]
  14. Results of a pilot study of multispectral digital colposcopy for the in vivo detection of cervical intraepithelial neoplasia. Milbourne, A., Park, S.Y., Benedet, J.L., Miller, D., Ehlen, T., Rhodes, H., Malpica, A., Matisic, J., Van Niekirk, D., Atkinson, E.N., Hadad, N., Mackinnon, N., Macaulay, C., Richards-Kortum, R., Follen, M. Gynecol. Oncol. (2005) [Pubmed]
  15. Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis. Jury, J.A., Perry, A.C., Hall, L. Mol. Hum. Reprod. (1999) [Pubmed]
  16. Adrenergic beta-blocking agents in congestive heart failure due to idiopathic dilated cardiomyopathy. Waagstein, F. Eur. Heart J. (1995) [Pubmed]
  17. Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrin. Reymond, M.T., Huo, S., Duggan, B., Wright, P.E., Dyson, H.J. Biochemistry (1997) [Pubmed]
  18. Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution. Moura-da-Silva, A.M., Theakston, R.D., Crampton, J.M. J. Mol. Evol. (1996) [Pubmed]
  19. Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23. Sagane, K., Yamazaki, K., Mizui, Y., Tanaka, I. Gene (1999) [Pubmed]
  20. Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin. Schwettmann, L., Tschesche, H. Protein Expr. Purif. (2001) [Pubmed]
  21. The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone. McCulloch, D.R., Harvey, M., Herington, A.C. Mol. Cell. Endocrinol. (2000) [Pubmed]
  22. Decreased interferon-alpha production and impaired T helper 1 polarization by dendritic cells from patients with chronic hepatitis C. Murakami, H., Akbar, S.M., Matsui, H., Horiike, N., Onji, M. Clin. Exp. Immunol. (2004) [Pubmed]
  23. Durability of aneurysm embolization with matrix detachable coils. Fiorella, D., Albuquerque, F.C., McDougall, C.G. Neurosurgery (2006) [Pubmed]
WikiGenes - Universities