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Gene Review

ADAM22  -  ADAM metallopeptidase domain 22

Homo sapiens

Synonyms: ADAM 22, Disintegrin and metalloproteinase domain-containing protein 22, MDC2, Metalloproteinase-disintegrin ADAM22-3, Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2
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Disease relevance of ADAM22


High impact information on ADAM22

  • ADAM22 can act to inhibit cell proliferation, however, it has been suggested that it also acts as an adhesion protein [3].
  • Deletion of both 14-3-3 binding sites and newly identified ER retention motifs restored localization of ADAM22 at the cell surface [3].
  • ADAM22 point mutants lacking functional 14-3-3 protein binding motifs could no longer accumulate efficiently at the cell surface [3].
  • In addition, we show that 14-3-3 proteins interact preferentially with the serine phosphorylated precursor form of ADAM22 [3].
  • The interaction between ADAM22 and 14-3-3 proteins is dependent on phosphorylation of ADAM22, but not of 14-3-3 proteins [3].

Chemical compound and disease context of ADAM22


Biological context of ADAM22

  • Human chromosomal mapping indicated that ADAM22 and ADAM23 mapped to chromosome 7q21 and 2q33, respectively, while the three pseudogenes 1-2, 3-3, and 1-32 mapped to chromosome 14q24.1, 8p23, and 14q24.1, respectively [4].
  • These results strongly demonstrated a functional role for ADAM22/14-3-3 in cell adhesion and spreading [5].
  • Finally, the control of RNA degradation for the normalization of genes of interest was also tested. mRNA expression levels for superoxide dismutase 1 (SOD1) and metalloproteinase domain 22 (ADAM22) were examined at several artificial post-mortem times, and their expression levels compared with those for putative controls beta-actin and GUS [6].
  • Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission [7].
  • Using a classical mutagenesis and selection approach we have isolated a Nonomuraea sp. ATCC 39727 mutant strain able to direct production towards new A40926 analogues dechloro-A40926 (DDC) lacking two chlorine atoms and the two monochloro-A40926 (MDC1 and MDC2) that are not produced fermenting the wild type strain [8].

Anatomical context of ADAM22


Associations of ADAM22 with chemical compounds


Other interactions of ADAM22

  • These findings suggest that three murine cDNAs that we have isolated are the murine ADAM11, ADAM22 and ADAM23 cDNAs [10].

Analytical, diagnostic and therapeutic context of ADAM22

  • In this paper, we report the cloning and sequence analysis of two novel additional members of this family, which we have termed MDC2 and MDC3 [11].
  • We identified three 14-3-3 protein members by a yeast two-hybrid screen and show by co-immunoprecipitation that the cytoplasmic domain of ADAM22 can interact with all six 14-3-3 proteins expressed in the brain [3].
  • METHODS: Specimens of low- and high-grade gliomas and normal brain were analyzed for ADAM11 and ADAM22 expression using Western blotting [1].
  • To elucidate the physiological functions of ADAM22, we employed gene targeting to generate ADAM22 knockout mice [2].
  • The three main subsets of BDC were distinguished by flow cytometry: BDCA-2(+)/CD123(+)/HLA-DR(+) (plasmacytoid, PDC) and two myeloid subtypes BDCA-1(+)/CD11c(+)/HLA-DR(+) (MDC1) and BDCA-3(+)/CD32(-)/HLA-DR(+) (MDC2) [12].


  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. Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice. Sagane, K., Hayakawa, K., Kai, J., Hirohashi, T., Takahashi, E., Miyamoto, N., Ino, M., Oki, T., Yamazaki, K., Nagasu, T. BMC neuroscience [electronic resource]. (2005) [Pubmed]
  3. Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members. Gödde, N.J., D'Abaco, G.M., Paradiso, L., Novak, U. J. Cell. Sci. (2006) [Pubmed]
  4. The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. Poindexter, K., Nelson, N., DuBose, R.F., Black, R.A., Cerretti, D.P. Gene (1999) [Pubmed]
  5. ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3. Zhu, P., Sang, Y., Xu, H., Zhao, J., Xu, R., Sun, Y., Xu, T., Wang, X., Chen, L., Feng, H., Li, C., Zhao, S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  6. TaqMan PCR assay in the control of RNA normalization in human post-mortem brain tissue. Barrachina, M., Castaño, E., Ferrer, I. Neurochem. Int. (2006) [Pubmed]
  7. Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. Fukata, Y., Adesnik, H., Iwanaga, T., Bredt, D.S., Nicoll, R.A., Fukata, M. Science (2006) [Pubmed]
  8. Production and characterization of monochlorinated and dechlorinated A40926 derivatives. Beltrametti, F., Lazzarini, A., Brunati, C., Marazzi, A., Jovetic, S., Selva, E., Marinelli, F. J. Antibiot. (2003) [Pubmed]
  9. The number and distribution of blood dendritic cells in the epidermis and dermis of healthy human subjects. Narbutt, J., Lesiak, A., Sysa-Jedrzejowska, A., Smolewski, P., Robak, T., Zalewska, A. Folia Histochem. Cytobiol. (2006) [Pubmed]
  10. Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23. Sagane, K., Yamazaki, K., Mizui, Y., Tanaka, I. Gene (1999) [Pubmed]
  11. Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. Sagane, K., Ohya, Y., Hasegawa, Y., Tanaka, I. Biochem. J. (1998) [Pubmed]
  12. Exposure to low doses of solar-simulated radiation induces an increase in the myeloid subtype of blood dendritic cells. Narbutt, J., Skibinska, M., Lesiak, A., Wozniacka, A., Sysa-Jedrzejowska, A., Cebula, B., Robak, T., Smolewski, P. Scand. J. Immunol. (2004) [Pubmed]
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