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Adam10  -  a disintegrin and metallopeptidase domain 10

Mus musculus

Synonyms: 1700031C13Rik, ADAM 10, Disintegrin and metalloproteinase domain-containing protein 10, Kuz, Kuzbanian protein homolog, ...
 
 
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Disease relevance of Adam10

 

High impact information on Adam10

  • To illustrate the utility of MADM, we show that cerebellar granule cell progenitors are fated at an early stage to produce granule cells with axonal projections limited to specific sublayers of the cerebellar cortex [2].
  • Furthermore, invertebrate models point towards a key role of the ADAM 10 orthologues Kuzbanian and sup-17 in Notch signalling [3].
  • During mouse embryonic development Kuz is expressed mainly in the sympathoadrenal and olfactory neural precursors [1].
  • Once sympathoadrenal cells differentiate into chromaffin cells in the adult adrenal medulla, they no longer express Kuz [1].
 

Other interactions of Adam10

  • We identify ADAM9 and -15 as the proteases responsible for releasing the ADAM10 ectodomain, and Presenilin/gamma-Secretase as the protease responsible for the release of the ADAM10 intracellular domain (ICD) [4].

References

  1. Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. Yavari, R., Adida, C., Bray-Ward, P., Brines, M., Xu, T. Hum. Mol. Genet. (1998) [Pubmed]
  2. Mosaic analysis with double markers in mice. Zong, H., Espinosa, J.S., Su, H.H., Muzumdar, M.D., Luo, L. Cell (2005) [Pubmed]
  3. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. Hartmann, D., de Strooper, B., Serneels, L., Craessaerts, K., Herreman, A., Annaert, W., Umans, L., Lübke, T., Lena Illert, A., von Figura, K., Saftig, P. Hum. Mol. Genet. (2002) [Pubmed]
  4. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase. Tousseyn, T., Thathiah, A., Jorissen, E., Raemaekers, T., Konietzko, U., Reiss, K., Maes, E., Snellinx, A., Serneels, L., Nyabi, O., Annaert, W., Saftig, P., Hartmann, D., De Strooper, B. J. Biol. Chem. (2009) [Pubmed]
 
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