ADAM10

Last updated on: 25.03.2022

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DefinitionThis section has been translated automatically.

ADAM10 is the acronym for "A Disintegrin And Metalloprotease Domain 10", a transmembrane protease of the ADAM (metalloproteinase) family. The protein ADAM 10 is encoded by a gene of the same name located on chromosome 15q21.3.

Members of the ADAM family are cell surface proteins with a unique structure that possess both potential adhesion and protease domains (sheddases). Sheddases primarily serve to cleave membrane proteins at the cellular surface. Once cleaved, the sheddases release soluble ectodomains with altered location and function (Moss ML et al. 2004; Nagano O et al. 2004).

Alternative splicing of the ADAM10 gene results in multiple transcript variants encoding different proteins that may have similar function. Related signaling pathways include EPHA forward signaling and immune response and the "IL-6 signaling pathway." An important paralog of this gene is ADAM17. ADAM10 is predominantly involved in constitutive cleavage of proteins, whereas ADAM17 mediates inducible cleavage (Ludwig A et al. 2005).

General informationThis section has been translated automatically.

Other Functions:

The protease ADAM 10 cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. The protease is responsible for the proteolytic release of several other cell surface proteins, including heparin-binding epidermal growth-like factor, as well as ephrin-A2, CD44 and CDH2 . ADAM10 is responsible for the constitutive and regulated alpha-secretase cleavage of amyloid precursor proteins.

Furthermore, ADAM10 is involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles. The latter suggests its vesicle-based protease activity. Also controls proteolytic processing of Notch and mediates lateral inhibition during neurogenesis . ADAM10 mediates proteolytic cleavage of LAG3, leading to release of the soluble form of LAG3.

ADAM10 mediates the proteolytic cleavage of IL6R and IL11RA, resulting in the release of the soluble forms of IL6R and IL11RA. Furthermore, the protease cleaves TREM2, leading to cleavage of the TREM2 ectodomain .

Microbiology: A number of different proteins on the surface of Plasmodium falciparum, the malaria parasite, help the parasite bind to red blood cells. However, once bound to the host's blood cells, the parasites need to shed these "sticky" surface proteins, otherwise their entry into the cell would be hindered. They accomplish this with the help of an ADAM metallopeptidase (Sheddase- PfSUB2 ). Once these proteins are removed, the parasite gains access to a red blood cell. The entire invasion takes about 30 seconds and without this ADAM metallopeptidase, malaria would be ineffective at invading red blood cells (Collins CR et al. 2020)

ADAM10 is involved in the development and maturation of the glomerular and coronary vasculature. It promotes columnar cell separation during development of the cochlear organ of Corti by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions .

Clinical pictureThis section has been translated automatically.

Diseases associated with ADAM10 include.

LiteratureThis section has been translated automatically.

  1. Blobel CP (2005). ADAMs: key components in EGFR signalling and development. Nature Reviews Molecular Cell Biology 6: 32-43.
  2. Collins CR et al (2020) The malaria parasite sheddase SUB2 governs host red blood cell membrane sealing at invasion. Elife 9:e61121.
  3. Ludwig A et al. (2005) Metalloproteinase inhibitors for the disintegrin-like metalloproteinases ADAM10 and ADAM17 that differentially block constitutive and phorbol ester-inducible shedding of cell surface molecules. Comb Chem High Throughput Screen 8:161-171.
  4. Moss ML et al (2004) Therapeutic benefits from targeting of ADAM family members. Biochemistry 43: 7227-7235.
  5. Nagano O et al (2004) Mechanism and biological significance of CD44 cleavage. Cancer Science 95: 930-935.

Last updated on: 25.03.2022