Written | 2011-06 | Astrid Evers, Karina Reiss |
Department of Dermatology, Allergology, University Hospital Schleswig Holstein, Campus Kiel, Schittenhelmstrasse 7, Kiel D-24105, Germany |
Identity |
Alias (NCBI) | ADAM18 | CD156B | CSVP | MGC71942 | TACE |
HGNC (Hugo) | ADAM17 |
HGNC Alias symb | cSVP | CD156B |
HGNC Previous name | TACE |
HGNC Previous name | "tumor necrosis factor, alpha, converting enzyme" |
LocusID (NCBI) | 6868 |
Atlas_Id | 572 |
Location | 2p25.1 [Link to chromosome band 2p25] |
Location_base_pair | Starts at 9488486 and ends at 9555830 bp from pter ( according to GRCh38/hg38-Dec_2013) [Mapping ADAM17.png] |
Fusion genes (updated 2017) | Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands) |
ADAM17 (2p25.1) / WWTR1 (3q25.1) | ADAM17 (2p25.1) / YWHAQ (2p25.1) | IAH1 (2p25.1) / ADAM17 (2p25.1) | |
Note | There are several recommendable reviews about ADAM17 and related proteases, for example Blobel, 2005; Arribas and Esselens, 2009; Gooz, 2010; and Saftig and Reiss, 2011. |
DNA/RNA |
Description | The genomic DNA of ADAM17 extends 66505 base pairs with 19 exons. There is only one known transcription variant. |
Transcription | The mRNA of ADAM17 (NM_003183.4) contains 3572 base pairs and the open reading frame spans from bp 184 to bp 2658. Different isoforms due to differential splicing are not known. |
Pseudogene | No pseudogenes have been reported for ADAM17. |
Protein |
Note | ADAM17 belongs to the ADAM (a disintegrin and metalloprotease) family which is part of the adamalysin proteins. The activity and function of several membrane proteins is regulated by the proteolytic release of their ectodomains, a process known as shedding. About 2-4% of the proteins on the cell surface are affected by ectodomain shedding (Arribas and Massague, 1995). Since there are several of functionally and structurally diverse substrates, ADAMs are involved in various cellular processes. They take part in the regulation of cell adhesion, migration, development and signalling and are also implicated in pathologic conditions such as inflammation and cancer. The consequences of ectodomain shedding can vary, depending on the function of the substrate protein. Membrane-bound precursor proteins can be released by ADAMs as mature active molecules, for example ligands of the EGF receptor or cytokines like TNFa (Peschon et al., 1998; Blobel, 2005). Receptors, for example ErbB2 and ErbB4, can also be cleaved by ADAMs and thus become inactive or may still function as soluble decoy receptors (Molina et al., 2001; Vecchi et al., 1998). Contrariwise, receptors like Notch require proteolytic cleavage to generate intracellular signalling fragments that act as transcription factors after translocation to the nucleus. In this case ectodomain shedding is the prerequisite for regulated intramembrane proteolysis (RIP) mediated by intramembrane cleaving enzymes (Pan and Rubin, 1997; Brou et al., 2000). | ||||||||||||||||||||||||||||||||
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The structure of "a disintegrin and metalloproteases" consists of a N-terminal prodomain (aa 1-214) followed by a metalloprotease domain (aa 223-477), a disintegrin domain (aa 484-560) with a cystein-rich region, an epidermal growth factor-like domain (EGF) (aa 571-602), a transmembrane domain (TM) (aa 672-694) and a cytoplasmic tail (aa 695-824) (Arribas and Esselens, 2009 - modified). Amino acid specifications according to Pubmed graphics for ADAM17 (NP_003174.3). | |||||||||||||||||||||||||||||||||
Description | The preproform of ADAM17 contains 824 amino acids (134 kDa). After cleavage of the prodomain by furin or other proprotein convertases, the mature form has a predicted molecular weight of 98 kDa. The prodomain serves as a chaperone and keeps the enzyme in an inactive state during maturation in the trans-Golgi network (Schlöndorff et al., 2000). The catalytic domain contains the characteristic zinc binding motif (HEXXHXXGXXH) and three potential N-glycosylation sites. The disintegrin domain is discussed to be involved in regulation of the catalytic activity of ADAM17 (Li and Fan, 2004; Smith et al., 2002), but might also be involved in interaction with integrins and therefore mediate cell-cell adhesion or cell-matrix interaction. The cytoplasmic tail of ADAM17 was thought to be important in regulation of the enzyme activity because of its potential tyrosine phosphorylation site, but recent studies showed that overexpressed ADAM17 lacking its cytoplasmic domain was able to cleave TNFalpha upon phorbolester stimulation (Reddy et al., 2000; Horiuchi et al., 2007). The transmembrane domain might play a role in regulation of ADAM activity as studies with ADAM-chimera with exchanged transmembrane domains and experiments with plasma membrane modulating stimuli indicate (Le Gall et al., 2010; Reiss et al., 2011). | ||||||||||||||||||||||||||||||||
Expression | ADAM17 is ubiquitously expressed in various tissues, for example in the brain, kidney, heart and skeletal muscles. The expression pattern changes during embryonic development and the adult life (Black et al., 1997). | ||||||||||||||||||||||||||||||||
Localisation | ADAM17 is a type I transmembrane protein, but only 10% of the total protein can be found in the plasma membrane on the cell surface (Schlöndorff et al., 2000). Most of the protein is localised in the endoplasmic reticulum and trans-Golgi network. It is suggested that ADAM17 accumulates in cholesterol rich departments of the plasma membrane (lipid rafts) (Tellier et al., 2006). | ||||||||||||||||||||||||||||||||
Function | ADAM17 knockout mice display a severe phenotype that resembles mice lacking the epidermal growth factor receptor (EGFR) or one of its ligands (TGFalpha, HB-EGF or amphiregulin). Perinatal mortality is probably due to defects in heart development. Because of their catalytic and their disintegrin domain, ADAMs can have both adhesive and proteolytic functions. ADAM17 is best studied for its proteolytic properties and cleaves its substrates in the juxtamembrane region. The proteins processed by ADAM17 have different functions and therefore proteolytic processing can either activate or abrogate processes. For example both receptors and ligands can be cleaved, thus signalling can be either initiated or stopped by ADAM17. | ||||||||||||||||||||||||||||||||
Homology | Homologs of the human ADAM17 are found in various species ranging from other mammalians to primitive chordates like zebrafish. See table 1 for results of NCBI-Blast/blastp with human ADAM17 (NP_003174.3) as query sequence. Its closest relative in the family of human ADAM metalloproteases is ADAM10 (NP_001101.1), but there is only less than 30% amino acid sequence identity according to NCBI-Blast (blastp).
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Mutations |
Note | So far no common germinal or somatic mutation variants are known. |
Implicated in |
Note | |
Entity | Cancer |
Note | Various growth factors necessary for tumor progression and growth are shed by ADAM17 and increased shedding of EGFR ligands was observed in tissues developing a malignant phenotype (Katakowski et al., 2009). ADAM17 is supposed to play a role in different malignancies: increased levels of the enzyme were detected in gastric carcinoma (Yoshimura et al., 2002), primary colon carcinoma (Blanchot-Jossic et al., 2005), skin malignancies (Oh et al., 2009) and ovarian cancer (Tanaka et al., 2005) but its role is best studied in breast cancer (see below). |
Entity | Breast cancer |
Disease | It was shown that overexpression of ADAM17 in breast cancer correlated with TGFalpha expression (Borrell-Pages et al., 2003), metastasis and tumor progression (McGowan et al., 2007) and shorter survival of patients (McGowan et al., 2008). Recent studies by Kenny and Bissell demonstrated that the malignant phenotype of a breast cancer cell line was reverted to a normal phenotype using siRNA against ADAM17 (Kenny and Bissell, 2007). |
Entity | Inflammation |
Note | The identification of ADAM17 as TNFalpha converting enzyme suggested an important role of this metalloprotease in inflammatory diseases with elevated levels of soluble TNFalpha, such as rheumatoid arthritis and inflammatory bowel disease. Indeed, increased enzymatic activity of ADAM17 was shown in tissues of patients with osteoarthritis (Amin, 1999) and rheumatoid arthritis (Ohta et al., 2001). Furthermore ADAM17 was shown to process several factors that are involved in leukocyte recruitment to the site of inflammation. Moreover ADAM17 regulates leukocyte transmigration through the vascular endothelium for example by cleaving adhesion molecules between endothelial cells. The vascular cell adhesion molecule (CC: TXT: V-CAM ID: 42784>) is released by ADAM17 and functions as the ligand of the leukocyte very late antigen 4 (VLA-4 or alpha4beta1 integrin), which is implicated in the leukocyte adhesion to the vascular endothelium (Garton et al., 2003). L-Selectin cleavage by ADAM17 promotes leukocyte migration through the basal membrane after adhering to the endothelium (Faveeuw et al., 2001; Peschon et al., 1998). ADAM17 was also identified as the sheddase of the tight junction molecule JAM-1 between endothelial cells (Koenen et al., 2009). Cleavage of JAM-1 contributes to the passage of leukocytes through the endothelial cell layer and the processed molecule serves as a biomarker of inflammation. |
Disease | - rheumatoid arthritis (see above), - osteoarthritis (see above), - inflammatory bowel disease (high levels of ADAM17 expression were reported in epithelial cells during the active phase of Crohn's disease (Cesaro et al., 2009)), - psoriasis (ADAM17 expression was upregulated in keratinocytes, blood vessels and mast cells from patients (Kawaguchi et al., 2005)), - pulmonary inflammation (reduced invasion of eosinophils in a model of acute allergic lung inflammation after treatment with ADAM17/MMP inhibitors (Trifilieff et al., 2002)). |
Entity | Alzheimer's disease |
Note | The majority of the amyloid precursor protein (APP) is physiologically cleaved by alpha-secretase (ADAM10 or ADAM17). This cleavage leads to the generation of a soluble non-amyloidogenic fragment (sAPPalpha), whereas shedding of APP by beta-secretase produces the amyloidogenic Abeta peptide (Allinson et al., 2003). Accordingly, decreased activity of alpha-secretase results in the formation of amyloid plaques. While ADAM10 represents the most important alpha-secretase, ADAM17 could contribute to APP-processing under certain conditions (Buxbaum et al., 1998; Jorissen et al., 2010). |
Entity | Kidney diseases |
Note | In polycystic kidney disease (PDK) increased activation of the EGF receptor leads to cyst formation and loss of kidney function. These symptoms could be significantly decreased by treatment with ADAM17 inhibitors (Richards et al., 1998; Dell et al., 2001). Which EGFR ligand is responsible in this context remains unclear, but TGFalpha knockout mice were shown to still develop PDK (Nemo et al., 2005). ADAM17 is also involved in chronic kidney disease (CDK) and it is suggested that this is due to the transactivation of EGFR through the GPCR agonist angiotensin-II (Lautrette et al., 2005). In this process ADAM17 is activated by the GPCR and releases TGFalpha, which in turn activates the EGFR. |
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Citation |
This paper should be referenced as such : |
Evers, A ; Reiss, K |
ADAM17 (ADAM metallopeptidase domain 17) |
Atlas Genet Cytogenet Oncol Haematol. 2011;15(12):989-993. |
Free journal version : [ pdf ] [ DOI ] |
Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ] |
ADAM17/YWHAQ (2p25)
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External links |
REVIEW articles | automatic search in PubMed |
Last year publications | automatic search in PubMed |
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