ADAM10

Summary

Gene Symbol: ADAM10
Description: ADAM metallopeptidase domain 10
Alias: AD10, AD18, CD156c, CDw156, HsT18717, MADM, RAK, kuz, disintegrin and metalloproteinase domain-containing protein 10, a disintegrin and metalloprotease domain 10, kuzbanian protein homolog, mammalian disintegrin-metalloprotease
Species: human
Products:     ADAM10

Top Publications

  1. Hakulinen J, Keski Oja J. ADAM10-mediated release of complement membrane cofactor protein during apoptosis of epithelial cells. J Biol Chem. 2006;281:21369-76 pubmed
    ..Both the metalloproteinase inhibitor GM6001 and RNA interference of ADAM10 completely prevented the release of sCD46 and increased the expression of vCD46 on HaCaT cell vesicles, suggesting ..
  2. Marcello E, Gardoni F, Mauceri D, Romorini S, Jeromin A, Epis R, et al. Synapse-associated protein-97 mediates alpha-secretase ADAM10 trafficking and promotes its activity. J Neurosci. 2007;27:1682-91 pubmed
    ..a protein involved in dynamic trafficking of proteins to the excitatory synapse, is responsible for driving ADAM10 (a disintegrin and metalloproteinase 10, the most accredited candidate for alpha-secretase) to the postsynaptic ..
  3. Kavanagh D, McKay G, Patterson C, McKnight A, Maxwell A, Savage D. Association analysis of Notch pathway signalling genes in diabetic nephropathy. Diabetologia. 2011;54:334-8 pubmed publisher
    ..We assessed single-nucleotide polymorphisms (SNPs; n = 42) in four of these key genes (JAG1, HES1, NOTCH3 and ADAM10) for association with diabetic nephropathy using a case-control design...
  4. Xu D, Sharma C, Hemler M. Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein. FASEB J. 2009;23:3674-81 pubmed publisher
    Using mass spectrometry, we identified ADAM10 (a membrane-associated metalloproteinase) as a partner for TSPAN12, a tetraspanin protein...
  5. Janes P, Saha N, Barton W, Kolev M, Wimmer Kleikamp S, Nievergall E, et al. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell. 2005;123:291-304 pubmed
    ..Cleavage of ephrin-A2 by the ADAM10 membrane metalloprotease enables contact repulsion between Eph- and ephrin-expressing cells...
  6. Endres K, Fahrenholz F. Upregulation of the alpha-secretase ADAM10--risk or reason for hope?. FEBS J. 2010;277:1585-96 pubmed publisher
    A decade ago, a disintegrin and metalloproteinase 10 (ADAM10) was identified as an alpha-secretase and as a key proteinase in the processing of the amyloid precursor protein...
  7. Ebsen H, Schröder A, Kabelitz D, Janssen O. Differential surface expression of ADAM10 and ADAM17 on human T lymphocytes and tumor cells. PLoS ONE. 2013;8:e76853 pubmed publisher
    ..The crucial role of ADAM proteases (e.g. ADAM10 and 17) for mammalian development became evident from respective knockout mice, that displayed pre- or perinatal ..
  8. Wang Y, Ye Z, Li L, Zhao Z, Shao Q, Tao H. ADAM 10 is associated with gastric cancer progression and prognosis of patients. J Surg Oncol. 2011;103:116-23 pubmed publisher
    ..ADAM 10 and C-erbB-2 proteins could be useful markers to predict tumor progression and prognosis. ..
  9. Pan Y, Han C, Wang C, Hu G, Luo C, Gan X, et al. ADAM10 promotes pituitary adenoma cell migration by regulating cleavage of CD44 and L1. J Mol Endocrinol. 2012;49:21-33 pubmed publisher
    b>ADAM10 is a metalloproteinase that regulates invasiveness in many tumors. Here, we found that ADAM10 expression correlates with the invasiveness of pituitary adenomas and contributes to invasion by cleaving L1 and CD44...

More Information

Publications71

  1. Möller Hackbarth K, Dewitz C, Schweigert O, Trad A, Garbers C, Rose John S, et al. A disintegrin and metalloprotease (ADAM) 10 and ADAM17 are major sheddases of T cell immunoglobulin and mucin domain 3 (Tim-3). J Biol Chem. 2013;288:34529-44 pubmed publisher
    ..We identified ADAM10 and ADAM17 as major sheddases of Tim-3 as shown by ADAM-specific inhibitors and the ADAM10 pro-domain in HEK293 ..
  2. Gutwein P, Abdel Bakky M, Schramme A, Doberstein K, Kämpfer Kolb N, Amann K, et al. CXCL16 is expressed in podocytes and acts as a scavenger receptor for oxidized low-density lipoprotein. Am J Pathol. 2009;174:2061-72 pubmed publisher
    ..Here we demonstrate that CXCL16 and ADAM10 are constitutively expressed in human podocytes in normal renal tissue...
  3. Kirkin V, Cahuzac N, Guardiola Serrano F, Huault S, Lückerath K, Friedmann E, et al. The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells. Cell Death Differ. 2007;14:1678-87 pubmed
    ..processing of overexpressed and endogenous FasL in T-cells by the disintegrin and metalloprotease ADAM10 generates a 17-kDa N-terminal fragment, which lacks the receptor-binding extracellular domain...
  4. Dittmer A, Hohlfeld K, Lützkendorf J, Müller L, Dittmer J. Human mesenchymal stem cells induce E-cadherin degradation in breast carcinoma spheroids by activating ADAM10. Cell Mol Life Sci. 2009;66:3053-65 pubmed publisher
    ..In addition, hMSCs enhanced the motility of breast cancer cells. Inhibition of ADAM10 (a disintegrin and metalloprotease 10), known to cleave E-cadherin, prevented both hMSC-mediated E-cadherin ..
  5. Marcello E, Saraceno C, Musardo S, Vara H, de la Fuente A, Pelucchi S, et al. Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease. J Clin Invest. 2013;123:2523-38 pubmed publisher
    A disintegrin and metalloproteinase 10 (ADAM10), a disintegrin and metalloproteinase that resides in the postsynaptic densities (PSDs) of excitatory synapses, has previously been shown to limit ?-amyloid peptide (A?) formation in ..
  6. Soundararajan R, Sayat R, Robertson G, Marignani P. Triptolide: An inhibitor of a disintegrin and metalloproteinase 10 (ADAM10) in cancer cells. Cancer Biol Ther. 2009;8:2054-62 pubmed
    ..We identified a disintegrin and metalloproteinase 10 (ADAM10) as a novel molecular target of triptolide using affinity chromatography and mass spectrometry...
  7. Moss M, POWELL G, Miller M, Edwards L, Qi B, Sang Q, et al. ADAM9 inhibition increases membrane activity of ADAM10 and controls ?-secretase processing of amyloid precursor protein. J Biol Chem. 2011;286:40443-51 pubmed publisher
    ..neuroblastoma cells overexpressing amyloid precursor protein, proA9 treatment reduces the amount of endogenous ADAM10 enzyme in the medium while increasing membrane-bound ADAM10, as shown both by Western and activity assays with ..
  8. Donners M, Wolfs I, Olieslagers S, Mohammadi Motahhari Z, Tchaikovski V, Heeneman S, et al. A disintegrin and metalloprotease 10 is a novel mediator of vascular endothelial growth factor-induced endothelial cell function in angiogenesis and is associated with atherosclerosis. Arterioscler Thromb Vasc Biol. 2010;30:2188-95 pubmed publisher
    ..By using a yeast-2-hybrid assay, we identified A Disintegrin And Metalloprotease 10 (ADAM10) as a novel binding partner of VEGFR2...
  9. Schramme A, Abdel Bakky M, Kämpfer Kolb N, Pfeilschifter J, Gutwein P. The role of CXCL16 and its processing metalloproteinases ADAM10 and ADAM17 in the proliferation and migration of human mesangial cells. Biochem Biophys Res Commun. 2008;370:311-6 pubmed publisher
    ..The constitutive release of CXCL16 from hMCs was rapidly induced by the stimulation with cytokines. We identified ADAM10 and ADAM17 as being responsible for the cytokine-induced shedding of CXCL16...
  10. Bozkulak E, Weinmaster G. Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling. Mol Cell Biol. 2009;29:5679-95 pubmed publisher
    ..Although both ADAM10 and ADAM17 have been reported to cleave Notch to facilitate NICD release by gamma-secretase, the relevant ADAM has ..
  11. Bekris L, Lutz F, Li G, Galasko D, Farlow M, Quinn J, et al. ADAM10 expression and promoter haplotype in Alzheimer's disease. Neurobiol Aging. 2012;33:2229.e1-2229.e9 pubmed publisher
    ..Neuritic plaques contain amyloid-? (A?) and lower levels of A? correspond to an increase in ADAM10 ?-secretase activity...
  12. Matthews V, Schuster B, Schütze S, Bussmeyer I, Ludwig A, Hundhausen C, et al. Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE). J Biol Chem. 2003;278:38829-39 pubmed
    ..highly dependent on the metalloproteinase ADAM17 (tumor necrosis factor-alpha-converting enzyme), and the related ADAM10, which is identified here for the first time as an enzyme involved in constitutive and induced shedding of the ..
  13. Sommer A, Fries A, Cornelsen I, Speck N, Koch Nolte F, Gimpl G, et al. Melittin modulates keratinocyte function through P2 receptor-dependent ADAM activation. J Biol Chem. 2012;287:23678-89 pubmed publisher
    ..Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts...
  14. Schulte M, Reiss K, Lettau M, Maretzky T, Ludwig A, Hartmann D, et al. ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death. Cell Death Differ. 2007;14:1040-9 pubmed
    ..function studies in murine embryonic fibroblasts (MEFs), we demonstrate that the disintegrin and metalloprotease ADAM10 is critically involved in the shedding of FasL...
  15. Jian X, Wang K, Wu T, Hillhouse J, Mullersman J. Association of ADAM10 and CAMK2A polymorphisms with conduct disorder: evidence from family-based studies. J Abnorm Child Psychol. 2011;39:773-82 pubmed publisher
    ..20 SNPs had suggestive associations with CD (p<10(-3)), nine of which were located in known genes, including ADAM10 (rs383902, p=0.00036) and CAMK2A (rs2053053, p=0.00098)...
  16. Kohga K, Takehara T, Tatsumi T, Miyagi T, Ishida H, Ohkawa K, et al. Anticancer chemotherapy inhibits MHC class I-related chain a ectodomain shedding by downregulating ADAM10 expression in hepatocellular carcinoma. Cancer Res. 2009;69:8050-7 pubmed publisher
    ..drugs suppress MICA ectodomain shedding by inhibiting expression of a disintegrin and metalloproteinase 10 (ADAM10)...
  17. Colciaghi F, Borroni B, Pastorino L, Marcello E, Zimmermann M, Cattabeni F, et al. [alpha]-Secretase ADAM10 as well as [alpha]APPs is reduced in platelets and CSF of Alzheimer disease patients. Mol Med. 2002;8:67-74 pubmed
    ..One of the candidate alpha-secretases identified in this family is ADAM10. The present study addresses the following major questions: 1) Are the levels of an alpha-secretase candidate (i.e...
  18. Haining E, Yang J, Bailey R, Khan K, Collier R, Tsai S, et al. The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression. J Biol Chem. 2012;287:39753-65 pubmed publisher
    A disintegrin and metalloprotease 10 (ADAM10) is a ubiquitous transmembrane metalloprotease that cleaves the extracellular regions from over 40 different transmembrane target proteins, including Notch and amyloid precursor protein...
  19. Suh J, Choi S, Romano D, Gannon M, Lesinski A, Kim D, et al. ADAM10 missense mutations potentiate ?-amyloid accumulation by impairing prodomain chaperone function. Neuron. 2013;80:385-401 pubmed publisher
    ..We identified two rare mutations (Q170H and R181G) in the prodomain of the metalloprotease, ADAM10, that cosegregate with late-onset AD (LOAD)...
  20. Liu P, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells. Cancer Biol Ther. 2006;5:657-64 pubmed
    ..siRNAs that selectively inhibited ADAM10 expression reduced HER2 shedding...
  21. Schulz B, Pruessmeyer J, Maretzky T, Ludwig A, Blobel C, Saftig P, et al. ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin. Circ Res. 2008;102:1192-201 pubmed publisher
    ..We found that VE-cadherin is specifically cleaved by the disintegrin and metalloprotease ADAM10 in its ectodomain, releasing a soluble fragment and generating a carboxyl-terminal membrane-bound stub, which is a ..
  22. Wada S, Morishima Kawashima M, Qi Y, Misono H, Shimada Y, Ohno Iwashita Y, et al. Gamma-secretase activity is present in rafts but is not cholesterol-dependent. Biochemistry. 2003;42:13977-86 pubmed
    ..The membrane domains purified with BCtheta did indeed produce Abeta. These observations indicate that the gamma-cleavage required for generating Abeta occurs in rafts, but its activity is virtually cholesterol-independent. ..
  23. Hundhausen C, Misztela D, Berkhout T, Broadway N, Saftig P, Reiss K, et al. The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood. 2003;102:1186-95 pubmed
    ..Here we demonstrate a role of the closely related disintegrin-like metalloproteinase 10 (ADAM10) in the constitutive CX3CL1 cleavage...
  24. Janes P, Wimmer Kleikamp S, Frangakis A, Treble K, Griesshaber B, Sabet O, et al. Cytoplasmic relaxation of active Eph controls ephrin shedding by ADAM10. PLoS Biol. 2009;7:e1000215 pubmed publisher
    ..intracellular domain away from the cell membrane into a conformation that facilitates productive association with ADAM10. Accordingly, EphA3 mutants with constitutively-released kinase domains efficiently support shedding, even when ..
  25. Kuhn P, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart J, et al. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J. 2010;29:3020-32 pubmed publisher
    ..Using a novel alpha-secretase-cleavage site-specific antibody, we found that RNAi-mediated knockdown of ADAM10, but surprisingly not of ADAM9 or 17, completely suppressed APP alpha-secretase cleavage in different cell lines ..
  26. Bekris L, Galloway N, Millard S, Lockhart D, Li G, Galasko D, et al. Amyloid precursor protein (APP) processing genes and cerebrospinal fluid APP cleavage product levels in Alzheimer's disease. Neurobiol Aging. 2011;32:556.e13-23 pubmed publisher
    ..n = 170) and AD patients (n = 92) were genotyped for 19 putative regulatory tagging SNPs within 9 genes (APP, ADAM10, BACE1, BACE2, PSEN1, PSEN2, PEN2, NCSTN and APH1B) involved in the APP processing pathway...
  27. Gutwein P, Mechtersheimer S, Riedle S, Stoeck A, Gast D, Joumaa S, et al. ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. FASEB J. 2003;17:292-4 pubmed
    ..How such different compounds can induce shedding is presently unknown. We show here that ADAM10 is involved in L1 cleavage, which occurs at the cell surface and in the Golgi apparatus...
  28. Martin L, Fluhrer R, Reiss K, Kremmer E, Saftig P, Haass C. Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J Biol Chem. 2008;283:1644-52 pubmed
    ..we now describe that the Bri2 protein, similar to gamma-secretase substrates, undergoes an additional cleavage by ADAM10 in its ectodomain...
  29. Yuan S, Lei S, Wu S. ADAM10 is overexpressed in human hepatocellular carcinoma and contributes to the proliferation, invasion and migration of HepG2 cells. Oncol Rep. 2013;30:1715-22 pubmed publisher
    The overexpression of A disintegrin and metalloproteinase 10 (ADAM10) has been found to be closely associated with the development and progression of various types of tumors...
  30. Jones A, Lambert D, Speight P, Whawell S. ADAM 10 is over expressed in oral squamous cell carcinoma and contributes to invasive behaviour through a functional association with ?v?6 integrin. FEBS Lett. 2013;587:3529-34 pubmed publisher
    ..This may result from ADAM 10-induced up-regulation of MMPs. We conclude ADAM 10 may influence OSCC invasion by functionally interacting with ?v?6 integrin which we have previously shown is over expressed in OSCC. ..
  31. Arduise C, Abache T, Li L, Billard M, Chabanon A, Ludwig A, et al. Tetraspanins regulate ADAM10-mediated cleavage of TNF-alpha and epidermal growth factor. J Immunol. 2008;181:7002-13 pubmed
    ..CD9, CD81, CD82) increases epidermal growth factor and/or TNF-alpha secretion through a mechanism dependent on ADAM10. The effect of anti-tetraspanin mAb on TNF-alpha release is rapid, not relayed by intercellular signaling, and ..
  32. Anderegg U, Eichenberg T, Parthaune T, Haiduk C, Saalbach A, Milkova L, et al. ADAM10 is the constitutive functional sheddase of CD44 in human melanoma cells. J Invest Dermatol. 2009;129:1471-82 pubmed publisher
    ..b>ADAM10, ADAM17, and MMP14 have previously been implicated in the shedding of CD44 from various tumor cells...
  33. Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, et al. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci. 2010;30:4833-44 pubmed publisher
    The metalloproteinase and major amyloid precursor protein (APP) alpha-secretase candidate ADAM10 is responsible for the shedding of proteins important for brain development, such as cadherins, ephrins, and Notch receptors...
  34. Blume K, Soeroes S, Keppeler H, Stevanovic S, Kretschmer D, Rautenberg M, et al. Cleavage of annexin A1 by ADAM10 during secondary necrosis generates a monocytic "find-me" signal. J Immunol. 2012;188:135-45 pubmed publisher
    ..annexin A1 during secondary necrosis coincided with proteolytic processing within its unique N-terminal domain by ADAM10. Most importantly, we demonstrate that the released peptide and culture supernatants of secondary necrotic, ..
  35. Powers M, Kim H, Wang Y, Bubeck Wardenburg J. ADAM10 mediates vascular injury induced by Staphylococcus aureus ?-hemolysin. J Infect Dis. 2012;206:352-6 pubmed publisher
    ..The ?-hemolysin binding to its receptor A-disintegrin and metalloprotease 10 (ADAM10) upregulates the receptor's metalloprotease activity on endothelial cells, causing vascular endothelial-cadherin ..
  36. Six E, Ndiaye D, Laabi Y, Brou C, Gupta Rossi N, Israel A, et al. The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase. Proc Natl Acad Sci U S A. 2003;100:7638-43 pubmed
    ..Kuzbanian/ADAM10 is involved in this processing event, but other proteases can probably substitute for it...
  37. Arima T, Enokida H, Kubo H, Kagara I, Matsuda R, Toki K, et al. Nuclear translocation of ADAM-10 contributes to the pathogenesis and progression of human prostate cancer. Cancer Sci. 2007;98:1720-6 pubmed
    ..Our results suggest that in human PC, the nuclear translocation of ADAM-10 coupled with the androgen receptor is involved in tumor growth and progression. ..
  38. Poghosyan Z, Robbins S, Houslay M, Webster A, Murphy G, Edwards D. Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. J Biol Chem. 2002;277:4999-5007 pubmed
    ..These data demonstrate selective, phosphorylation-dependent interactions of ADAM15 with Src family PTKs and Grb2, which highlight the potential for integration of ADAM functions and cellular signaling. ..
  39. Raucci A, Cugusi S, Antonelli A, Barabino S, Monti L, Bierhaus A, et al. A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). FASEB J. 2008;22:3716-27 pubmed publisher
    ..chemical inhibitors and genetically modified mouse embryonic fibroblasts (MEFs), we identify the sheddase ADAM10 as a membrane protease responsible for RAGE cleavage. Binding of its ligand HMGB1 promotes RAGE shedding...
  40. Song J, Yu J, Liu M, Yan C, Tan L. Genetic association between ADAM10 gene polymorphism and Alzheimer's disease in a Northern Han Chinese population. Brain Res. 2011;1421:78-81 pubmed publisher
    The ADAM10 gene encodes a member of a disintegrin and metalloprotease family, which, after overexpression in Alzheimer's disease (AD), prevents amyloid pathology and improves long-term potentiation and memory...
  41. Maretzky T, Reiss K, Ludwig A, Buchholz J, Scholz F, Proksch E, et al. ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation. Proc Natl Acad Sci U S A. 2005;102:9182-7 pubmed
    ..Analysis of ADAM10-deficient fibroblasts, inhibitor studies, and RNA interference-mediated down-regulation of ADAM10 demonstrated ..
  42. Schirrmeister W, Gnad T, Wex T, Higashiyama S, Wolke C, Naumann M, et al. Ectodomain shedding of E-cadherin and c-Met is induced by Helicobacter pylori infection. Exp Cell Res. 2009;315:3500-8 pubmed publisher
    ..Our results show that infection with H. pylori provokes shedding of the surface proteins c-Met and E-cadherin. Evidence is provided that ADAM10 contributes to the shedding of c-Met and E-cadherin.
  43. Kim M, Suh J, Romano D, Truong M, Mullin K, Hooli B, et al. Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity. Hum Mol Genet. 2009;18:3987-96 pubmed publisher
    b>ADAM10, a member of a disintegrin and metalloprotease family, is an alpha-secretase capable of anti-amyloidogenic proteolysis of the amyloid precursor protein...
  44. Heiseke A, Schöbel S, Lichtenthaler S, Vorberg I, Groschup M, Kretzschmar H, et al. The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP shedding. Traffic. 2008;9:1116-29 pubmed publisher
    ..Our data provide new insights into the cellular mechanisms of PrP(c) shedding and show how this can affect cellular PrP(Sc) conversion. ..
  45. Reiss K, Maretzky T, Haas I, Schulte M, Ludwig A, Frank M, et al. Regulated ADAM10-dependent ectodomain shedding of gamma-protocadherin C3 modulates cell-cell adhesion. J Biol Chem. 2006;281:21735-44 pubmed
    ..C3 and Pcdh gamma B4 are specifically cleaved within their ectodomains by the disintegrin and metalloprotease ADAM10. Analysis of ADAM10-deficient fibroblasts and embryos, inhibitor studies, as well as RNA interference-mediated ..
  46. Ko S, Lin S, Wong Y, Liu C, Chang K, Liu T. Increase of disintergin metalloprotease 10 (ADAM10) expression in oral squamous cell carcinoma. Cancer Lett. 2007;245:33-43 pubmed
    ..Recent research shows that ADAM10 alpha-secretase activity can release the secreted form of APP...
  47. Li Y, Liao F, Yin X, Cui L, Ma G, Nong X, et al. An association study on ADAM10 promoter polymorphisms and atherosclerotic cerebral infarction in a Chinese population. CNS Neurosci Ther. 2013;19:785-94 pubmed publisher
    Dysregulation of the activity of the disintegrin/metalloproteinase ADAM10 could contribute to the development of atherosclerosis...
  48. Lee S, Schramme A, Doberstein K, Dummer R, Abdel Bakky M, Keller S, et al. ADAM10 is upregulated in melanoma metastasis compared with primary melanoma. J Invest Dermatol. 2010;130:763-73 pubmed publisher
    b>ADAM10 (a disintegrin and metalloproteinase 10) is involved in the ectodomain shedding of various substrates, including adhesion molecules such as L1 cell adhesion molecule (L1-CAM) and CD44, which are known to have important roles in the ..
  49. Armanious H, Gelebart P, Anand M, Belch A, Lai R. Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNF?/NF?B pathway. Blood. 2011;117:6237-46 pubmed publisher
    One of the main functions of A Disintegrin and Metalloproteinase 10 (ADAM10) is to regulate the bioavailability of adhesion molecules and ligands to various cellular-signaling receptors...
  50. Gavert N, Sheffer M, Raveh S, Spaderna S, Shtutman M, Brabletz T, et al. Expression of L1-CAM and ADAM10 in human colon cancer cells induces metastasis. Cancer Res. 2007;67:7703-12 pubmed
    ..We identified ADAM10, a metalloproteinase that cleaves the L1-CAM extracellular domain, as a novel target gene of beta-catenin-TCF ..
  51. Yavari R, Adida C, Bray Ward P, Brines M, Xu T. Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. Hum Mol Genet. 1998;7:1161-7 pubmed
    ..The Drosophila kuzbanian (kuz) gene is required in neurogenesis and encodes a highly conserved, membrane-bound metalloprotease- disintegrin ..
  52. Guo J, He L, Yuan P, Wang P, Lu Y, Tong F, et al. ADAM10 overexpression in human non-small cell lung cancer correlates with cell migration and invasion through the activation of the Notch1 signaling pathway. Oncol Rep. 2012;28:1709-18 pubmed publisher
    A disintegrin and metalloproteinase 10 (ADAM10) was identified as a key protease in the ectodomain shedding of various substrates, such as Notch1 protein, ErbB2 and E-cadherin, which are important in the development of non-small cell lung ..
  53. Tanaka M, Nanba D, Mori S, Shiba F, Ishiguro H, Yoshino K, et al. ADAM binding protein Eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands. J Biol Chem. 2004;279:41950-9 pubmed
  54. Kohutek Z, diPierro C, Redpath G, Hussaini I. ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration. J Neurosci. 2009;29:4605-15 pubmed publisher
    ..Together, these results suggest that N-cadherin cleavage is regulated by a PKC-alpha-ADAM-10 cascade in GBM cells and may be involved in mediating GBM cell migration. ..
  55. Sanderson M, Erickson S, Gough P, Garton K, Wille P, Raines E, et al. ADAM10 mediates ectodomain shedding of the betacellulin precursor activated by p-aminophenylmercuric acetate and extracellular calcium influx. J Biol Chem. 2005;280:1826-37 pubmed
    ..In contrast, overexpression of WT ADAM10 enhanced constitutive and activated shedding of pro-BTC, whereas overexpression of catalytically inactive ADAM10 ..
  56. Hattori M, Osterfield M, Flanagan J. Regulated cleavage of a contact-mediated axon repellent. Science. 2000;289:1360-5 pubmed
    ..These studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling. ..
  57. Solanas G, Cortina C, Sevillano M, Batlle E. Cleavage of E-cadherin by ADAM10 mediates epithelial cell sorting downstream of EphB signalling. Nat Cell Biol. 2011;13:1100-7 pubmed publisher
    ..EphB receptors interact with E-cadherin and with the metalloproteinase ADAM10 at sites of adhesion and their activation induces shedding of E-cadherin by ADAM10 at interfaces with ephrin-B1-..
  58. Malinverno M, Carta M, Epis R, Marcello E, Verpelli C, Cattabeni F, et al. Synaptic localization and activity of ADAM10 regulate excitatory synapses through N-cadherin cleavage. J Neurosci. 2010;30:16343-55 pubmed publisher
    ..Recent studies have shown that N-cadherin can be cleaved by the metalloproteinase ADAM10. Here we demonstrate that impairing ADAM10 localization and activity at synaptic sites decreases its processing of ..
  59. Guo S, Peng M, Zhao Q, Zhang W. Role of ADAM10 and ADAM17 in CD16b shedding mediated by different stimulators. Chin Med Sci J. 2012;27:73-9 pubmed
    ..The cell line was then overexpressed with a disintegrin and metalloproteinase 10 (ADAM10) or ADAM17, suppressed with short hairpin RNA of ADAM10 or ADAM17, and reconstituted with ADAM10 or ADAM17, ..
  60. Manilay J, Anderson A, Kang C, Robey E. Impairment of thymocyte development by dominant-negative Kuzbanian (ADAM-10) is rescued by the Notch ligand, delta-1. J Immunol. 2005;174:6732-41 pubmed
    ..Our data suggest that multiple Notch-dependent steps in early thymocyte development require Kuzbanian, but differ in the involvement of other Notch signaling components. ..
  61. Schramme A, Abdel Bakky M, Gutwein P, Obermüller N, Baer P, Hauser I, et al. Characterization of CXCL16 and ADAM10 in the normal and transplanted kidney. Kidney Int. 2008;74:328-38 pubmed publisher
    ..In human renal tissue the expression pattern of the disintegrin-like metalloproteinase ADAM10 is similar to that of CXCL16, suggesting ADAM10 can potentially cleave CXCL16 in vivo...
  62. Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem. 2001;276:37743-6 pubmed
    ..a general zinc-metalloprotease inhibitors, as well as BB3103 and TAPI, the inhibitors of metalloenzymes ADAM10 (A disintegrin and metalloprotease); and TACE, tumor necrosis factor alpha-converting enzyme; ADAM17), ..