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ADAM metallopeptidase domain 15

The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: metalloprotease, V1a, ADAM9, CAN, ADAM10
Papers on ADAM15
ADAM15 targets MMP9 activity to promote lung cancer cell invasion.
Li et al., Chengdu, China. In Oncol Rep, Nov 2015
ADAM15 is a membrane-associated proteinase belonging to a disintegrin and metalloproteinase (ADAM) family.
Antitumor and anti-angiogenic activity of the recombinant human disintegrin domain of A disintegrin and metalloproteinase 15.
Jin et al., Wuxi, China. In Mol Med Report, Aug 2015
ADAM15 is unique among the ADAMs in having an Arg-Gly-Asp motif in its disintegrin domain.
Blood Vessel Maturation by Disintegrin in Oxygen-Induced Retinopathy.
Kim et al., Seoul, South Korea. In Curr Eye Res, Aug 2015
MATERIALS AND METHODS: EGT022, an RGD-containing disintegrin originated from human a disintegrin and metalloproteinase 15 (ADAM15), was used to investigate the role of the disintegrin in vascular development in OIR mouse model.
Integration of disease association and eQTL data using a Bayesian colocalisation approach highlights six candidate causal genes in immune-mediated diseases.
Wallace et al., Cambridge, United Kingdom. In Hum Mol Genet, Jul 2015
Previously published candidate causal genes were over-represented amongst genes exhibiting colocalisation (odds ratio > 1.5), and we identified evidence for colocalisation (posterior odds > 5) between cis eQTLs in at least one cell type and at least one disease for six genes: ADAM15, RGS1, CARD9, LTBR, CTSH and SYNGR1.
A disintegrin and metallproteinase 15 knockout decreases migration of fibroblast-like synoviocytes and inflammation in rheumatoid arthritis.
Song et al., Changchun, China. In Mol Med Report, Jun 2015
The aim of the present study was to determine whether the expression of A disintegrin and metallproteinase 15 (ADAM15) affected the inflammatory conditions and cell migration in human fibroblast‑like synoviocytes (FLSs) in a rat model of rheumatoid arthritis (RA).
In-silico identification and functional validation of allele-dependent AR enhancers.
Demichelis et al., Trento, Italy. In Oncotarget, Apr 2015
We observed allele-specific enhancer activity, responsiveness to ligand-bound AR, and potentially influence on the transcription of closely located genes (RAB20, ING1, ARHGEF7, ADAM15).
Molecular genetic study of novel biomarkers for early diagnosis of oral squamous cell carcinoma.
Jong-Ho et al., Seoul, South Korea. In Med Oral Patol Oral Cir Bucal, Mar 2015
A genetic analysis of functional networks and ontologies, validated by using a qRT-PCR analysis of the tissue samples, identified four genes, ADAM15, CDC7, IL12RB2 and TNFRSF8, that demonstrated excellent concordance with the microarray data.
ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets.
Ludwig et al., Aachen, Germany. In Am J Physiol Lung Cell Mol Physiol, Mar 2015
ADAM8, ADAM9, ADAM15, and ADAM33 are upregulated during acute or chronic lung inflammation, and recent functional or genetic analyses have linked them to disease development.
ADAM15 participates in fertilization through a physical interaction with acrogranin.
Hernández-González et al., San Luis Potosí, Mexico. In Reproduction, 2014
In this study, we demonstrate the proteolytic processing of ADAM15 during epididymal maturation of guinea pig spermatozoa to produce a mature form a size of 45 kDa.
MicroRNA-147b regulates vascular endothelial barrier function by targeting ADAM15 expression.
Yuan et al., Sacramento, United States. In Plos One, 2013
A disintegrin and metalloproteinase15 (ADAM15) has been shown to be upregulated and mediate endothelial hyperpermeability during inflammation and sepsis.
ADAM22 as a prognostic and therapeutic drug target in the treatment of endocrine-resistant breast cancer.
Young et al., Dublin, Ireland. In Vitam Horm, 2012
A number of ADAM proteins have been implicated in the occurrence of breast cancer, including ADAM 9, ADAM12, ADAM15, ADAM17, ADAM22, and ADAM28.
Exosome release of ADAM15 and the functional implications of human macrophage-derived ADAM15 exosomes.
Kim et al., Seoul, South Korea. In Faseb J, 2012
Exosomes rich in ADAM15 display enhanced binding affinity for integrin alphavbeta3 in an RGD-dependent manner and suppress vitronectin- and fibronectin-induced cell adhesion, growth, and migration, as well as in vivo tumor growth.
ADAM15 protein amplifies focal adhesion kinase phosphorylation under genotoxic stress conditions.
Burkhardt et al., Frankfurt am Main, Germany. In J Biol Chem, 2012
ADAM15 tail can transduce a percepted extracellular signal to enhance FAK and Src phosphorylation.
Role of ADAM-15 in wound healing and melanoma development.
Zigrino et al., Köln, Germany. In Exp Dermatol, 2012
dispensable for cutaneous wound healing and B16F1 melanoma growth, but significantly contributes to metastasis formation
Differential expression of ADAM15 and ADAM17 metalloproteases in the rat brain after severe hypobaric hypoxia and hypoxic preconditioning.
Samoilov et al., Saint Petersburg, Russia. In Neurosci Res, 2012
The present findings implicate ADAM15 in the processes of neuronal hypoxic injury
Lack of ADAM15 in mice is associated with increased osteoblast function and bone mass.
Chiusaroli et al., Boston, United States. In Biol Chem, 2011
Adult Adam15(-/-) mice displayed an increase in bone volume and thickness with an increase in the number and activity of osteoblasts, whereas osteoclasts were apparently unaffected.
ADAM-15 disintegrin-like domain structure and function.
Lu et al., London, United Kingdom. In Toxins (basel), 2010
Human ADAM-15 is the only member of the ADAM family with the integrin binding motif Arg-Gly-Asp (RGD) in its disintegrin-like domain.
The role of ADAMs in disease pathophysiology.
McGowan et al., Dublin, Ireland. In Clin Chim Acta, 2009
Multiple ADAMs, including ADAM-9, ADAM-10, ADAM-12, ADAM-15 and ADAM-17, have been shown to play a role in either cancer formation or progression.
The therapeutic potential of ADAM15.
Day et al., Ann Arbor, United States. In Curr Pharm Des, 2008
ADAM15 is a widely expressed multi-domain protease that has been implicated in the pathogenesis of many human diseases.
ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23.
Blobel et al., New York City, United States. In Nat Immunol, 2006
Here we used loss-of-function and gain-of-function experiments with cells lacking or overexpressing candidate CD23-releasing enzymes (ADAM8, ADAM9, ADAM10, ADAM12, ADAM15, ADAM17, ADAM19 and ADAM33), ADAM-knockout mice and a selective inhibitor to identify ADAM10 as the main CD23-releasing enzyme in vivo.
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