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ADAM-like, decysin 1

ADAMDEC1, ADAM-like decysin-1, disintegrin protease
This encoded protein is thought to be a secreted protein belonging to the disintegrin metalloproteinase family. Its expression is upregulated during dendritic cells maturation. This protein may play an important role in dendritic cell function and their interactions with germinal center T cells. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, metalloprotease, ADAM23, TOP, Barr
Papers on ADAMDEC1
EBNA3C Directs Recruitment of RBPJ (CBF1) to Chromatin during the Process of Gene Repression in EBV Infected B Cells.
Allday et al., London, United Kingdom. In Plos Pathog, Jan 2016
COBLL1, a gene of unknown function, is regulated by EBNA3C alone and the two co-regulated disintegrin/metalloproteases, ADAM28 and ADAMDEC1 have been described previously as targets of both EBNA3A and EBNA3C.
Evidence for restricted reactivity of ADAMDEC1 with protein substrates and endogenous inhibitors.
Overgaard et al., Aalborg, Denmark. In J Biol Chem, Apr 2015
ADAMDEC1 is a proteolytically active metzincin metalloprotease displaying rare active site architecture with a zinc-binding Asp residue (Asp-362).
Transcriptome comparisons identify new cell markers for theca interna and granulosa cells from small and large antral ovarian follicles.
Rodgers et al., Adelaide, Australia. In Plos One, 2014
Many genes up regulated in theca interna were common to both sizes of follicles (MGP, DCN, ASPN, ALDH1A1, COL1A2, FN1, COL3A1, OGN, APOD, COL5A2, IGF2, NID1, LHFP, ACTA2, DUSP12, ACTG2, SPARCL1, FILIP1L, EGFLAM, ADAMDEC1, HPGD, COL12A1, FBLN5, RAMP2, COL15A1, PLK2, COL6A3, LOXL1, RARRES1, FLI1, LAMA2).
Molecular landscape of T cell-mediated rejection in human kidney transplants: prominence of CTLA4 and PD ligands.
Halloran et al., Edmonton, Canada. In Am J Transplant, 2014
PDL1, CD86, SLAMF8, ADAMDEC1), B cells (e.g.
A gene expression profile related to immune dampening in the tumor microenvironment is associated with poor prognosis in gastric adenocarcinoma.
Federico et al., São Paulo, Brazil. In J Gastroenterol, 2014
A gene trio (OLR1, CXCL11 and ADAMDEC1) was identified as an independent marker of prognosis, being the last two markers validated in an independent patient cohort.
Infliximab restores the dysfunctional matrix remodeling protein and growth factor gene expression in patients with inflammatory bowel disease.
Arijs et al., Leuven, Belgium. In Inflamm Bowel Dis, 2014
RESULTS: In patients with active IBD before infliximab versus controls, gene expression of many MMPs, TIMPs, ADAM(TS)s, and growth factors was upregulated, whereas colonic expression of MMP28 and TGFA and ileal expression of ADAMDEC1 and AGT were downregulated.
Proteomic analysis of human osteoarthritis synovial fluid.
Pandey et al., Pune, India. In Clin Proteomics, 2013
These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2).
Modulation of enhancer looping and differential gene targeting by Epstein-Barr virus transcription factors directs cellular reprogramming.
West et al., Brighton, United Kingdom. In Plos Pathog, 2013
At an EBNA 3-only intergenic enhancer site between ADAM28 and ADAMDEC1 EBNA 3C was also able to independently direct epigenetic repression of both genes through enhancer-promoter looping.
ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity.
Overgaard et al., Aalborg, Denmark. In J Biol Chem, 2013
ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metalloprotease with an unknown physiological role, selectively expressed in mature dendritic cells and macrophages.
Early dynamic transcriptomic changes during preoperative radiotherapy in patients with rectal cancer: a feasibility study.
Chérel et al., Saint-Herblain, France. In World J Gastroenterol, 2013
According to the Gene Ontology project classification, these genes are involved in protein metabolism (ADAMDEC1; AKAP7; CAPN5; CLIC5; CPE; CREB3L1; NEDD4L; RAB27A), ion transport (AKAP7; ATP2A3; CCL28; CLIC5; F2RL2; NEDD4L; SLC6A8), transcription (AKAP7; CREB3L1; ISX; PABPC1L; TXNIP), signal transduction (CAPN5; F2RL2; RAB27A; TNFRSF11A), cell adhesion (ADAMDEC1; PXDN; SPON1; S100A2), immune response (CCL28; PXDN; TNFRSF11A) and apoptosis (ITM2C; PDCD4; PVT1).
Gene biomarkers in peripheral white blood cells of horses with experimentally induced osteoarthritis.
Orr et al., Fort Collins, United States. In Am J Vet Res, 2013
RESULTS: A metalloproteinase domain-like protein decysin-1 (ADAMDEC1), glucose-regulated protein (GRP) 94, hematopoietic cell signal transducer (HCST), Unc-93 homolog A (hUNC-93A), and ribonucleotide reductase M2 polypeptide (RRM2) were significantly differentially regulated in WBCs of horses with osteoarthritis, compared with values prior to induction of osteoarthritis.
Expression and inhibition of ADAMDEC1 in craniopharyngioma cells.
Li et al., Chengdu, China. In Neurol Res, 2012
The ADAM-like decysin 1 (ADAMDEC1) is a member of a disintegrin and metalloprotease (ADAM) family which correlates with tumor progression and aggressive behavior.
Downregulation of integrin receptor-signaling genes by Epstein-Barr virus EBNA 3C via promoter-proximal and -distal binding elements.
West et al., Brighton, United Kingdom. In J Virol, 2012
We performed transcription profiling on EBNA 3C-expressing B cells and identified several chemokines and members of integrin receptor-signaling pathways, including CCL3, CCL4, CXCL10, CXCL11, ITGA4, ITGB1, ADAM28, and ADAMDEC1, as cellular target genes that could be repressed by the action of EBNA 3C alone.
Gene expression profiling identifies MMP-12 and ADAMDEC1 as potential pathogenic mediators of pulmonary sarcoidosis.
Eng et al., Columbus, United States. In Am J Respir Crit Care Med, 2009
Gene expression profiling performed on tissues obtained from pulmonary sarcoidosis patients identified ADAMDEC1 as a potential pathogenic mediator of lung damage and/or remodeling and may serve as a marker for this disease.
The role of the disintegrin metalloproteinase ADAM15 in prostate cancer progression.
Day et al., Ann Arbor, United States. In J Cell Biochem, 2009
The metalloproteinase ADAM15 is a multi-domain disintegrin protease that is upregulated in a variety of human cancers.
The therapeutic potential of ADAM15.
Day et al., Ann Arbor, United States. In Curr Pharm Des, 2008
Taken together, this multi-functional disintegrin protease not only offers a variety of potential targets for therapeutic intervention, but also represents an attractive target for pharmaceutical consideration due to its involvement in key cellular processes and various disease states.
Association of ADAMDEC1 haplotype with high factor VIII levels in venous thromboembolism.
Schambeck et al., Würzburg, Germany. In Thromb Haemost, 2008
The ADAMDEC 1 haplotype may indicate an underlying mechanism for high FVIII levels in venous thromboembolism.
The ADAMDEC1 (decysin) gene structure: evolution by duplication in a metalloprotease gene cluster on chromosome 8p12.
Mueller et al., France. In Immunogenetics, 2002
molecular evolution by duplication in a metalloprotease gene cluster on chromosome 8p12
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