ADAM23

ADAM metallopeptidase domain 23
Identifiers
Symbols ADAM23 ; MDC-3; MDC3
External IDs OMIM: 603710 MGI: 1345162 HomoloGene: 2826 GeneCards: ADAM23 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 8745 23792
Ensembl ENSG00000114948 ENSMUSG00000025964
UniProt O75077 Q9R1V7
RefSeq (mRNA) NM_003812 NM_001177600
RefSeq (protein) NP_003803 NP_001171071
Location (UCSC) Chr 2:
206.44 – 206.62 Mb		 Chr 1:
63.45 – 63.6 Mb
PubMed search

Disintegrin and metalloproteinase domain-containing protein 23 is an enzyme that in humans is encoded by the ADAM23 gene.[1][2]

Function

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene is highly expressed in the brain and may function as an integrin ligand in the brain.[2]

References

  1. ↑ Sagane K, Ohya Y, Hasegawa Y, Tanaka I (Aug 1998). "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain". The Biochemical Journal. 334 ( Pt 1) (Pt 1): 93–8. PMC 1219666. PMID 9693107.
  2. 1 2 "Entrez Gene: ADAM23 ADAM metallopeptidase domain 23".

Further reading

  • Roberts CM, Tani PH, Bridges LC, Laszik Z, Bowditch RD (Oct 1999). "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes". The Journal of Biological Chemistry 274 (41): 29251–9. doi:10.1074/jbc.274.41.29251. PMID 10506182. 
  • Poindexter K, Nelson N, DuBose RF, Black RA, Cerretti DP (Sep 1999). "The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries". Gene 237 (1): 61–70. doi:10.1016/S0378-1119(99)00302-9. PMID 10524237. 
  • Cal S, Freije JM, López JM, Takada Y, López-Otín C (Apr 2000). "ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism". Molecular Biology of the Cell 11 (4): 1457–69. doi:10.1091/mbc.11.4.1457. PMC 14859. PMID 10749942. 
  • Sun YP, Deng KJ, Wang F, Zhang J, Huang X, Qiao S, Zhao S (Jan 2004). "Two novel isoforms of Adam23 expressed in the developmental process of mouse and human brains". Gene 325: 171–8. doi:10.1016/j.gene.2003.10.012. PMID 14697522. 
  • Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA (Jun 2004). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nature Biotechnology 22 (6): 724–31. doi:10.1038/nbt969. PMID 15146195. 
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
  • Costa FF, Colin C, Shinjo SM, Zanata SM, Marie SK, Sogayar MC, Camargo AA (Jun 2005). "ADAM23 methylation and expression analysis in brain tumors". Neuroscience Letters 380 (3): 260–4. doi:10.1016/j.neulet.2005.01.050. PMID 15862898. 
  • Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (Aug 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384. 
  • Takada H, Imoto I, Tsuda H, Nakanishi Y, Ichikura T, Mochizuki H, Mitsufuji S, Hosoda F, Hirohashi S, Ohki M, Inazawa J (Dec 2005). "ADAM23, a possible tumor suppressor gene, is frequently silenced in gastric cancers by homozygous deletion or aberrant promoter hypermethylation". Oncogene 24 (54): 8051–60. doi:10.1038/sj.onc.1208952. PMID 16103878. 

External links

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