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CD47 molecule
Identifiers
Symbols CD47; IAP; MER6; OA3
External IDs OMIM601028 MGI96617 HomoloGene1346 GeneCards: CD47 Gene
RNA expression pattern
PBB GE CD47 213857 s at tn.png
PBB GE CD47 211075 s at tn.png
PBB GE CD47 213055 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 961 16423
Ensembl ENSG00000196776 ENSMUSG00000055447
UniProt Q08722 Q3U967
RefSeq (mRNA) NM_001025079 NM_010581
RefSeq (protein) NP_001020250 NP_034711
Location (UCSC) Chr 3:
109.24 - 109.29 Mb
Chr 16:
49.78 - 49.83 Mb
PubMed search [1] [2]

CD47 (Cluster of Differentiation 47) is a protein that in humans is encoded by the CD47 gene.[1]

Contents

Function

CD47 is a membrane protein, which is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The protein is also a receptor for the C-terminal cell binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This protein has broad tissue distribution, and is reduced in expression on Rh erythrocytes.

Four alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[1] Isoform 2 and 4 are the most abundant. Other than thrombospondin, CD47 also binds CD172a. CD47 deficient mice have been generated. Their reported phenotype is a defect in cellular migration of the CD172a expressing cells, suggesting that CD47 to CD172a interactions are necessary for the proper distribution of these cell types.

Interactions

CD47 has been shown to interact with BNIP3.[2]

Clinical significance

CD47 is used by bladder cancer cells to hide from normal scavenging by macrophages.[3]

See also

References

  1. ^ a b "Entrez Gene: CD47 CD47 molecule". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=961.  
  2. ^ Lamy, Laurence; Ticchioni Michel, Rouquette-Jazdanian Alexandre K, Samson Michel, Deckert Marcel, Greenberg Arnold H, Bernard Alain (Jun. 2003). "CD47 and the 19 kDa interacting protein-3 (BNIP3) in T cell apoptosis". J. Biol. Chem. (United States) 278 (26): 23915–21. doi:10.1074/jbc.M301869200. ISSN 0021-9258. PMID 12690108.  
  3. ^ Chan KS, Espinosa I, Chao M, Wong D, Ailles L, Diehn M, Gill H, Presti J, Chang HY, van de Rijn M, Shortliffe L, Weissman IL (August 2009). "Identification, molecular characterization, clinical prognosis, and therapeutic targeting of human bladder tumor-initiating cells". Proc. Natl. Acad. Sci. U.S.A. 106 (33): 14016–21. doi:10.1073/pnas.0906549106. PMID 19666525. Lay summary – Reuters.  

Further reading

  • Brown EJ, Frazier WA (2001). "Integrin-associated protein (CD47) and its ligands.". Trends Cell Biol. 11 (3): 130–5. doi:10.1016/S0962-8924(00)01906-1. PMID 11306274.  
  • Oldenborg PA (2004). "Role of CD47 in erythroid cells and in autoimmunity.". Leuk. Lymphoma 45 (7): 1319–27. doi:10.1080/1042819042000201989. PMID 15359629.  
  • Kaczorowski DJ, Billiar TR (2007). "Targeting CD47: NO limit on therapeutic potential.". Circ. Res. 100 (5): 602–3. doi:10.1161/01.RES.0000261609.44977.25. PMID 17363705.  
  • Campbell IG, Freemont PS, Foulkes W, Trowsdale J (1992). "An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains.". Cancer Res. 52 (19): 5416–20. PMID 1394148.  
  • Brown E, Hooper L, Ho T, Gresham H (1991). "Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins.". J. Cell Biol. 111 (6 Pt 1): 2785–94. doi:10.1083/jcb.111.6.2785. PMID 2277087.  
  • Lindberg FP, Gresham HD, Schwarz E, Brown EJ (1993). "Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in alpha v beta 3-dependent ligand binding.". J. Cell Biol. 123 (2): 485–96. doi:10.1083/jcb.123.2.485. PMID 7691831.  
  • Mawby WJ, Holmes CH, Anstee DJ, et al. (1995). "Isolation and characterization of CD47 glycoprotein: a multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3.". Biochem. J. 304 ( Pt 2): 525–30. PMID 7998989.  
  • Lindberg FP, Lublin DM, Telen MJ, et al. (1994). "Rh-related antigen CD47 is the signal-transducer integrin-associated protein.". J. Biol. Chem. 269 (3): 1567–70. PMID 8294396.  
  • Gao AG, Lindberg FP, Finn MB, et al. (1996). "Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin.". J. Biol. Chem. 271 (1): 21–4. doi:10.1074/jbc.271.1.21. PMID 8550562.  
  • Cherif-Zahar B, Raynal V, Gane P, et al. (1996). "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency.". Nat. Genet. 12 (2): 168–73. doi:10.1038/ng0296-168. PMID 8563755.  
  • Chung J, Gao AG, Frazier WA (1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3.". J. Biol. Chem. 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. PMID 9169439.  
  • Jiang P, Lagenaur CF, Narayanan V (1999). "Integrin-associated protein is a ligand for the P84 neural adhesion molecule.". J. Biol. Chem. 274 (2): 559–62. doi:10.1074/jbc.274.2.559. PMID 9872987.  
  • Hermann P, Armant M, Brown E, et al. (1999). "The vitronectin receptor and its associated CD47 molecule mediates proinflammatory cytokine synthesis in human monocytes by interaction with soluble CD23.". J. Cell Biol. 144 (4): 767–75. doi:10.1083/jcb.144.4.767. PMID 10037797.  
  • Chung J, Wang XQ, Lindberg FP, Frazier WA (1999). "Thrombospondin-1 acts via IAP/CD47 to synergize with collagen in alpha2beta1-mediated platelet activation.". Blood 94 (2): 642–8. PMID 10397731.  
  • Longhurst CM, White MM, Wilkinson DA, Jennings LK (1999). "A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states.". Eur. J. Biochem. 263 (1): 104–11. doi:10.1046/j.1432-1327.1999.00467.x. PMID 10429193.  
  • Mateo V, Lagneaux L, Bron D, et al. (1999). "CD47 ligation induces caspase-independent cell death in chronic lymphocytic leukemia.". Nat. Med. 5 (11): 1277–84. doi:10.1038/15233. PMID 10545994.  
  • Wu AL, Wang J, Zheleznyak A, Brown EJ (1999). "Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane.". Mol. Cell 4 (4): 619–25. doi:10.1016/S1097-2765(00)80212-9. PMID 10549293.  
  • Erb L, Liu J, Ockerhausen J, et al. (2001). "An RGD sequence in the P2Y(2) receptor interacts with alpha(V)beta(3) integrins and is required for G(o)-mediated signal transduction.". J. Cell Biol. 153 (3): 491–501. doi:10.1083/jcb.153.3.491. PMID 11331301.  
  • Rebres RA, Vaz LE, Green JM, Brown EJ (2001). "Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains.". J. Biol. Chem. 276 (37): 34607–16. doi:10.1074/jbc.M106107200. PMID 11454874.  

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