- 同
- B-cell adhesion molecule, Lutheran blood group
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/05/01 12:51:44」(JST)
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Basal cell adhesion molecule (Lutheran blood group) |
Rendering based on PDB 2PET.
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
2PET, 2PF6
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Identifiers |
Symbols |
BCAM ; AU; CD239; LU; MSK19 |
External IDs |
OMIM: 612773 MGI: 1929940 HomoloGene: 21149 GeneCards: BCAM Gene |
Gene ontology |
Molecular function |
• transmembrane signaling receptor activity
• laminin receptor activity
• protein binding
• protein C-terminus binding
• laminin binding
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Cellular component |
• plasma membrane
• integral component of plasma membrane
• external side of plasma membrane
• extracellular exosome
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Biological process |
• cell adhesion
• cell-matrix adhesion
• signal transduction
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
4059 |
57278 |
Ensembl |
ENSG00000187244 |
ENSMUSG00000002980 |
UniProt |
P50895 |
Q9R069 |
RefSeq (mRNA) |
NM_001013257 |
NM_020486 |
RefSeq (protein) |
NP_001013275 |
NP_065232 |
Location (UCSC) |
Chr 19:
44.81 – 44.82 Mb |
Chr 7:
19.76 – 19.77 Mb |
PubMed search |
[1] |
[2] |
|
Basal cell adhesion molecule is a protein that in humans is encoded by the BCAM gene.[1] BCAM has also recently been designated CD239 (cluster of differentiation 239).
Contents
- 1 Function
- 2 Interactions
- 3 References
- 4 Further reading
- 5 External links
Function
Lutheran blood group glycoprotein is a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five, N-terminus, extracellular immunoglobulin domains, a single transmembrane domain, and a short, C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Two transcript variants encoding different isoforms have been found for this gene.[1]
Interactions
BCAM has been shown to interact with Laminin, alpha 5.[2][3]
References
- ^ a b "Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)".
- ^ Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA (2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity". Blood 97 (1): 312–20. doi:10.1182/blood.v97.1.312. PMID 11133776.
- ^ Kikkawa Y, Moulson CL, Virtanen I, Miner JH (2002). "Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo". J. Biol. Chem. 277 (47): 44864–9. doi:10.1074/jbc.M208731200. PMID 12244066.
Further reading
- Eyler CE, Telen MJ (2006). "The Lutheran glycoprotein: a multifunctional adhesion receptor.". Transfusion 46 (4): 668–77. doi:10.1111/j.1537-2995.2006.00779.x. PMID 16584446.
- Lewis M, Kaita H, Coghlan G; et al. (1989). "The chromosome 19 linkage group LDLR, C3, LW, APOC2, LU, SE in man.". Ann. Hum. Genet. 52 (Pt 2): 137–44. doi:10.1111/j.1469-1809.1988.tb01089.x. PMID 2907851.
- Parsons SF, Mallinson G, Holmes CH; et al. (1995). "The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver.". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5496–500. doi:10.1073/pnas.92.12.5496. PMC 41722. PMID 7777537.
- Campbell IG, Foulkes WD, Senger G; et al. (1994). "Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily.". Cancer Res. 54 (22): 5761–5. PMID 7954395.
- Rahuel C, Le Van Kim C, Mattei MG; et al. (1996). "A unique gene encodes spliceoforms of the B-cell adhesion molecule cell surface glycoprotein of epithelial cancer and of the Lutheran blood group glycoprotein.". Blood 88 (5): 1865–72. PMID 8781446.
- Parsons SF, Mallinson G, Daniels GL; et al. (1997). "Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms.". Blood 89 (11): 4219–25. PMID 9166867.
- El Nemer W, Rahuel C, Colin Y; et al. (1997). "Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b) blood group polymorphism.". Blood 89 (12): 4608–16. PMID 9192786.
- Parsons SF, Lee G, Spring FA; et al. (2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity.". Blood 97 (1): 312–20. doi:10.1182/blood.V97.1.312. PMID 11133776.
- El Nemer W, Gane P, Colin Y; et al. (2001). "Characterization of the laminin binding domains of the Lutheran blood group glycoprotein.". J. Biol. Chem. 276 (26): 23757–62. doi:10.1074/jbc.M102978200. PMID 11319237.
- Kikkawa Y, Moulson CL, Virtanen I, Miner JH (2003). "Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo.". J. Biol. Chem. 277 (47): 44864–9. doi:10.1074/jbc.M208731200. PMID 12244066.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Shin BK, Wang H, Yim AM; et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function.". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
- Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519.
- Crew VK, Green C, Daniels G (2004). "Molecular bases of the antigens of the Lutheran blood group system.". Transfusion 43 (12): 1729–37. doi:10.1111/j.0041-1132.2003.00600.x. PMID 14641871.
- Zen Q, Batchvarova M, Twyman CA; et al. (2004). "B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease.". Am. J. Hematol. 75 (2): 63–72. doi:10.1002/ajh.10442. PMID 14755370.
- Kroviarski Y, El Nemer W, Gane P; et al. (2004). "Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin.". Br. J. Haematol. 126 (2): 255–64. doi:10.1111/j.1365-2141.2004.05010.x. PMID 15238148.
- Drewniok C, Wienrich BG, Schön M; et al. (2005). "Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer.". Arch. Dermatol. Res. 296 (2): 59–66. doi:10.1007/s00403-004-0481-4. PMID 15278364.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Cheng J, Kapranov P, Drenkow J; et al. (2005). "Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution.". Science 308 (5725): 1149–54. doi:10.1126/science.1108625. PMID 15790807.
- Vainionpää N, Kikkawa Y, Lounatmaa K; et al. (2006). "Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells.". Am. J. Physiol., Cell Physiol. 290 (3): C764–75. doi:10.1152/ajpcell.00285.2005. PMID 16236823.
External links
- BCAM protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
English Journal
- [Molecular basis of red blood cell adhesion to endothelium].
- Wautier JL, Wautier MP.SourceUniversité Paris Diderot Paris-7, 75013 Paris, France. jlwautier@ints.fr
- Annales pharmaceutiques françaises.Ann Pharm Fr.2011 Jan;69(1):3-6. doi: 10.1016/j.pharma.2010.10.003. Epub 2010 Dec 3.
- The extent of red blood cell adhesion is correlated with the incidence of vascular complications and the severity of the disease. Patients with sickle cell anemia (HbSS) experience vasoocclusive episodes. The adhesion of RBCs from HbSS patients is increased and related to VLA-4 exposure, which binds
- PMID 21296212
- The cell surface proteome of human mesenchymal stromal cells.
- Niehage C, Steenblock C, Pursche T, Bornhäuser M, Corbeil D, Hoflack B.SourceBiotechnology Center, Dresden University of Technology, Dresden, Germany.
- PloS one.PLoS One.2011;6(5):e20399. doi: 10.1371/journal.pone.0020399. Epub 2011 May 26.
- BACKGROUND: Multipotent human mesenchymal stromal cells (hMSCs) are considered as promising biological tools for regenerative medicine. Their antibody-based isolation relies on the identification of reliable cell surface markers.METHODOLOGY/PRINCIPAL FINDINGS: To obtain a comprehensive view of the c
- PMID 21637820
- Expression of adhesion factor CD239 in bone marrow cells in chronic myeloproliferative diseases.
- Hussein K, Theophile K, Denzer K, Kreipe H, Bock O.SourceInstitute of Pathology, Hannover Medical School, Carl-Neuberg-Strasse 1, Hannover, Germany. Hussein.Kais@MH-Hannover.de
- Journal of thrombosis and thrombolysis.J Thromb Thrombolysis.2009 Oct;28(3):299-303. doi: 10.1007/s11239-008-0285-z. Epub 2008 Oct 30.
- Patients suffering from Philadelphia chromosome-negative chronic myeloproliferative disease (Ph(-) CMPD), such as polycythaemia vera (PV), are frequently JAK2(V617F)-mutated and have an elevated risk for thromboembolic complications. Recent data indicated that the molecular basis of JAK2(V617F) and
- PMID 18972067
Related Links
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- This consultative document seeks views on the Health and Safety Executive’s proposals to remove fourteen legislative measures (one Act, twelve Regulations and one Order and with a related provision in the Factories Act 1961) and to withdraw approval for an associated Approved Code of Practice.
Related Pictures
★リンクテーブル★
[★]
- 同
- FcεRII, 低親和性IgE受容体、Leucine-20、Blast-2
発現細胞
- 成熟B細胞、活性化マクロファージ、好酸球、濾胞樹状細胞、血小板
WCH.37
- B lymphocytes, where it appears to be associated with IgD
- follicular DCs, especially those in the light zone of the germinal centers
- transiently on some T cells in allergic individuals
- Langerhans cels
- monocytes
- platelets
- NK cells
- nasopharyngeal carcinoma cells
- B-CLL
- EBV-transformed B cells
機能
- IgEの受容体(低親和性)
- CD21やα-chain of the β2 integrinsにも結合する。
- 可溶性のCD23(sCD23)はIgEの産生を亢進したりIgE/Agの提示を促進したりする。またsCD23はいろいろなサイトカイン様の作用を呈する(WCH.37)
別名
ファミリー
臨床関連
CLL and WM
[★]
- 同
- Leucine-5, SRBC receptor, LFA-2
- 関
- CD
発現細胞
分子量
機能
- リンパ球が抗原提示細胞と相互作用するのに重要 (IMM.343)
別名
ファミリー