Basal cell adhesion molecule

BCAM
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2PET, 2PF6
Identifiers
Aliases	BCAM, AU, CD239, LU, MSK19, basal cell adhesion molecule (Lutheran blood group)
External IDs	OMIM: 612773; MGI: 1929940; HomoloGene: 21149; GeneCards: BCAM; OMA:BCAM - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.32 Start 44,809,071 bp End 44,821,421 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 A3 Start 19,490,056 bp End 19,504,941 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube left lobe of thyroid gland popliteal artery tibial arteries right lobe of thyroid gland right coronary artery renal medulla left coronary artery apex of heart canal of the cervix Top expressed in interventricular septum lip molar right lung lumbar spinal ganglion left lung right lung lobe left lung lobe genital tubercle tunica media of zone of aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function laminin receptor activity protein C-terminus binding protein binding laminin binding transmembrane signaling receptor activity Cellular component integral component of membrane cell surface plasma membrane integral component of plasma membrane extracellular exosome membrane external side of plasma membrane extracellular matrix extracellular region collagen-containing extracellular matrix Biological process cell adhesion cell-matrix adhesion signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4059 57278 Ensembl ENSG00000187244 ENSMUSG00000002980 UniProt P50895 Q9R069 RefSeq (mRNA) NM_005581 NM_001013257 NM_020486 RefSeq (protein) NP_001013275 NP_005572 NP_065232 Location (UCSC) Chr 19: 44.81 – 44.82 Mb Chr 7: 19.49 – 19.5 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Basal cell adhesion molecule is a protein that in humans is encoded by the BCAM gene. BCAM has also recently been designated CD239 (cluster of differentiation 239).

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.

Interactions

BCAM has been shown to interact with Laminin, alpha 5.

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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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 U.S. 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.