BCAM

Basal cell adhesion molecule (Lutheran blood group)
Rendering based on PDB 2PET​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2PET​, 2PF6​
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 Cellular component • plasma membrane • integral component of plasma membrane • external side of plasma membrane • extracellular exosome Biological process • cell adhesion • cell-matrix adhesion • signal transduction Sources: Amigo / QuickGO
RNA expression pattern
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

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).

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

1. "Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)".
2. 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.
3. 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.