Basal cell adhesion molecule

Last updated
BCAM
Protein BCAM PDB 2PET.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases BCAM , AU, CD239, LU, MSK19, basal cell adhesion molecule (Lutheran blood group)
External IDs OMIM: 612773 MGI: 1929940 HomoloGene: 21149 GeneCards: BCAM
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Basal cell adhesion molecule, also known as Lutheran antigen , is a plasma membrane glycoprotein that in humans is encoded by the BCAM gene. [5] BCAM has also recently been designated CD239 (cluster of differentiation 239).

Contents

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. [5]

Interactions

BCAM has been shown to interact with Laminin, alpha 5. BCAM has also been shown to promote the metastasis of ovarian cancer. [6] [7] [8]

Related Research Articles

<span class="mw-page-title-main">L1 (protein)</span> Mammalian protein found in Homo sapiens

L1, also known as L1CAM, is a transmembrane protein member of the L1 protein family, encoded by the L1CAM gene. This protein, of 200-220 kDa, is a neuronal cell adhesion molecule with a strong implication in cell migration, adhesion, neurite outgrowth, myelination and neuronal differentiation. It also plays a key role in treatment-resistant cancers due to its function. It was first identified in 1984 by M. Schachner who found the protein in post-mitotic mice neurons.

<span class="mw-page-title-main">P-selectin glycoprotein ligand-1</span> Protein-coding gene in the species Homo sapiens

Selectin P ligand, also known as SELPLG or CD162, is a human gene.

<span class="mw-page-title-main">CD44</span> Cell-surface glycoprotein

The CD44 antigen is a cell-surface glycoprotein involved in cell–cell interactions, cell adhesion and migration. In humans, the CD44 antigen is encoded by the CD44 gene on chromosome 11. CD44 has been referred to as HCAM, Pgp-1, Hermes antigen, lymphocyte homing receptor, ECM-III, and HUTCH-1.

<span class="mw-page-title-main">CD164</span> Protein-coding gene in the species Homo sapiens

Sialomucin core protein 24 also known as endolyn or CD164 is a protein that in humans is encoded by the CD164 gene. CD164 functions as a cell adhesion molecule.

<span class="mw-page-title-main">CD146</span> Protein-coding gene in the species Homo sapiens

CD146 also known as the melanoma cell adhesion molecule (MCAM) or cell surface glycoprotein MUC18, is a 113kDa cell adhesion molecule currently used as a marker for endothelial cell lineage. In humans, the CD146 protein is encoded by the MCAM gene.

<span class="mw-page-title-main">Lutheran antigen system</span> Human blood group system

The Lutheran antigen systems is a classification of human blood based on the presence of substances called Lutheran antigens on the surfaces of red blood cells. There are 19 known Lutheran antigens. The name Lutheran stems from a blood donor's misspelled last name, reportedly named Lutteran or Luteran. All of these antigens arise from variations in a gene called BCAM. The system is based on the expression of two codominant alleles, designated Lua and Lub. The antigens Aua and Aub, known as the Auberger antigens, were once thought to make up a separate blood group but were later shown to be Lutheran antigens arising from variations in the BCAM gene.

<span class="mw-page-title-main">CEACAM1</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) also known as CD66a, is a human glycoprotein, and a member of the carcinoembryonic antigen (CEA) gene family.

<span class="mw-page-title-main">Laminin, alpha 5</span> Protein-coding gene in the species Homo sapiens

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.

<span class="mw-page-title-main">Laminin subunit gamma-2</span> Protein-coding gene in the species Homo sapiens

Laminin subunit gamma-2 is a protein that in humans is encoded by the LAMC2 gene.

<span class="mw-page-title-main">Signal-regulatory protein alpha</span> Protein-coding gene in the species Homo sapiens

Signal regulatory protein α (SIRPα) is a regulatory membrane glycoprotein from SIRP family expressed mainly by myeloid cells and also by stem cells or neurons.

<span class="mw-page-title-main">Cell adhesion molecule 1</span> Protein involved in attachment of cells

Cell adhesion molecule 1 is a protein that, in humans, is encoded by the CADM1 gene.

<span class="mw-page-title-main">Laminin subunit gamma-1</span> Protein-coding gene in the species Homo sapiens

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.

<span class="mw-page-title-main">Epithelial cell adhesion molecule</span> Transmembrane glycoprotein

Epithelial cell adhesion molecule (EpCAM), also known as CD326 among other names, is a transmembrane glycoprotein mediating Ca2+-independent homotypic cell–cell adhesion in epithelia. EpCAM is also involved in cell signaling, migration, proliferation, and differentiation. Additionally, EpCAM has oncogenic potential via its capacity to upregulate c-myc, e-fabp, and cyclins A & E. Since EpCAM is expressed exclusively in epithelia and epithelial-derived neoplasms, EpCAM can be used as diagnostic marker for various cancers. It appears to play a role in tumorigenesis and metastasis of carcinomas, so it can also act as a potential prognostic marker and as a potential target for immunotherapeutic strategies.

<span class="mw-page-title-main">Laminin, beta 1</span> Protein-coding gene in the species Homo sapiens

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.

<span class="mw-page-title-main">CEACAM6</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 6 (CEACAM6) also known as CD66c, is a member of the carcinoembryonic antigen (CEA) gene family..

<span class="mw-page-title-main">ALCAM</span> Protein-coding gene in the species Homo sapiens

CD166 antigen is a 100-105 kD typeI transmembrane glycoprotein that is a member of the immunoglobulin superfamily of proteins. In humans it is encoded by the ALCAM gene. It is also called CD166, MEMD, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat.

<span class="mw-page-title-main">NRCAM</span> Protein-coding gene in the species Homo sapiens

Neuronal cell adhesion molecule is a protein that in humans is encoded by the NRCAM gene.

<span class="mw-page-title-main">CEACAM8</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 8 (CEACAM8) also known as CD66b, is a member of the carcinoembryonic antigen (CEA) gene family. Its main function is cell adhesion, cell migration, and pathogen binding.

<span class="mw-page-title-main">Laminin subunit gamma-3</span> Protein-coding gene in the species Homo sapiens

Laminin subunit gamma-3 also known as LAMC3 is a protein that in humans is encoded by the LAMC3 gene.

<span class="mw-page-title-main">HEPACAM</span> Protein-coding gene in the species Homo sapiens

Gene HEPACAM*, named based on its original site of identification - hepatocytes and the nature of its protein product - a cell adhesion molecule (CAM), was first discovered and characterised in human liver and reported by Shali Shen in 2005. The gene encodes a protein of 416 amino acids, designated as hepaCAM**, which is a new member of the immunoglobulin superfamily of cell adhesion molecules. The main biological functions of hepaCAM include a) modulating cell-matrix adhesion and migration, and b) inhibiting cancer cell growth.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000187244 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000002980 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 "Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)".
  6. 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. S2CID   10715366.
  7. 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.
  8. Sivakumar S, Lieber S, Librizzi D (2023). "Basal cell adhesion molecule promotes metastasis-associated processes in ovarian cancer". Clin Transl Med. 13 (1): e1176. doi: 10.1002/ctm2.1176 . PMC   9842900 . PMID   36647260.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.