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Bcam  -  basal cell adhesion molecule

Mus musculus

Synonyms: 1200005K12Rik, B-CAM, B-CAM cell surface glycoprotein, Basal cell adhesion molecule, Gplu, ...
 
 
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Disease relevance of Bcam

 

High impact information on Bcam

  • Thus, B-CAM/LU appears to be the major laminin-binding protein of sickle red cells [4].
  • Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin [4].
  • These results further support a role for Lu gps in sickle cell disease and indicate the utility of mouse models to explore the function of Lu gp-laminin 10/11 interaction in normal erythropoiesis and in sickle cell disease [5].
  • Laminin alpha5 is present in the subendothelium and is also a constituent of bone marrow sinusoids, suggesting a role for the Lu/laminin interaction in erythropoiesis [5].
  • To this end, complementary DNA and genomic clones for the mouse homologue were sequenced and the mouse Lu gene mapped to a region on chromosome 7 with conserved synteny with human 19q13 [5].
 

Biological context of Bcam

  • As in the human, the mouse Lu gene is organized in 15 exons [1].
  • During mouse embryonic development, the Lu transcript is detected as early as day 7 of gestation [1].
  • Proteins derived from transgenes were detected in basement membranes and were assayed for their ability to bind Lu by examining the localization of endogenous Lu and the binding of sol-Lu applied to tissue sections [6].
  • In contrast, fetal skin (15th to 18th week of gestation) was characterized by B-CAM-positive cells in the basal layer of the epidermis as well as in the outer root sheath of hair follicles [2].
  • A strong B-CAM-positive phenotype can be found in the outer root sheath of hair follicles of adult and fetal human skin as well as in fetal basal keratinocytes [2].
 

Anatomical context of Bcam

  • We propose that laminin alpha5 is involved in concentrating Lu on the basal surface of epithelial cells [7].
  • Finally, in proof-of-principle experiments, human B-CAM was overexpressed both in murine and in human fibroblasts [3].
  • The pattern of B-CAM expression in cultured cells suggests that the molecule is associated with a substrate-adherent growth pattern in some lineages [2].
  • Treatment with DDTC moderately enhanced Cd levels in lung (Lu), heart (He) and testes (Te), and increased brain (Br) levels to over 500 percent of control values [8].
 

Associations of Bcam with chemical compounds

  • In vitro studies have suggested that the Lutheran blood group glycoprotein/basal cell adhesion molecule (Lu), an Ig superfamily transmembrane protein, is a receptor for laminins containing the alpha5 chain [7].
  • The haptotactic migration of these novel B-CAM+ cell populations on a laminin matrix was significantly increased (P = 0.02) as compared to mock-transfected cells when integrin-mediated adhesion was blocked by chelation of divalent cations [3].
 

Other interactions of Bcam

  • Towards this end, B-CAM expression was assessed in HaCaT transfectants overexpressing murine Bcl-2 and untransfected HaCaT cells exposed to various proapoptotic stimuli [9].
 

Analytical, diagnostic and therapeutic context of Bcam

  • We investigated the expression of B-CAM in normal and diseased human epidermis by means of immunohistochemistry employing a single batch of high-titer mouse monoclonal antibody G253 [2].

References

  1. Characterization of a mouse liminin receptor gene homologous to the human blood group Lutheran gene. Rahuel, C., Colin, Y., Goossens, D., Gane, P., El Nemer, W., Cartron, J.P., Le Van Kim, C. Immunogenetics (1999) [Pubmed]
  2. Expression of the basal cell adhesion molecule (B-CAM) in normal and diseased human skin. Bernemann, T.M., Podda, M., Wolter, M., Boehncke, W.H. J. Cutan. Pathol. (2000) [Pubmed]
  3. Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer. Drewniok, C., Wienrich, B.G., Schön, M., Ulrich, J., Zen, Q., Telen, M.J., Hartig, R.J., Wieland, I., Gollnick, H., Schön, M.P. Arch. Dermatol. Res. (2004) [Pubmed]
  4. Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. Udani, M., Zen, Q., Cottman, M., Leonard, N., Jefferson, S., Daymont, C., Truskey, G., Telen, M.J. J. Clin. Invest. (1998) [Pubmed]
  5. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. Parsons, S.F., Lee, G., Spring, F.A., Willig, T.N., Peters, L.L., Gimm, J.A., Tanner, M.J., Mohandas, N., Anstee, D.J., Chasis, J.A. Blood (2001) [Pubmed]
  6. Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo. Kikkawa, Y., Moulson, C.L., Virtanen, I., Miner, J.H. J. Biol. Chem. (2002) [Pubmed]
  7. Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo. Moulson, C.L., Li, C., Miner, J.H. Dev. Dyn. (2001) [Pubmed]
  8. Effects of diethyldithiocarbamate on organ distribution and excretion of cadmium. Gale, G.R., Atkins, L.M., Walker, E.M. Ann. Clin. Lab. Sci. (1982) [Pubmed]
  9. Basal cell adhesion molecule is inversely associated with apoptosis, but plays a limited role for protection against apoptotic stimuli. Drewniok, C., Schön, M., Schön, M.P. Skin pharmacology and physiology. (2004) [Pubmed]
 
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