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Gene Review:

BST2 - bone marrow stromal cell antigen 2

Homo sapiens

Synonyms: BST-2, Bone marrow stromal antigen 2, CD317, HM1.24 antigen, TETHERIN, ...

Ge, Y. et al., Ishikawa, J. et al., Walter-Yohrling, J. et al., Kupzig, S. et al., Ohtomo, T. et al., et al.

Loyet, Ouyang, Eaton, Stults,

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Disease relevance of BST2

In situ hybridization of metastatic and nonmetastatic ovarian cancer demonstrated selective expression of bone marrow stromal antigen 2 and tumor necrosis factor receptor superfamily member 5 in the metastatic disease [1].

High impact information on BST2

CMK sublines, transfected with the BST2 cDNA and incubated with HS-5 bone marrow stromal cells, exhibited up to 1.7-fold reduced cytosine arabinoside (ara-C)-induced apoptosis, compared with mock-transfected cells [2].
Transcripts for the bone marrow stromal-cell antigen 2 (BST2) gene, encoding a transmembrane glycoprotein potentially involved in interactions between leukemia cells and bone marrow stromal cells, were 7.3-fold higher (validated by real-time polymerase chain reaction) in the non-DS compared with the DS group [2].
The strongest correlations were for bone marrow stromal antigen 2, stathmin-like 3, tumor necrosis factor receptor superfamily member 5, and hepatocyte growth factor tyrosine kinase substrate [1].
Expression of the HM1.24 gene (BST2) was assessed using purified plasma cells and Affymetrix-U133A+B microarrays [3].
We also show that the cell surface pool of BST-2/HM1.24 is predominantly present in the apical plasma membrane of polarized cells [4].

Biological context of BST2

The BST-2 gene (HGMW-approved symbol BST2) is located on chromosome 19p13 [5].

Anatomical context of BST2

Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth [5].
We cloned a cDNA encoding BST-2 from a rheumatoid arthritis-derived synovial cell line [5].
BST-2 surface expression on fibroblast cell lines facilitated the stromal cell-dependent growth of a murine bone marrow-derived pre-B-cell line, DW34 [5].

Associations of BST2 with chemical compounds

The HM1.24 antigen is a type II membrane glycoprotein, which has been reported as a bone marrow stromal cell surface antigen BST2, and may exist as a homodimer on myeloma cell surface [6].
The fact that rat BST-2/HM1.24 apparently possesses a GPI anchor led us to speculate that it might exist in cholesterol-rich lipid microdomains (lipid rafts) at the plasma membrane [4].

Other interactions of BST2

The greatest differing Th1 to Th2 ratios were observed for BST2 (bone marrow stromal protein 2) and TRIM (T cell receptor interacting molecule) [7].

References

Identification of genes expressed in malignant cells that promote invasion. Walter-Yohrling, J., Cao, X., Callahan, M., Weber, W., Morgenbesser, S., Madden, S.L., Wang, C., Teicher, B.A. Cancer Res. (2003) [Pubmed]
Differential gene expression, GATA1 target genes, and the chemotherapy sensitivity of Down syndrome megakaryocytic leukemia. Ge, Y., Dombkowski, A.A., LaFiura, K.M., Tatman, D., Yedidi, R.S., Stout, M.L., Buck, S.A., Massey, G., Becton, D.L., Weinstein, H.J., Ravindranath, Y., Matherly, L.H., Taub, J.W. Blood (2006) [Pubmed]
Identification of a new HLA-A2-restricted T-cell epitope within HM1.24 as immunotherapy target for multiple myeloma. Hundemer, M., Schmidt, S., Condomines, M., Lupu, A., Hose, D., Moos, M., Cremer, F., Kleist, C., Terness, P., Belle, S., Ho, A.D., Goldschmidt, H., Klein, B., Christensen, O. Exp. Hematol. (2006) [Pubmed]
Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Kupzig, S., Korolchuk, V., Rollason, R., Sugden, A., Wilde, A., Banting, G. Traffic (2003) [Pubmed]
Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth. Ishikawa, J., Kaisho, T., Tomizawa, H., Lee, B.O., Kobune, Y., Inazawa, J., Oritani, K., Itoh, M., Ochi, T., Ishihara, K. Genomics (1995) [Pubmed]
Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells. Ohtomo, T., Sugamata, Y., Ozaki, Y., Ono, K., Yoshimura, Y., Kawai, S., Koishihara, Y., Ozaki, S., Kosaka, M., Hirano, T., Tsuchiya, M. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
Proteomic profiling of surface proteins on Th1 and Th2 cells. Loyet, K.M., Ouyang, W., Eaton, D.L., Stults, J.T. J. Proteome Res. (2005) [Pubmed]

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