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Chemical Compound Review

Borane(2)     $l^{2}-borane

Synonyms: BH2 Radical, AG-D-87723, CHEBI:33607, AC1L3FJG, CTK4C4116, ...
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Disease relevance of BH2 Radical


High impact information on BH2 Radical

  • The EGL-1 protein contains a nine amino acid region similar to the Bcl-2 homology region 3 (BH3) domain but does not contain a BH1, BH2, or BH4 domain, suggesting that EGL-1 may be a member of a family of cell death activators that includes the mammalian proteins Bik, Bid, Harakiri, and Bad [3].
  • Both yeast two-hybrid screening and lambda expression cloning identified a novel interacting protein, Bad, whose homology to Bcl-2 is limited to the BH1 and BH2 domains [4].
  • Using site-specific mutagenesis, we show here that the amino-acid residues critical for protection of cells by Bcl-XL against Sindbis virus-induced apoptosis are clustered within the Bcl-2-homology regions 1 and 2 (BH1 and BH2 regions) [5].
  • The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members [6].
  • A related protein that promotes cell death, Bax, wrestles with Bcl-2 through conserved motifs, BH1 and BH2, establishing a set point for these deaths [7].

Biological context of BH2 Radical

  • BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax [8].
  • A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions [9].
  • The overall amino acid sequence identity between KSbcl-2 and other Bcl-2 homologs is low (15-20%) but concentrated within the BH1 and BH2 regions [10].
  • The larger, more C-terminal region (within residues 90 to 203) encompassed, but extended beyond, two oligopeptide motifs called BH1 and BH2, which are known to mediate dimerization of Bc12 and related proteins [11].
  • Molecular modeling showed that BFL-1 could have a similar core structure as BCL-xL, consisting of seven alpha helices, although both proteins share only the conserved BCL-2 homology domains (BH1 and BH2 domains), but otherwise have very limited sequence homology, particularly in the N-terminal region [12].

Anatomical context of BH2 Radical


Associations of BH2 Radical with other chemical compounds


Gene context of BH2 Radical

  • The BCL2L12 protein contains one BH2 homology domain, one proline-rich region similar to the TC21 protein and, five consensus PXXP tetrapeptide sequences [20].
  • All BCL2 homology domains (BH1, BH2, BH3, and BH4) in bovine BCL2A1 were conserved as well as in other mammalian BCL2A1 [21].
  • Neither the BH1 nor the BH2 domain of Bax was required for binding to the wild-type Bcl-2 and Bax proteins [22].
  • We identified a short splicing variant of the MCL-1 mRNA in the human placenta encoding a protein, termed MCL-1 short (MCL-1S), with an altered C terminus as compared with the full-length MCL-1 long (MCL-1L), leading to the loss of BH1, BH2, and the transmembrane domains [23].
  • N-Bak is generated by neuron-specific splicing of a novel 20-base pair exon, which changes the previously described Bak, containing Bcl-2 homology (BH) domains BH1, BH2, and BH3, into a shorter BH3-only protein [24].

Analytical, diagnostic and therapeutic context of BH2 Radical

  • By GenBank database searches and PCR, we have identified a novel human Bcl2-like gene, Bcl2-L-10, which contains conserved BH4, BH1 and BH2 domains but lacks BH3 domain [25].
  • Immunoprecipitation studies revealed that Bax with deletions in BH1 and BH2 still associated with wild-type Bax while deletion of BH3 disrupted Bax homodimerization [26].
  • METHODS: An initial survey was conducted with reverse transcription-polymerase chain reaction (RT-PCR), using oligonucleotides against identified members of this family and against the conserved BH1 and BH2 domains [27].
  • Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family [20].
  • 4. Based on 16S rRNA gene sequence analysis and other physiological characteristics, strain BH2 constitutes a new species within the genus Ferroplasma [28].


  1. Electrophoretic mobility of mouse T-cell hybrids. Bubeník, J., Perlmann, P., Jónsdóttir, I., Kypĕnová, H., Bubeníková, D., Símová, J. Br. J. Cancer (1981) [Pubmed]
  2. T-cell hybrids. IV. One of parental cell lines is dominant in determining membrane characteristics of hybrid cells. Bubeník, J., Dreyer, G., Junge, C., Stolley, P., Abel, H., Mach, O., Indrová, M., Bubeníková, D., Jandlová, T., Símová, J. Neoplasma (1983) [Pubmed]
  3. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Conradt, B., Horvitz, H.R. Cell (1998) [Pubmed]
  4. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Yang, E., Zha, J., Jockel, J., Boise, L.H., Thompson, C.B., Korsmeyer, S.J. Cell (1995) [Pubmed]
  5. Bax-independent inhibition of apoptosis by Bcl-XL. Cheng, E.H., Levine, B., Boise, L.H., Thompson, C.B., Hardwick, J.M. Nature (1996) [Pubmed]
  6. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Muchmore, S.W., Sattler, M., Liang, H., Meadows, R.P., Harlan, J.E., Yoon, H.S., Nettesheim, D., Chang, B.S., Thompson, C.B., Wong, S.L., Ng, S.L., Fesik, S.W. Nature (1996) [Pubmed]
  7. Regulators of cell death. Korsmeyer, S.J. Trends Genet. (1995) [Pubmed]
  8. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Yin, X.M., Oltvai, Z.N., Korsmeyer, S.J. Nature (1994) [Pubmed]
  9. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. Chittenden, T., Flemington, C., Houghton, A.B., Ebb, R.G., Gallo, G.J., Elangovan, B., Chinnadurai, G., Lutz, R.J. EMBO J. (1995) [Pubmed]
  10. A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. Cheng, E.H., Nicholas, J., Bellows, D.S., Hayward, G.S., Guo, H.G., Reitz, M.S., Hardwick, J.M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  11. Functional dissection of the human Bc12 protein: sequence requirements for inhibition of apoptosis. Hunter, J.J., Bond, B.L., Parslow, T.G. Mol. Cell. Biol. (1996) [Pubmed]
  12. Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells. Zhang, H., Cowan-Jacob, S.W., Simonen, M., Greenhalf, W., Heim, J., Meyhack, B. J. Biol. Chem. (2000) [Pubmed]
  13. Mitogenic effects of tetrahydrobiopterin in PC12 cells. Anastasiadis, P.Z., States, J.C., Imerman, B.A., Louie, M.C., Kuhn, D.M., Levine, R.A. Mol. Pharmacol. (1996) [Pubmed]
  14. Inhibition by N-acetyl-5-hydroxytryptamine of nitric oxide synthase expression in cultured cells and in the anaesthetized rat. Klemm, P., Hecker, M., Stockhausen, H., Wu, C.C., Thiemermann, C. Br. J. Pharmacol. (1995) [Pubmed]
  15. T-cell hybrids. II. BH2 line-derivation by fusion between two (BW5147 X EL-4R) thymoma lines. Bubeník, J., Perlmann, P., Jónsdóttir, I., Kypĕnová, H., Bubeníková, D., Indrová, M., Loudová, M. Neoplasma (1982) [Pubmed]
  16. Bax can antagonize Bcl-XL during etoposide and cisplatin-induced cell death independently of its heterodimerization with Bcl-XL. Simonian, P.L., Grillot, D.A., Merino, R., Nuñez, G. J. Biol. Chem. (1996) [Pubmed]
  17. Modulation by pterins of the phosphorylation and phenylalanine activation of phenylalanine 4-mono-oxygenase. Døskeland, A.P., Haavik, J., Flatmark, T., Døskeland, S.O. Biochem. J. (1987) [Pubmed]
  18. Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity. McKinney, J., Teigen, K., Frøystein, N.A., Salaün, C., Knappskog, P.M., Haavik, J., Martínez, A. Biochemistry (2001) [Pubmed]
  19. Stereoselective effects in the interactions of pterin cofactors with rat-liver phenylalanine 4-monooxygenase. Haavik, J., Døskeland, A.P., Flatmark, T. Eur. J. Biochem. (1986) [Pubmed]
  20. Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family. Scorilas, A., Kyriakopoulou, L., Yousef, G.M., Ashworth, L.K., Kwamie, A., Diamandis, E.P. Genomics (2001) [Pubmed]
  21. Cloning of the bovine antiapoptotic regulator, BCL2-related protein A1, and its expression in trophoblastic binucleate cells of bovine placenta. Ushizawa, K., Takahashi, T., Kaneyama, K., Hosoe, M., Hashizume, K. Biol. Reprod. (2006) [Pubmed]
  22. Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. Zha, H., Aimé-Sempé, C., Sato, T., Reed, J.C. J. Biol. Chem. (1996) [Pubmed]
  23. MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. Bae, J., Leo, C.P., Hsu, S.Y., Hsueh, A.J. J. Biol. Chem. (2000) [Pubmed]
  24. Neuron-specific Bcl-2 homology 3 domain-only splice variant of Bak is anti-apoptotic in neurons, but pro-apoptotic in non-neuronal cells. Sun, Y.F., Yu, L.Y., Saarma, M., Timmusk, T., Arumae, U. J. Biol. Chem. (2001) [Pubmed]
  25. Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks apoptosis in the mitochondria death pathway but not in the death receptor pathway. Zhang, H., Holzgreve, W., De Geyter, C. Hum. Mol. Genet. (2001) [Pubmed]
  26. Bax homodimerization is not required for Bax to accelerate chemotherapy-induced cell death. Simonian, P.L., Grillot, D.A., Andrews, D.W., Leber, B., Nuñez, G. J. Biol. Chem. (1996) [Pubmed]
  27. Identification of the bcl-2 family of genes in the rat retina. Levin, L.A., Schlamp, C.L., Spieldoch, R.L., Geszvain, K.M., Nickells, R.W. Invest. Ophthalmol. Vis. Sci. (1997) [Pubmed]
  28. Ferroplasma cupricumulans sp. nov., a novel moderately thermophilic, acidophilic archaeon isolated from an industrial-scale chalcocite bioleach heap. Hawkes, R.B., Franzmann, P.D., O'hara, G., Plumb, J.J. Extremophiles (2006) [Pubmed]
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