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Gene Review

Dtnb  -  dystrobrevin, beta

Mus musculus

Synonyms: Beta-dystrobrevin, DTN-B, Dystrobrevin beta, mDTN-B
 
 
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Disease relevance of Dtnb

 

High impact information on Dtnb

  • In common with dystrophin, beta-dystrobrevin is found in neurons of the cortex and hippocampal formation but is not found in the brain microvasculature [2].
  • In addition, the levels of several beta-dystrobrevin-interacting proteins, namely Dp71 isoforms and the syntrophins, were greatly reduced from the basal membranes of kidney tubules and liver sinusoids and on Western blots of crude kidney and liver microsomes of beta-dystrobrevin-deficient mice [3].
  • Dystrobrevins are now thought to play an important role in intracellular signal transduction, in addition to providing a membrane scaffold in muscle, but the precise role of beta-dystrobrevin has not yet been determined [4].
  • These complexes can be broadly grouped according to their dystrobrevin content: beta-dystrobrevin containing complexes are present at the basal region of renal epithelial cells, whilst alpha-dystrobrevin-1 containing complexes are found in endothelial and smooth muscle cells [5].
  • In the present study, we assessed the kinetics of the dystrobrevin-Kif5A interaction by quantitative pull-down assay and surface plasmon resonance (SPR) analysis and found that beta-dystrobrevin binds to kinesin with high affinity (K(D) approximately 40 nM) [6].
 

Biological context of Dtnb

 

Anatomical context of Dtnb

  • Dialysis of myocytes with GSH (5 mM) or DTT (5 mM) prevented suppression of Ito by H2O2 and DTNB but did not alter the effects of NH2Cl or Ch-T on either Idr or Ito [8].
  • The effects of reduction by DTT, oxidation by DTNB and treatment with NEM on the thiol contents and insulin binding to its receptor in mice liver membranes were studied [9].
 

Associations of Dtnb with chemical compounds

  • Sequence analysis indicates that this gene, named DTN-B, is highly homologous to the rabbit A0, the previously described dystrobrevin (DTN), Torpedo 87 kDa and to the C-terminus of dystrophin [10].
  • Finally, DTT pretreatment enhanced the long lasting allodynia induced by i.t. administration of dynorphin, whereas post-treatment with DTNB reduced the permanent allodynia induced by dynorphin for 5 days [11].
  • The dibasic cleaving enzyme was completely inhibited in the presence of 20-50 mM amine buffers, 0.1 mM EDTA, 0.5 mM 1,10-phenanthroline, 0.5 mM N-ethylmaleimide, and 1mM DTNB [12].
  • Intrathecal (i.t.) administration of DTT (0.1-30 nmol), presumably reducing the NMDA receptor, dose-dependently enhanced NMDA-induced nociceptive behaviors, and this enhancement was blocked by the oxidizing agent, DTNB [11].
  • Arsenicals and arsinothiols, complexes of As(III)-containing compounds with L-cysteine or glutathione, were tested as inhibitors of the DTNB reductase activity of the purified enzyme [13].
 

Analytical, diagnostic and therapeutic context of Dtnb

References

  1. Genomic organization and refined mapping of the mouse beta-dystrobrevin gene. Loh, N.Y., Ambrose, H.J., Guay-Woodford, L.M., DasGupta, S., Nawrotzki, R.A., Blake, D.J., Davies, K.E. Mamm. Genome (1998) [Pubmed]
  2. beta-dystrobrevin, a member of the dystrophin-related protein family. Blake, D.J., Nawrotzki, R., Loh, N.Y., Górecki, D.C., Davies, K.E. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. Role of beta-dystrobrevin in nonmuscle dystrophin-associated protein complex-like complexes in kidney and liver. Loh, N.Y., Nebenius-Oosthuizen, D., Blake, D.J., Smith, A.J., Davies, K.E. Mol. Cell. Biol. (2001) [Pubmed]
  4. Beta-dystrobrevin interacts directly with kinesin heavy chain in brain. Macioce, P., Gambara, G., Bernassola, M., Gaddini, L., Torreri, P., Macchia, G., Ramoni, C., Ceccarini, M., Petrucci, T.C. J. Cell. Sci. (2003) [Pubmed]
  5. Assembly of multiple dystrobrevin-containing complexes in the kidney. Loh, N.Y., Newey, S.E., Davies, K.E., Blake, D.J. J. Cell. Sci. (2000) [Pubmed]
  6. Molecular basis of dystrobrevin interaction with kinesin heavy chain: structural determinants of their binding. Ceccarini, M., Torreri, P., Lombardi, D.G., Macchia, G., Macioce, P., Petrucci, T.C. J. Mol. Biol. (2005) [Pubmed]
  7. For want of a nail. ramifications of a single gene deletion, dystrophin, in the brain of the mouse. Wallis, T., Bubb, W.A., McQuillan, J.A., Balcar, V.J., Rae, C. Front. Biosci. (2004) [Pubmed]
  8. Differential modulation of voltage-dependent K+ currents in colonic smooth muscle by oxidants. Prasad, M., Goyal, R.K. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
  9. Role of thiol-disulfide exchange in insulin binding to its receptor. Xie, G.F., Li, S.L., Wanc, Z.Z. Sci. China, Ser. B, Chem. Life Sci. Earth Sci. (1992) [Pubmed]
  10. Identification and characterization of a novel member of the dystrobrevin gene family. Puca, A.A., Nigro, V., Piluso, G., Belsito, A., Sampaolo, S., Quaderi, N., Rossi, E., Di Iorio, G., Ballabio, A., Franco, B. FEBS Lett. (1998) [Pubmed]
  11. Redox manipulation of NMDA receptors in vivo: alteration of acute pain transmission and dynorphin-induced allodynia. Laughlin, T.M., Kitto, K.F., Wilcox, G.L. Pain (1999) [Pubmed]
  12. Purification and characterization of a secreted arginine-specific dibasic cleaving enzyme from EL-4 cells. Csuhai, E., Safavi, A., Hersh, L.B. Biochemistry (1995) [Pubmed]
  13. Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase. Lin, S., Cullen, W.R., Thomas, D.J. Chem. Res. Toxicol. (1999) [Pubmed]
  14. The properties of the metal-thiolate clusters in recombinant mouse metallothionein-4. Cai, B., Zheng, Q., Huang, Z.X. Protein J. (2005) [Pubmed]
 
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