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Gene Review

DTNB  -  dystrobrevin, beta

Homo sapiens

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

  • Likewise, L-cysteine induces mechanical DTNB-sensitive hyperalgesia in peripheral receptive fields [1].
  • However, the cell-surface thiol-reactive reagent 5, 5'-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion [2].
  • The K(M) values were 4.5 microM for NADPH, 480 microM for DTNB and 36 microM for Escherichia coli thioredoxin, the turnover number with DTNB being approximately 40 s(-1) [3].
  • Porphyrin photosensitization of proteins in cell membranes as studied by spin-labelling and by quantification of DTNB-reactive SH-groups [4].
  • Although unaffected by pertussis toxin, sulfite-triggered PMN adhesion was abrogated by pretreating cells with the membrane-impermeant sulfhydryl reagent 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), a modifier of thiol groups on the cell surface [5].

High impact information on DTNB

  • Contrary to expectations, however, we found that when compared to matched, nonpsychiatric controls, 73-93% of cases in two schizophrenia populations displayed presynaptic dysbindin-1 reductions averaging 18-42% (P = 0.027-0.0001) at hippocampal formation sites lacking neuronal dystrobrevin (i.e., beta-dystrobrevin) [6].
  • DTNB alone and in combination with mibefradil induces thermal analgesia [1].
  • Isolation and chemical analysis of the DTNB-treated GIF derivative revealed that binding the 5-thio-2-nitrobenzoic acid group with Cys-60 was responsible for the generation of the highly bioactive derivative [7].
  • NMDA-activated currents were recorded under control conditions and in the presence of a thiol reductant (DTT), an oxidant (5, 5'-dithio-bis[2-nitrobenzoic acid], DTNB), or the noncompetitive antagonist CP101,606 (CP) [8].
  • The classical inhibitor of LCAT activity, 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), which strongly (89%) inhibited the native enzyme, had partial (45%) inhibitory activity with mutant enzyme species containing a single -SH residue, while the double mutant was not significantly inhibited by DTNB [9].

Chemical compound and disease context of DTNB


Biological context of DTNB

  • These data are interpreted to suggest that Cys-31 and Cys-184 are vicinal both to each other and to the "interfacial binding site" at residues 177-182, and that DTNB exerts its effect by steric inhibition [9].
  • Both HDL cholesterol esterification and particle enlargement were abolished completely by the LCAT inhibitor DTNB and by heat inactivation of the purified normal LCAT [11].
  • Preincubation of these IDL with normal plasma in the absence of 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) increased the rate of hydrolysis, in the presence of DTNB, this increment was not observed [12].
  • Here, we identify a human gene on chromosome 2p22-23 that encodes a novel protein, beta-dystrobrevin, with significant homology to the other known dystrobrevin (now termed alpha-dystrobrevin) [13].
  • Dependence of retina cell aggregation on disulfide exchange activity was shown by blocking that activity with the inhibitor, DTNB, or with a recombinant human PDI with the -WCGHC- motif cysteines mutated [14].

Anatomical context of DTNB


Associations of DTNB with chemical compounds

  • However, treatment of the inactive rhGIF with ethylmercurithiosalicylate or 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) resulted in the generation of derivatives whose bioactivity was comparable to that of the Ts-derived bioactive GIF [7].
  • This shift in apoA-I mass to alpha electrophoretic mobility was blocked by the addition of either 1.4 mM DTNB or 10 mM menthol to the plasma prior to incubation, suggesting that lecithin:cholesterol acyltransferase (LCAT) activity was involved [20].
  • Interestingly, the T5A mutant exhibited distinct metal thiolate activity in the EDTA and DTNB reactions, and also lost its bioactivity [21].
  • It was shown previously that Cys-67 of the native enzyme reacted with 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB, Ellman's reagent) at pH 6.2, causing a reversible inactivation of the protease [22].
  • The reactivity of this synthetic peptide with DTNB mimicked that of the protease, being more reactive in the absence of 6 M guanidine hydrochloride than in its presence [22].

Physical interactions of DTNB


Regulatory relationships of DTNB


Other interactions of DTNB

  • Thus, like alpha-dystrobrevin, beta-dystrobrevin is likely to associate directly with dystrophin. alpha- and beta-dystrobrevins failed to copurify with each other, however [13].
  • Both the membrane-permeable thiol-group oxidizing agent DTNP [2,2'-dithiobis-(5-nitropyridine)] and the membrane-impermeable DTNB [5,5'-Dithiobis-(2-nitrobenzoic acid)] (50 microM) inhibited Kv1.3 channels, suggesting that extracellular domains of Kv1.3 are affected [25].
  • The analogues were competitive inhibitors with DTNB for reduction by thioredoxin reductase, with Ki values for III-2, IV-2, and VII-2 being 3.3, 13.0, and 8.6 microM, respectively [26].
  • Labeling of free SH groups with tritiated NEM after preincubation of cells with DTNB and VIP made possible the characterization of reacting SH groups which probably belong to the receptor [27].
  • Both this active mutant and wild-type NFI-C protein were inactivated by modification of their sulfhydryl residues with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), and preincubation with an oligonucleotide containing an NFI-binding site gave partial protection against inactivation [28].

Analytical, diagnostic and therapeutic context of DTNB


  1. Redox modulation of T-type calcium channels in rat peripheral nociceptors. Todorovic, S.M., Jevtovic-Todorovic, V., Meyenburg, A., Mennerick, S., Perez-Reyes, E., Romano, C., Olney, J.W., Zorumski, C.F. Neuron (2001) [Pubmed]
  2. Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion. Ou, W., Silver, J. Virology (2006) [Pubmed]
  3. The 58 kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase. Gromer, S., Schirmer, R.H., Becker, K. FEBS Lett. (1997) [Pubmed]
  4. Porphyrin photosensitization of proteins in cell membranes as studied by spin-labelling and by quantification of DTNB-reactive SH-groups. Moan, J., Vistnes, A.I. Photochem. Photobiol. (1986) [Pubmed]
  5. Sulfite induces adherence of polymorphonuclear neutrophils to immobilized fibrinogen through activation of Mac-1 beta2-integrin (CD11b/CD18). Shigehara, T., Mitsuhashi, H., Ota, F., Kuroiwa, T., Kaneko, Y., Ueki, K., Tsukada, Y., Maezawa, A., Nojima, Y. Life Sci. (2002) [Pubmed]
  6. Dysbindin-1 is reduced in intrinsic, glutamatergic terminals of the hippocampal formation in schizophrenia. Talbot, K., Eidem, W.L., Tinsley, C.L., Benson, M.A., Thompson, E.W., Smith, R.J., Hahn, C.G., Siegel, S.J., Trojanowski, J.Q., Gur, R.E., Blake, D.J., Arnold, S.E. J. Clin. Invest. (2004) [Pubmed]
  7. Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group. Nakano, T., Watarai, H., Liu, Y.C., Oyama, Y., Mikayama, T., Ishizaka, K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Functional consequences of NR2 subunit composition in single recombinant N-methyl-D-aspartate receptors. Brimecombe, J.C., Boeckman, F.A., Aizenman, E. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  9. Effects of site-directed mutagenesis at residues cysteine-31 and cysteine-184 on lecithin-cholesterol acyltransferase activity. Francone, O.L., Fielding, C.J. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  10. Sensitivity and resistance in human metastatic melanoma to the new chloroethylnitrosourea anti-tumor drug Fotemustine. Schallreuter, K.U., Wood, J.M. Biochim. Biophys. Acta (1991) [Pubmed]
  11. Normalization of high density lipoprotein in fish eye disease plasma by purified normal human lecithin: cholesterol acyltransferase. Holmquist, L., Carlson, L.A. Lipids (1988) [Pubmed]
  12. Impaired intermediate-density lipoprotein triglyceride hydrolysis in familial lecithin:cholesterol acyltransferase (LCAT) deficiency. Murano, S., Shirai, K., Saito, Y., Yoshida, S., Ohta, Y., Tsuchida, H., Yamamoto, S., Asano, G., Chen, C.H., Albers, J.J. Scand. J. Clin. Lab. Invest. (1987) [Pubmed]
  13. beta-dystrobrevin, a new member of the dystrophin family. Identification, cloning, and protein associations. Peters, M.F., O'Brien, K.F., Sadoulet-Puccio, H.M., Kunkel, L.M., Adams, M.E., Froehner, S.C. J. Biol. Chem. (1997) [Pubmed]
  14. The cell adhesion molecule retina cognin is a cell surface protein disulfide isomerase that uses disulfide exchange activity to modulate cell adhesion. Pariser, H.P., Zhang, J., Hausman, R.E. Exp. Cell Res. (2000) [Pubmed]
  15. Accumulation of high-density lipoprotein-derived estradiol-17beta fatty acid esters in low-density lipoprotein particles. Helisten, H., Höckerstedt, A., Wähälä, K., Tiitinen, A., Adlercreutz, H., Jauhiainen, M., Tikkanen, M.J. J. Clin. Endocrinol. Metab. (2001) [Pubmed]
  16. Selective carnitine palmitoyltransferase deficiency in fibroblasts from a patient with muscle CPT deficiency. Pula, T.P., Max, S.R., Zielke, H.R., Chacon, M., Baab, P., Gumbinas, M., Reed, W.D. Ann. Neurol. (1981) [Pubmed]
  17. The sulfonylurea-inhibited NADH oxidase activity of HeLa cell plasma membranes has properties of a protein disulfide-thiol oxidoreductase with protein disulfide-thiol interchange activity. Morré, D.J., Chueh, P.J., Lawler, J., Morré, D.M. J. Bioenerg. Biomembr. (1998) [Pubmed]
  18. Differential modulation of the uptake currents by redox interconversion of cysteine residues in the human neuronal glutamate transporter EAAC1. Trotti, D., Nussberger, S., Volterra, A., Hediger, M.A. Eur. J. Neurosci. (1997) [Pubmed]
  19. Antioxidant properties of cystic fibrosis sputum. Dauletbaev, N., Rickmann, J., Viel, K., Diegel, H., von Mallinckrodt, C., Stein, J., Wagner, T.O., Bargon, J. Am. J. Physiol. Lung Cell Mol. Physiol. (2005) [Pubmed]
  20. Interconversion between apolipoprotein A-I-containing lipoproteins of pre-beta and alpha electrophoretic mobilities. Kunitake, S.T., Mendel, C.M., Hennessy, L.K. J. Lipid Res. (1992) [Pubmed]
  21. The role of Thr5 in human neuron growth inhibitory factor. Cai, B., Zheng, Q., Teng, X.C., Chen, D., Wang, Y., Wang, K.Q., Zhou, G.M., Xie, Y., Zhang, M.J., Sun, H.Z., Huang, Z.X. J. Biol. Inorg. Chem. (2006) [Pubmed]
  22. Reactivity of cysteine-67 of the human immunodeficiency virus-1 protease: studies on a peptide spanning residues 59 to 75. D'Ettorre, C., Levine, R.L. Arch. Biochem. Biophys. (1994) [Pubmed]
  23. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix. Fuentes-Mera, L., Rodríguez-Muñoz, R., González-Ramírez, R., García-Sierra, F., González, E., Mornet, D., Cisneros, B. Exp. Cell Res. (2006) [Pubmed]
  24. A high-sensitivity, single-gel, polyacrylamide gel electrophoresis method for the quantitative determination of glutathione reductases. Ye, B., Gitler, C., Gressel, J. Anal. Biochem. (1997) [Pubmed]
  25. Inhibitory effects of oxidants on n-type K+ channels in T lymphocytes and Xenopus oocytes. Szabó, I., Nilius, B., Zhang, X., Busch, A.E., Gulbins, E., Suessbrich, H., Lang, F. Pflugers Arch. (1997) [Pubmed]
  26. Reversible inhibition of human thioredoxin reductase activity by cytotoxic alkyl 2-imidazolyl disulfide analogues. Oblong, J.E., Chantler, E.L., Gallegos, A., Kirkpatrick, D.L., Chen, T., Marshall, N., Powis, G. Cancer Chemother. Pharmacol. (1994) [Pubmed]
  27. Modifications of the binding properties of the human VIP receptor of IGR39 cells by sulfhydryl reagents. Fouchier, F., Forget, P., Pic, P., Marvaldi, J., Pichon, J. Eur. J. Cell Biol. (1992) [Pubmed]
  28. Four conserved cysteine residues are required for the DNA binding activity of nuclear factor I. Novak, A., Goyal, N., Gronostajski, R.M. J. Biol. Chem. (1992) [Pubmed]
  29. The effect of the EAAEAE insert on the property of human metallothionein-3. Zheng, Q., Yang, W.M., Yu, W.H., Cai, B., Teng, X.C., Xie, Y., Sun, H.Z., Zhang, M.J., Huang, Z.X. Protein Eng. (2003) [Pubmed]
  30. A method for measuring disulfide reduction by cultured mammalian cells: relative contributions of glutathione-dependent and glutathione-independent mechanisms. Biaglow, J.E., Donahue, J., Tuttle, S., Held, K., Chrestensen, C., Mieyal, J. Anal. Biochem. (2000) [Pubmed]
  31. Glutathione content of human skin carcinomas. Engin, A. Archives for dermatological research. Archiv für dermatologische Forschung. (1976) [Pubmed]
  32. Relationships between muscle carnitine, age and oxidative status. Starling, R.D., Costill, D.L., Fink, W.J. European journal of applied physiology and occupational physiology. (1995) [Pubmed]
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