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Chemical Compound Review

KST-1B8679     1-[8-(2,5-dioxopyrrolidin-1- yl)-8-oxo...

Synonyms: AC1L3FZZ, AC1Q6KYZ, CTK8D7540, AR-1B3383, AC1Q5H8E, ...
 
 
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Disease relevance of Disuccinimidyl suberate

  • The affinity cross-linking of the delta-opioid receptor in neuroblastoma x glioma NG108-15 cells was undertaken using (3-[125I]iodotyrosyl27)human-beta-endorphin ([125I]beta-endorphin) and disuccinimidyl suberate (DSS) or bis(sulfosuccinimidyl) suberate (BS3) in order to estimate molecular size [1].
 

High impact information on Disuccinimidyl suberate

  • Erythropoietin bound to the surface of infected Sf9 cells could be cross-linked to two proteins with molecular masses of 90 and 65 kD using the homobifunctional cross-linker, disuccinimidyl suberate (DSS) [2].
  • The structure of the insulin receptor in intact human erythrocytes was defined using the techniques of disuccinimidyl suberate (DSS) cross-linking of 125I-insulin and surface [125I]iodination followed by receptor immunoprecipitation [3].
  • 125I-labeled vasoactive intestinal polypeptide (125I-VIP) was covalently cross-linked with its binding sites on intact cultured human lymphoblasts by each of three bifunctional reagents: disuccinimidyl suberate (DSS), ethylene glycol bis(succinimidyl succinate) (EGS), and N-succinimidyl 6-(4'-azido-2'-nitrophenylamino) hexanoate (SANAH) [4].
  • Using a similar DSS cross-linking technique, we identified Sm-C-binding proteins in second trimester amniotic fluid [apparent molecular mass (Mr), 38,000 and 35,000] and term cord plasma (Mr, 41,000, 38,000, and 35,000) [5].
  • Chemical cross-linking of [125I]endothelin to rat brain membranes by using the cross-linking reagent disuccinimidyl suberate (DSS) revealed two specific proteins of Mr = 52,000 and Mr = 30,000 [6].
 

Anatomical context of Disuccinimidyl suberate

  • Disuccinimidyl-suberate cross-linking of receptor-bound 125I-TNF-alpha and SDS-PAGE of membrane preparations of either U937 or K562 cells suggest a single receptor protein with an apparent molecular weight of 76 kDa [7].
  • Finally, the 135 Kd radioactive band was specially visualized in the affinity labeling of bovine adrenal cortex with disuccinimidyl suberate (DSS) [8].
  • In the present study, we examined the binding sites of the inhibitor on the mitochondrial membrane using chemical cross-linkers, disuccinimidyl suberate (DSS) and N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ) [9].
  • Covalent attachment of [32P]HuIFN-gamma to placental plasma membranes via DSS produced 2 crosslinked complexes with the molecular sizes of 100-120 kD and 60-70 kD [10].
 

Associations of Disuccinimidyl suberate with other chemical compounds

  • BSA was modified with lysine specific cross-linkers, bis(sulfosuccinimidyl) suberate (BS(3)), disuccinimidyl suberate (DSS) or disuccinimidyl glutarate (DSG), digested with trypsin and analyzed by tandem mass spectrometry [11].
  • 125I-labeled human somatotropin specifically bound to the lactogenic sites of microsomal membranes from pregnant rat liver, originated a radioactive covalent complex of Mr 63,000 upon reaction with dimethyl suberimidate, disuccinimidyl suberate (DSS) and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide [12].
 

Gene context of Disuccinimidyl suberate

  • An 18 mer (MORF18) was made bivalent by dimerizing both with disuccinimidyl suberate (DSS) and disuccinimidyl glutarate (DSG) linkers [13].
  • When [125I]mIL-3 was cross-linked to receptor sites on the surfaces of intact B6SUtA1 cells with disuccinimidyl suberate (DSS), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed the existence of two radiolabeled species with molecular weights of 140 (p140) and 70 (p70) kd (after subtraction of [125I]mIL-3) [14].
  • When [32P]HuIFN-gamma was bound and crosslinked to IFN-gamma the receptor of human cells with a bifunctional crosslinker disuccinimidyl suberate (DSS), a single diffused 32P-labeled band corresponding to the IFN-gamma.receptor complex was visualized by SDS-polyacrylamide gel electrophoresis and autoradiography [10].
  • The reactivity order obtained in that study (M1 approximate, equals K6 approximate, equals K48 approximate, equals K63) > K33 > K11 > (K27, K29), shows that the cross-link first formed in ubiquitin by reaction with DSS and DSG occurs between the most reactive residues [15].
  • In the present work, we have studied A beta-AChE interactions using the crosslinker reagent disuccinimidyl suberate (DSS), in the presence of [125I]-A beta peptide [16].
 

Analytical, diagnostic and therapeutic context of Disuccinimidyl suberate

  • Phosphorylated R-tau became resistant to DSS upon dephosphorylation and was recovered as a monomeric species from the gel filtration column [17].
  • 125I-insulin was crosslinked to its receptor using disuccinimidyl suberate (DSS), and the structure of the receptor complex was identified by SDS-polyacrylamide gel electrophoresis and autoradiography; a major band with Mr = 145,000 was identified, which corresponds to the alpha-subunit of the insulin receptor reported in other tissues [18].

References

  1. Affinity cross-linked delta-opioid receptor in NG108-15 cells is low molecular weight (25 kDa) and coupled to GTP-binding proteins. Harada, J., Ueda, H., Iso, Y., Satoh, M. Eur. J. Pharmacol. (1992) [Pubmed]
  2. Isolation of the full-length murine erythropoietin receptor using a baculovirus expression system. Spivak, J.L., Avedissian, L.S., Pierce, J.H., Williams, D., Hankins, W.D., Jensen, R.A. Blood (1996) [Pubmed]
  3. Structure of the human erythrocyte insulin receptor. Ward, G.M., Harrison, L.C. Diabetes (1986) [Pubmed]
  4. Covalent cross-linking of vasoactive intestinal polypeptide to its receptors on intact human lymphoblasts. Wood, C.L., O'Dorisio, M.S. J. Biol. Chem. (1985) [Pubmed]
  5. Affinity-labeled somatomedin-C receptors and binding proteins from the human fetus. Grizzard, J.D., D'Ercole, A.J., Wilkins, J.R., Moats-Staats, B.M., Williams, R.W. J. Clin. Endocrinol. Metab. (1984) [Pubmed]
  6. Identification of endothelin receptors by chemical cross-linking. Schvartz, I., Ittoop, O., Hazum, E. Endocrinology (1990) [Pubmed]
  7. Quantification and characterization of high-affinity membrane receptors for tumor necrosis factor on human leukemic cell lines. Scheurich, P., Ucer, U., Krönke, M., Pfizenmaier, K. Int. J. Cancer (1986) [Pubmed]
  8. Porcine brain natriuretic peptide receptor in bovine adrenal cortex. Higuchi, K., Hashiguchi, T., Ohashi, M., Takayanagi, R., Haji, M., Matsuo, H., Nawata, H. Life Sci. (1989) [Pubmed]
  9. A yeast mitochondrial ATPase inhibitor interacts with three proteins that are easy to dissociate from the mitochondrial inner membrane. Ichikawa, N., Nakabayashi, K., Hashimoto, T. J. Biochem. (2002) [Pubmed]
  10. Immune interferon receptor: chemical and enzymatic sensitivity. Rashidbaigi, A., Stefanos, S., Jung, V., Langer, J.A. J. Interferon Res. (1988) [Pubmed]
  11. Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. Huang, B.X., Kim, H.Y., Dass, C. J. Am. Soc. Mass Spectrom. (2004) [Pubmed]
  12. Specificity of covalently stabilized complexes of 125I-labeled human somatotropin and components of the lactogenic binding sites of rat liver. Caamaño, C.A., Fernandez, H.N., Paladini, A.C. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  13. Affinity enhancement bivalent morpholinos for pretargeting: surface plasmon resonance studies of molecular dimensions. He, J., Liu, X., Zhang, S., Liu, G., Hnatowich, D.J. Bioconjug. Chem. (2005) [Pubmed]
  14. Characterization of the interleukin 3 receptor. Murthy, S.C., Mui, A.L., Krystal, G. Exp. Hematol. (1990) [Pubmed]
  15. A top-down approach to protein structure studies using chemical cross-linking and Fourier transform mass spectrometry. Novak, P., Young, M.M., Schoeniger, J.S., Kruppa, G.H. European journal of mass spectrometry (Chichester, England) (2003) [Pubmed]
  16. Crosslinking of amyloid-beta peptide to brain acetylcholinesterase. Opazo, C., Inestrosa, N.C. Mol. Chem. Neuropathol. (1998) [Pubmed]
  17. Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro. Paudel, H.K. J. Biol. Chem. (1997) [Pubmed]
  18. Processing of insulin by bovine endothelial cells in culture. Internalization without degradation. Jialal, I., King, G.L., Buchwald, S., Kahn, C.R., Crettaz, M. Diabetes (1984) [Pubmed]
 
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