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Chemical Compound Review

EGATA     2-[2-[2-[2- (bis(carboxymethyl)amino) ethoxy...

Synonyms: Gedta, EGTA, Magnesium-EGTA, Egtazic acid, Tetrasodium EGTA, ...
 
 
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Disease relevance of Egtazic acid

 

High impact information on Egtazic acid

  • When rat skeletal muscle cells were treated with EGTA, an inhibitor of cell fusion, a battery of muscle-specific mRNAs was synthesized but not translated despite the synthesis of many other proteins [6].
  • Three types of muscle-specific gene expression in fusion-blocked rat skeletal muscle cells: translational control in EGTA-treated cells [6].
  • The anti-L3T4-insensitive increase in [Ca2+]i induced by Con A was inhibited by EGTA, suggesting that this mitogen also stimulated an influx of Ca2+ via an additional transport mechanism distinct from that stimulated by antigen [7].
  • Most of the muscle-specific mRNAs were associated with polysomes in fused myotubes, whereas they were found in postpolysomal fractions in EGTA-treated cells [6].
  • Also, EGTA attenuates the usual inhibition of EGF binding caused by phorbol esters [8].
 

Chemical compound and disease context of Egtazic acid

  • Calcium displaceable by lanthanum or EGTA appears to contribute to Nao-free or Nao- and Cao-free contracture [9].
  • Nramp2, but not Nramp1, was found to complement hypersensitivity to EGTA of the smf1/smf2 mutant under oxidative stress conditions (methyl viologen) [10].
  • Proteolysis of the receptor could be blocked by preparing the cytosol in the presence of EGTA, leupeptin, or a heat-stable factor present in the cytosol of rat liver and WEHI-7 mouse thymoma cells [11].
  • Viral penetration was tested in the presence of H7 (protein kinase C inhibition), EGTA (extracellular Ca2+ chelation), cyclosporine A (inhibition of Ca2+/calmodulin-dependent activation), or pertussis toxin (inhibition of G protein function) [12].
  • Moreover, LPA-induced increases in Ca2+ transients and/or iNOS expression in highly purified rat liver nuclei were prevented by pertussis toxin, phosphoinositide 3-kinase/Akt inhibitor wortmannin and Ca2+ chelator and channel blockers EGTA and SK&F96365, respectively [13].
 

Biological context of Egtazic acid

  • Intracellular injections of EGTA block induction of hippocampal long-term potentiation [14].
  • Maximum phosphorylation occurred after incubation for 1 min and was inhibited by the addition of either yohimbine, prostaglandin E1, or EGTA [15].
  • These changes were accompanied by a progressive increase in cytosolic [Ca2+]i. In patch-clamped myocytes dialyzed internally with high EGTA concentrations, LPC caused membrane depolarization, shortening of the action potential duration, and abnormal automaticity as seen in multicellular preparations [16].
  • Intracellular Ca2+ buffers with rapid binding kinetics, dimethyl BAPTA and BAPTA, prevented the effect of ChTx, but EGTA, a Ca2+ buffer with similar affinity for Ca2+ but slower binding kinetics, did not [17].
  • Parallel second messengers did not contribute to GnRH-induced exocytosis, because IP3 alone was as effective as GnRH, and because even GnRH failed to trigger rapid exocytosis when the [Ca2+]i rise was blunted by EGTA [18].
 

Anatomical context of Egtazic acid

  • Preventing calcium entry with EGTA or enhancing intracellular calcium with A23187 in intact cells modulates EGF receptor affinity in membranes isolated subsequently [8].
  • These conclusions are based on measurements of exocytotic secretion from permeabilized neutrophils into which we have been able to introduce, individually and in combination, Ca2+ chelators (EGTA and BAPTA), Ca2+ (buffered at micromolar concentrations with EGTA), analogues of GTP and GDP and the direct activator of protein kinase C, PMA [19].
  • Are cardiac muscle cells skinned by EGTA or EDTA [20]?
  • EGTA and proteinase reversal of cellular aggregation of activated lymphocytes [21].
  • In the presence of EGTA, gelsolin has no effect on the movement of membranous organelles, but in the presence of 10 microM Ca2+ it completely blocks transport of all membranous organelles [22].
 

Associations of Egtazic acid with other chemical compounds

  • We have developed an immunoadsorption technique for quantitating EGTA-resistant gelsolin/actin complexes in macrophages extracted with Triton X-100 [23].
  • Histidine, a strong chelator of divalent cations other than calcium and magnesium, had no effect on monocyte superoxide production or on ionized calcium concentrations, indicating that EGTA inhibition was due to cell calcium depletion [24].
  • Bovine parathyroid hormone stimulated the 1- and reduced the 24-hydroxylase in 6 h, but this only occurred in cultures either previously treated with 1,25(OH)2D3 and EGTA to lower Ca to 0.8 mM or in cultures grown in the presence of 25-hydroxyvitamin D3 (25(OH)D3) [25].
  • Fusion to form hybrid organelles was inhibited by 1,2-bis(2-aminophenoxy) ethane-N,N,N',N'-tetraacetic acid (BAPTA), but not by EGTA, and this inhibition was reversed by adding additional Ca(2+) [26].
  • 8G5 IgG-Sepharose columns retained gelsolin (as GCa2) or brevin (as BCa2) in 0.1 mM CaCl2 containing buffers, but released these molecules when eluted with 4 mM EGTA [27].
 

Gene context of Egtazic acid

  • The role of extracellular Ca2+ in Fc gamma R(CD16)-dependent induction of lymphokine gene expression has been tested by evaluating production, mRNA accumulation and transcription of IFN-gamma and TNF in NK cells stimulated with Fc gamma R(CD16) ligands and/or rIL-2 in the presence of EGTA [28].
  • Third, Myo2p coimmunoprecipitates with calmodulin in the presence of Ca2+ or EGTA [29].
  • The calcium chelating agent EGTA also inhibits the IL-10 production induced by Nef, and this inhibition is reversed by the addition of calcium along with Nef [30].
  • This hydrolysis is inhibited by EGTA, and the calpain inhibitor I, N-acetyl-leu-leu-norleucinal, but not by several caspases inhibitors, suggesting that BARD1 is hydrolyzed by the calcium-dependent cysteine proteases, calpains [31].
  • The intracellular calcium chelator (EGTA/AM) further increased ERK activation by native and mildly modified LDL (P < 0.05) [32].
 

Analytical, diagnostic and therapeutic context of Egtazic acid

  • When solubilized mitochondrial proteins were subjected to calmodulin-Sepharose affinity chromatography and eluted with 1 mM EGTA, there were two major polypeptides 120,000 and 67,000 daltons and at least three minor species (100,000, 60,000 and 40,000 daltons) [33].
  • The antigen can be extracted from cells with isotonic buffers containing EGTA, binds to Concanavalin A, and when analyzed on SDS gels by immunoblotting, two major antigenic glycoproteins are detected at 57 kd (isoelectric point, 5.1) and at 44 kd (isoelectric point, 5.4) [34].
  • Microinjection of the Ca2+ buffer EGTA into presynaptic terminals had no effect on transmitter release or synaptic depression [35].
  • Removal of Ca2+ from cell culture medium by EGTA inhibited U937 cell-mediated peroxidation of LDL lipids [36].
  • Elution with 4 mM EGTA released material that gel filtration showed to be the EGTA-stable 130,000-mol-wt gelsolin-actin complex, GA1Ca1 [27].

References

  1. Absence of nucleosomes in a histone-containing nucleoprotein complex obtained by dissociation of purified SV40 virions. Moyne, G., Harper, F., Saragosti, S., Yaniv, M. Cell (1982) [Pubmed]
  2. Fractalkine and CX3CR1 mediate a novel mechanism of leukocyte capture, firm adhesion, and activation under physiologic flow. Fong, A.M., Robinson, L.A., Steeber, D.A., Tedder, T.F., Yoshie, O., Imai, T., Patel, D.D. J. Exp. Med. (1998) [Pubmed]
  3. Mechanism of inhibition of polypeptide chain initiation in calcium-depleted Ehrlich ascites tumor cells. Kumar, R.V., Wolfman, A., Panniers, R., Henshaw, E.C. J. Cell Biol. (1989) [Pubmed]
  4. Role of Ca++ in virus-induced membrane fusion. Ca++ accumulation and ultrastructural changes induced by Sendai virus in chicken erythrocytes. Volsky, D.J., Loyter, A. J. Cell Biol. (1978) [Pubmed]
  5. Agonist-induced myopathy at the neuromuscular junction is mediated by calcium. Leonard, J.P., Salpeter, M.M. J. Cell Biol. (1979) [Pubmed]
  6. Three types of muscle-specific gene expression in fusion-blocked rat skeletal muscle cells: translational control in EGTA-treated cells. Endo, T., Nadal-Ginard, B. Cell (1987) [Pubmed]
  7. The role of the L3T4 molecule in mitogen and antigen-activated signal transduction. Rosoff, P.M., Burakoff, S.J., Greenstein, J.L. Cell (1987) [Pubmed]
  8. EGF receptor affinity is regulated by intracellular calcium and protein kinase C. Fearn, J.C., King, A.C. Cell (1985) [Pubmed]
  9. Control of cytosolic calcium activity during low sodium exposure in cultured chick heart cells. Kim, D., Okada, A., Smith, T.W. Circ. Res. (1987) [Pubmed]
  10. Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family. Pinner, E., Gruenheid, S., Raymond, M., Gros, P. J. Biol. Chem. (1997) [Pubmed]
  11. Degradation without apparent change in size of molybdate-stabilized nonactivated glucocorticoid-receptor complexes in rat thymus cytosol. Mendel, D.B., Holbrook, N.J., Bodwell, J.E. J. Biol. Chem. (1985) [Pubmed]
  12. Penetration of CD4 T cells by HIV-1. The CD4 receptor does not internalize with HIV, and CD4-related signal transduction events are not required for entry. Orloff, G.M., Orloff, S.L., Kennedy, M.S., Maddon, P.J., McDougal, J.S. J. Immunol. (1991) [Pubmed]
  13. Modulation of pro-inflammatory gene expression by nuclear lysophosphatidic acid receptor type-1. Gobeil, F., Bernier, S.G., Vazquez-Tello, A., Brault, S., Beauchamp, M.H., Quiniou, C., Marrache, A.M., Checchin, D., Sennlaub, F., Hou, X., Nader, M., Bkaily, G., Ribeiro-da-Silva, A., Goetzl, E.J., Chemtob, S. J. Biol. Chem. (2003) [Pubmed]
  14. Intracellular injections of EGTA block induction of hippocampal long-term potentiation. Lynch, G., Larson, J., Kelso, S., Barrionuevo, G., Schottler, F. Nature (1983) [Pubmed]
  15. (-)-Adrenaline-induced, calcium-dependent phosphorylation of proteins in human platelets. Block, L.H., Jaksche, H., Erne, P., Bolli, P., Bühler, F.R. J. Clin. Invest. (1985) [Pubmed]
  16. Effects of lysophosphatidylcholine on electrophysiological properties and excitation-contraction coupling in isolated guinea pig ventricular myocytes. Liu, E., Goldhaber, J.I., Weiss, J.N. J. Clin. Invest. (1991) [Pubmed]
  17. Functional colocalization of calcium and calcium-gated potassium channels in control of transmitter release. Robitaille, R., Garcia, M.L., Kaczorowski, G.J., Charlton, M.P. Neuron (1993) [Pubmed]
  18. Local Ca2+ release from internal stores controls exocytosis in pituitary gonadotrophs. Tse, F.W., Tse, A., Hille, B., Horstmann, H., Almers, W. Neuron (1997) [Pubmed]
  19. Two roles for guanine nucleotides in the stimulus-secretion sequence of neutrophils. Barrowman, M.M., Cockcroft, S., Gomperts, B.D. Nature (1986) [Pubmed]
  20. Are cardiac muscle cells skinned by EGTA or EDTA? Winegrad, S. Nature (1979) [Pubmed]
  21. EGTA and proteinase reversal of cellular aggregation of activated lymphocytes. Neely, A.N., Sitzmann, J.V., Kersey, J.H. Nature (1976) [Pubmed]
  22. Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments. Brady, S.T., Lasek, R.J., Allen, R.D., Yin, H.L., Stossel, T.P. Nature (1984) [Pubmed]
  23. Reversibility of gelsolin/actin interaction in macrophages. Evidence of Ca2+-dependent and Ca2+-independent pathways. Chaponnier, C., Yin, H.L., Stossel, T.P. J. Exp. Med. (1987) [Pubmed]
  24. Relationship of superoxide production to cytoplasmic free calcium in human monocytes. Scully, S.P., Segel, G.B., Lichtman, M.A. J. Clin. Invest. (1986) [Pubmed]
  25. Regulation of the metabolism of 25-hydroxyvitamin D3 in primary cultures of chick kidney cells. Trechsel, U., Bonjour, J.P., Fleisch, H. J. Clin. Invest. (1979) [Pubmed]
  26. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. Pryor, P.R., Mullock, B.M., Bright, N.A., Gray, S.R., Luzio, J.P. J. Cell Biol. (2000) [Pubmed]
  27. Immuno-identification of Ca2+-induced conformational changes in human gelsolin and brevin. Hwo, S., Bryan, J. J. Cell Biol. (1986) [Pubmed]
  28. Fc gamma R(CD16) interaction with ligand induces Ca2+ mobilization and phosphoinositide turnover in human natural killer cells. Role of Ca2+ in Fc gamma R(CD16)-induced transcription and expression of lymphokine genes. Cassatella, M.A., Anegón, I., Cuturi, M.C., Griskey, P., Trinchieri, G., Perussia, B. J. Exp. Med. (1989) [Pubmed]
  29. The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. Brockerhoff, S.E., Stevens, R.C., Davis, T.N. J. Cell Biol. (1994) [Pubmed]
  30. Interleukin 10 is induced by recombinant HIV-1 Nef protein involving the calcium/calmodulin-dependent phosphodiesterase signal transduction pathway. Brigino, E., Haraguchi, S., Koutsonikolis, A., Cianciolo, G.J., Owens, U., Good, R.A., Day, N.K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  31. Identification of an apoptotic cleavage product of BARD1 as an autoantigen: a potential factor in the antitumoral response mediated by apoptotic bodies. Gautier, F., Irminger-Finger, I., Grégoire, M., Meflah, K., Harb, J. Cancer Res. (2000) [Pubmed]
  32. Native and modified LDL activate extracellular signal-regulated kinases in mesangial cells. Jenkins, A.J., Velarde, V., Klein, R.L., Joyce, K.C., Phillips, K.D., Mayfield, R.K., Lyons, T.J., Jaffa, A.A. Diabetes (2000) [Pubmed]
  33. The identification of calmodulin-binding sites on mitochondria in cultured 3T3 cells. Pardue, R.L., Kaetzel, M.A., Hahn, S.H., Brinkley, B.R., Dedman, J.R. Cell (1981) [Pubmed]
  34. Control of cell locomotion: perturbation with an antibody directed against specific glycoproteins. Goodman, S.L., Vollmers, H.P., Birchmeier, W. Cell (1985) [Pubmed]
  35. Role of residual calcium in synaptic depression and posttetanic potentiation: fast and slow calcium signaling in nerve terminals. Swandulla, D., Hans, M., Zipser, K., Augustine, G.J. Neuron (1991) [Pubmed]
  36. Dual Ca2+ requirement for optimal lipid peroxidation of low density lipoprotein by activated human monocytes. Li, Q., Tallant, A., Cathcart, M.K. J. Clin. Invest. (1993) [Pubmed]
 
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