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Chemical Compound Review

glutamin     2-amino-4-aminocarbonyl- butanoic acid

Synonyms: Hgln, L-Glutamid, DL-Glutamine, H-DL-Gln-OH, DL Glutamine, ...
 
 
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Disease relevance of proglumide

 

Psychiatry related information on proglumide

 

High impact information on proglumide

  • Notably, tTG can also cross-link glutamine residues of peptides to lysine residues in other proteins including tTG itself [10].
  • For example, if tumors are preferential glutamine utilizers, then TPN-enriched solutions might be employed to increase the number of cells in a phase of mitosis that makes them more susceptible to attack by cell-cycle specific chemotherapeutic agents [11].
  • Similarly, overexpression of wild-type and glutamine-expanded hAtx-1 reduces Gfi-1 levels in Purkinje cells [2].
  • Upon cell binding and introduction into the cytosol, CNF1 deamidates glutamine 63 of RhoA (or 61 of Rac and Cdc42), rendering constitutively active these GTPases [12].
  • We find that the Gln/Asn-rich prion domains of two proteins, New1p and Rnq1p, can control susceptibility to [PSI(+)] induction as well as enhance aggregation of a human glutamine expansion disease protein [13].
 

Chemical compound and disease context of proglumide

 

Biological context of proglumide

 

Anatomical context of proglumide

  • Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial [23]?
  • To test directly whether the glutamine-rich region is required for Sry function in vivo, we created truncation mutations of the Mus musculus musculus Sry gene and tested their ability to induce testis formation in XX embryos using a transgenic mouse assay [19].
  • The single-channel conductance properties of these AChR mutants expressed in Xenopus laevis oocytes indicate that three clusters of negatively charged and glutamine residues neighbouring segment M2 of the alpha-, beta-, gamma- and delta-subunits, probably forming three anionic rings, are major determinants of the rate of ion transport [24].
  • Here we describe the isolation of glycyl glutamine from porcine pituitary and present evidence for its presence in sheep brain stem [25].
  • Therefore, the requirement for glutamine in protein synthesis in these cells and organelles is provided by the conversion of glutamate attached to an 'incorrectly' charged tRNA [26].
 

Associations of proglumide with other chemical compounds

  • In addition, the effect of factor XIII was shown to require covalent crossliking of CIG to the fibrinogen or fibrin, which involved a glutamine residue on the CIG molecule and could be prevented by prior crosslinking of CIG with putrescine or with itself [27].
  • To identify those amino acid residues that interact with permeating ions, we have introduced various point mutations into the Torpedo AChR subunit cDNAs to alter the net charge of the charged or glutamine residues around the proposed transmembrane segments [24].
  • This conversion is an unusual form of protein modification in that it requires catalysis by an intramolecular reaction where both the substrate (asparagine and glutamine side chains) and "catalytic site" (the peptide nitrogen of the succeeding residue) are constituents of several consecutive residues along the polypeptide chain [28].
  • Intravenous and iontophoretic proglumide administration consistently blocked cholecystokinin-induced excitations while having no effect on glutamic acid-induced increases in activity [29].
  • The NH2-terminus of HRR25 contains the hallmark features of protein kinases, whereas the COOH-terminus is rich in proline and glutamine [30].
 

Gene context of proglumide

  • In both Drosophila cells and yeast, TAF110 specifically interacts with the glutamine-rich activation domains of Sp1 [31].
  • SCA1 belongs to a growing group of neurodegenerative disorders caused by expansion of CAG repeats, which encode glutamine [32].
  • The longest cDNA insert encodes a polypeptide of 169 amino acids, containing unique repeats of a CAG sequence which would encode 12 consecutive glutamine residues within the active IL-2 molecule [33].
  • In each of five affected males, a point mutation was identified in the eighth exon of the MAOA structural gene, which changes a glutamine to a termination codon [34].
  • The PDE1B structure shows that in dual-specific PDEs a key histidine residue may enable the invariant glutamine to toggle between cAMP and cGMP [35].
 

Analytical, diagnostic and therapeutic context of proglumide

References

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  2. The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins. Tsuda, H., Jafar-Nejad, H., Patel, A.J., Sun, Y., Chen, H.K., Rose, M.F., Venken, K.J., Botas, J., Orr, H.T., Bellen, H.J., Zoghbi, H.Y. Cell (2005) [Pubmed]
  3. Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA. Wray, L.V., Zalieckas, J.M., Fisher, S.H. Cell (2001) [Pubmed]
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  8. Noncirrhotic portal vein thrombosis exhibits neuropsychological and MR changes consistent with minimal hepatic encephalopathy. Mínguez, B., García-Pagán, J.C., Bosch, J., Turnes, J., Alonso, J., Rovira, A., Córdoba, J. Hepatology (2006) [Pubmed]
  9. Pentagastrin induced motility pattern in the human upper gastrointestinal tract is reversed by proglumide. Erckenbrecht, J.F., Caspari, J., Wienbeck, M. Gut (1984) [Pubmed]
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  12. CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion. Doye, A., Mettouchi, A., Bossis, G., Clément, R., Buisson-Touati, C., Flatau, G., Gagnoux, L., Piechaczyk, M., Boquet, P., Lemichez, E. Cell (2002) [Pubmed]
  13. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Osherovich, L.Z., Weissman, J.S. Cell (2001) [Pubmed]
  14. Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4. Bentley, A.K., Rees, D.J., Rizza, C., Brownlee, G.G. Cell (1986) [Pubmed]
  15. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Megee, P.C., Morgan, B.A., Mittman, B.A., Smith, M.M. Science (1990) [Pubmed]
  16. Astrocytic control of glutamatergic activity: astrocytes as stars of the show. Hertz, L., Zielke, H.R. Trends Neurosci. (2004) [Pubmed]
  17. A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Nakanishi, N., Shneider, N.A., Axel, R. Neuron (1990) [Pubmed]
  18. Glucose-derived osmolytes and energy impairment in brain edema accompanying liver failure: the role of glutamine reevaluated. Albrecht, J. Gastroenterology (2003) [Pubmed]
  19. Sry requires a CAG repeat domain for male sex determination in Mus musculus. Bowles, J., Cooper, L., Berkman, J., Koopman, P. Nat. Genet. (1999) [Pubmed]
  20. A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Geisterfer-Lowrance, A.A., Kass, S., Tanigawa, G., Vosberg, H.P., McKenna, W., Seidman, C.E., Seidman, J.G. Cell (1990) [Pubmed]
  21. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel. Zhuchenko, O., Bailey, J., Bonnen, P., Ashizawa, T., Stockton, D.W., Amos, C., Dobyns, W.B., Subramony, S.H., Zoghbi, H.Y., Lee, C.C. Nat. Genet. (1997) [Pubmed]
  22. Novel subunit-subunit interactions in the structure of glutamine synthetase. Almassy, R.J., Janson, C.A., Hamlin, R., Xuong, N.H., Eisenberg, D. Nature (1986) [Pubmed]
  23. Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? Sisodia, S.S. Cell (1998) [Pubmed]
  24. Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance. Imoto, K., Busch, C., Sakmann, B., Mishina, M., Konno, T., Nakai, J., Bujo, H., Mori, Y., Fukuda, K., Numa, S. Nature (1988) [Pubmed]
  25. Glycyl glutamine, an inhibitory neuropeptide derived from beta-endorphin. Parish, D.C., Smyth, D.G., Normanton, J.R., Wolstencroft, J.H. Nature (1983) [Pubmed]
  26. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Schön, A., Kannangara, C.G., Gough, S., Söll, D. Nature (1988) [Pubmed]
  27. Fibroblast adhesion to fibrinogen and fibrin substrata: requirement for cold-insoluble globulin (plasma fibronectin). Grinnell, F., Feld, M., Minter, D. Cell (1980) [Pubmed]
  28. Tertiary structure is a principal determinant to protein deamidation. Kossiakoff, A.A. Science (1988) [Pubmed]
  29. Proglumide: selective antagonism of excitatory effects of cholecystokinin in central nervous system. Chiodo, L.A., Bunney, B.S. Science (1983) [Pubmed]
  30. HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA. Hoekstra, M.F., Liskay, R.M., Ou, A.C., DeMaggio, A.J., Burbee, D.G., Heffron, F. Science (1991) [Pubmed]
  31. Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. Hoey, T., Weinzierl, R.O., Gill, G., Chen, J.L., Dynlacht, B.D., Tjian, R. Cell (1993) [Pubmed]
  32. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Matilla, A., Koshy, B.T., Cummings, C.J., Isobe, T., Orr, H.T., Zoghbi, H.Y. Nature (1997) [Pubmed]
  33. Unique structure of murine interleukin-2 as deduced from cloned cDNAs. Kashima, N., Nishi-Takaoka, C., Fujita, T., Taki, S., Yamada, G., Hamuro, J., Taniguchi, T. Nature (1985) [Pubmed]
  34. Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Brunner, H.G., Nelen, M., Breakefield, X.O., Ropers, H.H., van Oost, B.A. Science (1993) [Pubmed]
  35. A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Zhang, K.Y., Card, G.L., Suzuki, Y., Artis, D.R., Fong, D., Gillette, S., Hsieh, D., Neiman, J., West, B.L., Zhang, C., Milburn, M.V., Kim, S.H., Schlessinger, J., Bollag, G. Mol. Cell (2004) [Pubmed]
  36. Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis. Clarke, A.R., Wigley, D.B., Chia, W.N., Barstow, D., Atkinson, T., Holbrook, J.J. Nature (1986) [Pubmed]
  37. Potentiation of opiate analgesia and apparent reversal of morphine tolerance by proglumide. Watkins, L.R., Kinscheck, I.B., Mayer, D.J. Science (1984) [Pubmed]
  38. The Aspergillus nidulans fluG gene is required for production of an extracellular developmental signal and is related to prokaryotic glutamine synthetase I. Lee, B.N., Adams, T.H. Genes Dev. (1994) [Pubmed]
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