Protein Glycation in Plants-An Under-Researched Field with Much Still to Discover.

作者: Naila Rabbani , Maryam Al-Motawa , Paul J. Thornalley

DOI: 10.3390/IJMS21113942

关键词:

摘要: Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with potential contributory role to the functional impairment plant proteome. Reducing sugars free aldehyde or ketone group such glucose, fructose and galactose react N-terminal lysine side chain amino groups proteins. A common early-stage adduct formed from glucose is Ne-fructosyl-lysine (FL). Saccharide-derived reactive dicarbonyls are arginine residue-directed glycating agents, forming advanced endproducts (AGEs). dominant dicarbonyl methylglyoxal-formed mainly by trace-level degradation triosephosphates, including through Calvin cycle photosynthesis. Methylglyoxal forms major quantitative AGE, hydroimidazolone MG-H1. Glucose methylglyoxal concentrations change developmental stage, senescence, light dark cycles also likely biotic abiotic stresses. Proteomics analysis indicates that there an enrichment acid residue targets glycation, residues, predicted sites proteome, suggesting susceptibility inactivation glycation. In this review, we give brief introduction agents adducts plants. We consider stress, vulnerability proteome arginine-directed methylglyoxal-mediated activation unfolded protein response The latter linked recent suggestion sugar signaling metabolism. overexpression glyoxalase 1, which suppresses glyoxal, produced resistant high salinity, drought, extreme temperature other Further decrease may lead improved growth assist breeding varieties environmental stress senescence-including commercial ornamental crop cultivation value.

参考文章(79)
Susan A. PHILLIPS, Paul J. THORNALLEY, The formation of methylglyoxal from triose phosphates FEBS Journal. ,vol. 212, pp. 101- 105 ,(1993) , 10.1111/J.1432-1033.1993.TB17638.X
Naila Rabbani, Paul J. Thornalley, Dicarbonyls (Glyoxal, Methylglyoxal, and 3-Deoxyglucosone) Uremic Toxins. pp. 177- 192 ,(2012) , 10.1002/9781118424032.CH12
M U Ahmed, S R Thorpe, J W Baynes, Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. Journal of Biological Chemistry. ,vol. 261, pp. 4889- 4894 ,(1986) , 10.1016/S0021-9258(19)89188-3
Michael Morcos, Xueliang Du, Friederike Pfisterer, Harald Hutter, Ahmed AR Sayed, Paul Thornalley, Naila Ahmed, John Baynes, Suzanne Thorpe, Georgi Kukudov, Andreas Schlotterer, Farastuk Bozorgmehr, Randa Abd El Baki, David Stern, Frank Moehrlen, Youssef Ibrahim, Dimitrios Oikonomou, Andreas Hamann, Christian Becker, Martin Zeier, Vedat Schwenger, Nexhat Miftari, Per Humpert, Hans‐Peter Hammes, Markus Buechler, Angelika Bierhaus, Michael Brownlee, Peter P Nawroth, None, Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans. Aging Cell. ,vol. 7, pp. 260- 269 ,(2008) , 10.1111/J.1474-9726.2008.00371.X
Michael P. Murphy, Arne Holmgren, Nils-Göran Larsson, Barry Halliwell, Christopher J. Chang, Balaraman Kalyanaraman, Sue Goo Rhee, Paul J. Thornalley, Linda Partridge, David Gems, Thomas Nyström, Vsevolod Belousov, Paul T. Schumacker, Christine C. Winterbourn, Unraveling the biological roles of reactive oxygen species. Cell Metabolism. ,vol. 13, pp. 361- 366 ,(2011) , 10.1016/J.CMET.2011.03.010
G. Delpierre, M. H. Rider, F. Collard, V. Stroobant, F. Vanstapel, H. Santos, E. Van Schaftingen, Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes. ,vol. 49, pp. 1627- 1634 ,(2000) , 10.2337/DIABETES.49.10.1627
Charanpreet Kaur, Sneh L. Singla-Pareek, Sudhir K. Sopory, Glyoxalase and methylglyoxal as biomarkers for plant stress tolerance. Critical Reviews in Plant Sciences. ,vol. 33, pp. 429- 456 ,(2014) , 10.1080/07352689.2014.904147