Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-2-14
pubmed:abstractText
In plants, sugars are the main respiratory substrates and important signaling molecules in the regulation of carbon metabolism. Sugar signaling studies suggested that sugar sensing involves several key components, among them hexokinase (HXK). Although the sensing mechanism of HXK is unknown, several experiments support the hypothesis that hexose phosphorylation is a determining factor. Glucose (Glc) analogs transported into cells but not phosphorylated are frequently used to test this hypothesis, among them 3-O-methyl-Glc (3-OMG). The aim of the present work was to investigate the effects and fate of 3-OMG in heterotrophic plant cells. Measurements of respiration rates, protein and metabolite contents, and protease activities and amounts showed that 3-OMG is not a respiratory substrate and does not contribute to biosynthesis. Proteolysis and lipolysis are induced in 3-OMG-fed maize (Zea mays L. cv DEA) roots in the same way as in sugar-starved organs. However, contrary to the generally accepted idea, phosphorous and carbon nuclear magnetic resonance experiments and enzymatic assays prove that 3-OMG is phosphorylated to 3-OMG-6-phosphate, which accumulates in the cells. Insofar as plant HXK is involved in sugar sensing, these findings are discussed on the basis of the kinetic properties because the catalytic efficiency of HXK isolated from maize root tips is five orders of magnitude lower for 3-OMG than for Glc and Man.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10087931, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10217505, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10493925, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10508760, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10557216, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-10656404, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-11080291, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-11161045, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-11244127, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-11432937, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-11788774, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-13373862, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-1368, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-16656877, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-16661466, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-16667770, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-16668231, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-1889412, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-3005285, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-3031035, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-3888622, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-3956737, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-6712659, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-7619043, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-7632917, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-7784506, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-7827498, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-8252064, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-8947499, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-9025302, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-942051, http://linkedlifedata.com/resource/pubmed/commentcorrection/12586906-9737962
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
824-37
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed-meshheading:12586906-3-O-Methylglucose, pubmed-meshheading:12586906-Arabidopsis, pubmed-meshheading:12586906-Carbohydrate Metabolism, pubmed-meshheading:12586906-Carbon, pubmed-meshheading:12586906-Carbon Isotopes, pubmed-meshheading:12586906-Cell Respiration, pubmed-meshheading:12586906-Endopeptidases, pubmed-meshheading:12586906-Glucose-6-Phosphate, pubmed-meshheading:12586906-Hexokinase, pubmed-meshheading:12586906-Kinetics, pubmed-meshheading:12586906-Lycopersicon esculentum, pubmed-meshheading:12586906-Magnetic Resonance Spectroscopy, pubmed-meshheading:12586906-Peptide Hydrolases, pubmed-meshheading:12586906-Phosphorus Isotopes, pubmed-meshheading:12586906-Phosphorylation, pubmed-meshheading:12586906-Plant Proteins, pubmed-meshheading:12586906-Plant Roots, pubmed-meshheading:12586906-Plants, pubmed-meshheading:12586906-Signal Transduction, pubmed-meshheading:12586906-Zea mays
pubmed:year
2003
pubmed:articleTitle
In plants, 3-o-methylglucose is phosphorylated by hexokinase but not perceived as a sugar.
pubmed:affiliation
Commissariat à l'Energie Atomique, Centre National de la Recherche Scientifique, Université Joseph Fourier, Unité Mixte de Recherche 5019 Physiologie Cellulaire Végétale, 17 rue des Martyrs, 38054 Grenoble cedex 9, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't