Linked Life Data

16230332

Source:http://linkedlifedata.com/resource/pubmed/id/16230332

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2005-12-29
pubmed:abstractText
During starch degradation, chloroplasts export neutral sugars into the cytosol where they appear to enter a complex glycan metabolism. Interactions between glycans and glucosyl transferases residing in the cytosol were studied by analyzing transgenic potato (Solanum tuberosum L.) plants that possess either decreased or elevated levels of the cytosolic (Pho 2) phosphorylase isoform. Water-soluble heteroglycans (SHGs) were isolated from these plants and were characterized. SHG contains, as major constituents, arabinose, rhamnose, galactose and glucose. Non-aqueous fractionation combined with other separation techniques revealed a distinct pool of the SHG that is located in the cytosol. Under in vitro conditions, the cytosolic heteroglycans act as glucosyl acceptor selectively for Pho 2. Acceptor sites were characterized by a specific hydrolytic degradation following the Pho 2-catalyzed glucosyl transfer. The size distribution of the cytosolic SHG increased during the dark period, indicating a distinct metabolic activity related to net starch degradation. Antisense inhibition of Pho 2 resulted in increased glucosyl and rhamnosyl contents of the glycans. Overexpression of Pho 2 decreased the content of both residues. Compared with the wild type, in both types of transgenic plants the size of the cytosolic glycans was increased.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0032-0781
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1987-2004
pubmed:dateRevised
2010-5-12
pubmed:meshHeading
pubmed-meshheading:16230332-Adaptation, Physiological, pubmed-meshheading:16230332-Arabinose, pubmed-meshheading:16230332-Blotting, Northern, pubmed-meshheading:16230332-Carbohydrate Conformation, pubmed-meshheading:16230332-Cytosol, pubmed-meshheading:16230332-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16230332-Galactose, pubmed-meshheading:16230332-Gene Expression Regulation, Plant, pubmed-meshheading:16230332-Glucose, pubmed-meshheading:16230332-Glycoside Hydrolases, pubmed-meshheading:16230332-Immunohistochemistry, pubmed-meshheading:16230332-Isoenzymes, pubmed-meshheading:16230332-Phosphorylases, pubmed-meshheading:16230332-Plant Leaves, pubmed-meshheading:16230332-Plants, Genetically Modified, pubmed-meshheading:16230332-Polysaccharides, pubmed-meshheading:16230332-Rhamnose, pubmed-meshheading:16230332-Solanum tuberosum, pubmed-meshheading:16230332-Substrate Specificity
pubmed:year
2005
pubmed:articleTitle
Analysis of cytosolic heteroglycans from leaves of transgenic potato (Solanum tuberosum L.) plants that under- or overexpress the Pho 2 phosphorylase isozyme.
pubmed:affiliation
Department of Plant Physiology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, Building 20, D-14476 Potsdam-Golm, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't