Linked Life Data

3136158

Source:http://linkedlifedata.com/resource/pubmed/id/3136158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1988-9-16
pubmed:abstractText
[3H]Fucose, intravenously injected into androgen-treated mice, was incorporated at high rates into the immunopurified kidney lysosomal enzymes beta-glucuronidase and beta-galactosidase. Initially, label was incorporated into high molecular weight proenzyme forms. Processing of fucose-labeled proenzyme forms to lower molecular weight mature forms was very rapid, being detectable at 30 min, and complete by 90 min, compared with the several hours required for processing of lysosomal enzymes labeled with amino acids. This result is consistent with addition of fucose residues within the Golgi apparatus just before transfer of lysosomal proenzyme forms to the lysosome where maturation is thought to occur. The combination of the high rates of incorporation of [3H]fucose and the known metabolic stability of this precursor sugar suggests that the mouse kidney system is advantageous for studies of the synthesis, processing, and degradation of fucose-containing complex oligosaccharides of lysosomal enzymes and, by extension, of other kidney glycoproteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11302-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Synthesis and processing of lysosomal enzymes of mouse kidney after treatment with [3H]fucose.
pubmed:affiliation
Department of Obstetrics and Gynecology, School of Medicine, Vanderbilt University, Nashville, Tennessee 37232.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.