Linked Life Data

1331083

Source:http://linkedlifedata.com/resource/pubmed/id/1331083

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1992-12-16
pubmed:abstractText
We have examined the phosphorylation of Asn-linked oligosaccharides introduced at seven novel sites on human cathepsin D to determine whether the location of an oligosaccharide on a lysosomal enzyme affects its ability to serve as a substrate for UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransferase), the enzyme that catalyzes the initial step in the biosynthesis of mannose 6-phosphate residues. The glycosylation sites were introduced into the cathepsin D cDNA by site-directed mutagenesis and were selected to be widely distributed over the surface of the molecule. When the constructs were expressed in Xenopus oocytes, the oligosaccharides at each glycosylation site were phosphorylated at levels considerably above background (19-70% phosphorylation versus < 0.4% for the secretory protein glycopepsinogen). However, oligosaccharides located closer to the essential components of the phosphotransferase recognition domain (lysine 203 and amino acids 265-292) were phosphorylated better than oligosaccharides located further away. Similar results were obtained for oligosaccharides at homologous sites on a pepsinogen/cathepsin D chimera containing only lysine 203 and residues 265-319 of cathepsin D, although the absolute levels of phosphorylation were lower. These results demonstrate that there is considerable flexibility in the placement of glycosylation sites on cathepsin D in terms of the ability of the oligosaccharides to serve as substrates for phosphotransferase, although oligosaccharides located closer to the phosphotransferase recognition determinant are preferentially phosphorylated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23357-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1331083-Animals, pubmed-meshheading:1331083-Asparagine, pubmed-meshheading:1331083-Carbohydrate Conformation, pubmed-meshheading:1331083-Carbohydrate Sequence, pubmed-meshheading:1331083-Cathepsin D, pubmed-meshheading:1331083-Cloning, Molecular, pubmed-meshheading:1331083-Glycoside Hydrolases, pubmed-meshheading:1331083-Glycosylation, pubmed-meshheading:1331083-Humans, pubmed-meshheading:1331083-Kinetics, pubmed-meshheading:1331083-Lysosomes, pubmed-meshheading:1331083-Molecular Sequence Data, pubmed-meshheading:1331083-Oligosaccharides, pubmed-meshheading:1331083-Oocytes, pubmed-meshheading:1331083-Phosphorylation, pubmed-meshheading:1331083-Phosphotransferases, pubmed-meshheading:1331083-Plasmids, pubmed-meshheading:1331083-Protein Conformation, pubmed-meshheading:1331083-Restriction Mapping, pubmed-meshheading:1331083-Substrate Specificity, pubmed-meshheading:1331083-Transferases (Other Substituted Phosphate Groups), pubmed-meshheading:1331083-Xenopus laevis
pubmed:year
1992
pubmed:articleTitle
Phosphorylation of Asn-linked oligosaccharides located at novel sites on the lysosomal enzyme cathepsin D.
pubmed:affiliation
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.