Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1981-7-20
pubmed:abstractText
The clearance of native human placental glucocerebrosidase by rat liver shows the presence of two distinct enzyme forms with different recognition characteristics. The clearance and uptake of native enzyme by liver cells was compared to that of glucocerebrosidase sequentially treated with neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase. The initial rate of clearance of infused enzyme was increased greater than 10-fold for the asialo-, agalacto- and ahexoenzymes over that of native glucocerebrosidase. Incorporation of asialo enzyme was increased in hepatocytes over that of native enzyme, while the distribution of agalacto- and ahexoenzyme preparations was increased in non-parenchymal cells. This observation is consistent with the identification of a galactose receptor on hepatocytes and N-acetylglucosamine/mannose receptors on Kupffer cells. These data and inhibition studies by specified monosaccharide-terminal glycoprotein derivatives demonstrate the importance of these sugars in the uptake of this lysosomal enzyme by receptor-mediated endocytosis. Modification of the enzyme to expose certain monosaccharide moieties results in increased delivery to specific cell types. Therefore, naturally occurring receptors can be utilized for targeting glucocerebrosidase to the non-parenchymal cell in liver.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
673
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
425-34
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't