rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5-6
|
pubmed:dateCreated |
1993-2-12
|
pubmed:abstractText |
We studied the receptor mediated endocytosis of a modified glycoprotein (N-acetylglucosamine-BSA) and mannan in cultured hepatocytes isolated from 19-days-old embryos. The binding sites for molecules exposing terminal N-acetylglucosamine (GlcNac) and mannose residues were localized and quantified at the ultrastructural level by means of protein-gold complexes. The binding sites were found to be randomly distributed as single gold particles on cultured hepatocyte cell surfaces not restricted to specialized areas of the plasma membrane. The gold ligands were internalized following a receptor mediated pathway, which was studied at different interval times (15, 30 and 60 min.) after incubating the cells with the electron dense markers.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0145-5680
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
38
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
621-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1336427-Acetylglucosamine,
pubmed-meshheading:1336427-Animals,
pubmed-meshheading:1336427-Biological Transport,
pubmed-meshheading:1336427-Carbohydrate Metabolism,
pubmed-meshheading:1336427-Cell Membrane,
pubmed-meshheading:1336427-Cells, Cultured,
pubmed-meshheading:1336427-Chick Embryo,
pubmed-meshheading:1336427-Endocytosis,
pubmed-meshheading:1336427-Ligands,
pubmed-meshheading:1336427-Liver,
pubmed-meshheading:1336427-Mannans,
pubmed-meshheading:1336427-Receptors, Cell Surface,
pubmed-meshheading:1336427-Serum Albumin
|
pubmed:articleTitle |
Receptor mediated endocytosis of N-acetylglucosamine and mannose exposing molecules by cultured chick embryo hepatocytes.
|
pubmed:affiliation |
Department of Biology, University of Rome Tor Vergata, Italy.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|