|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5872
|
|
pubmed:dateCreated |
1982-8-26
|
|
pubmed:abstractText |
A wide range of receptors are located at the blood sinusoidal aspect of the hepatocyte plasma membrane. Many circulating ligands that bind to receptors on the cell surfaces are interiorized along two pathways. Asialoglycoproteins are transferred from the plasma membrane to lysosomes and degraded, whereas immunoglobulin A and bile acids are transported across the hepatocyte interior and released into bile. Asialotransferrin type 3 (ref. 6) follows a further pathway termed diacytosis. After binding to the asialoglycoprotein receptor, asialotransferrin is endocytosed and then returned to blood with a proportion of its carbohydrate side chains resialylated. We now describe in liver the properties of intracellular asialotransferrin-enclosing vesicles (diacytosomes) and show that they differ from Golgi, lysosome and plasma membrane fractions. Furthermore, we show that the asialoglycoprotein binding sites are located on the cytoplasmic (outer) surface of diacytosomes.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Asialoglycoprotein Receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Asialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/asialotransferrins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0028-0836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
22
|
|
pubmed:volume |
298
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
398-400
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:6283390-Animals,
pubmed-meshheading:6283390-Asialoglycoprotein Receptor,
pubmed-meshheading:6283390-Asialoglycoproteins,
pubmed-meshheading:6283390-Cell Fractionation,
pubmed-meshheading:6283390-Cell Membrane,
pubmed-meshheading:6283390-Cytoplasm,
pubmed-meshheading:6283390-Galactosyltransferases,
pubmed-meshheading:6283390-Golgi Apparatus,
pubmed-meshheading:6283390-Insulin,
pubmed-meshheading:6283390-Intracellular Membranes,
pubmed-meshheading:6283390-Liver,
pubmed-meshheading:6283390-Octoxynol,
pubmed-meshheading:6283390-Organoids,
pubmed-meshheading:6283390-Polyethylene Glycols,
pubmed-meshheading:6283390-Rats,
pubmed-meshheading:6283390-Receptor, Insulin,
pubmed-meshheading:6283390-Receptors, Cell Surface,
pubmed-meshheading:6283390-Transferrin,
pubmed-meshheading:6283390-Trypsin
|
|
pubmed:year |
1982
|
|
pubmed:articleTitle |
Receptor-rich intracellular membrane vesicles transporting asialotransferrin and insulin in liver.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
