Linked Life Data

2439503

Source:http://linkedlifedata.com/resource/pubmed/id/2439503

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1987-7-29
pubmed:abstractText
The uptake, internalization, and intracellular degradation of 125I-labeled recombinant tissue-type plasminogen activator (rt-PA) by isolated rat hepatocytes was investigated. Incubation at 37 degrees C resulted in internalization of 125I-rt-PA, followed by the appearance of labeled trichloroacetic acid-soluble material in the incubation media due to degradation of rt-PA. Degradation of rt-PA was inhibited by the presence of NH4Cl (10 mM) or chloroquine (1 mM) (lysosomal tropic agents) in the incubation media. This suggests that rt-PA degradation occurs intracellularly, perhaps within the lysosomes. 125I-rt-PA was taken up by rat hepatocytes through a specific, high affinity mechanism with half-maximal uptake at 10 nM. Uptake of 125I-rt-PA was not inhibited by glycopeptides isolated from rt-PA nor by several other glycoproteins known to be cleared by identified hepatic receptors. These results suggest that the uptake of rt-PA by rat hepatocytes involves a receptor specific for t-PA and is not mediated by a carbohydrate-specific receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8716-20
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Cellular catabolism of recombinant tissue-type plasminogen activator. Identification and characterization of a novel high affinity uptake system on rat hepatocytes.
pubmed:publicationType
Journal Article, In Vitro