Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1984-4-13
pubmed:abstractText
The uptake and degradation of 125I-labeled formaldehyde-denatured serum albumin in nonparenchymal rat liver cells were studied in vitro. Nonparenchymal cells bound formaldehyde-denatured serum albumin at two types of binding site, one with a high affinity and one a low affinity. The number of high affinity binding sites was approx. 10(5) per cell and the association constant, Ka 10(8) M-1. Inhibition of protein synthesis with cycloheximide did not affect the uptake and degradation of formaldehyde-denatured serum albumin suggesting reutilization of the binding sites. The presence of monensin-reduced uptake and degradation to less than 10% of control values. Pronase treatment of nonparenchymal liver cells completely abolished the uptake and degradation of the ligand. The uptake mechanism was not specific for formaldehyde-denatured serum albumin. Unlabeled acetylated, as well as malondialdehyde treated, serum albumin reduced the uptake of 125I-labeled formaldehyde-denatured serum albumin as effectively as unlabeled formaldehyde-denatured serum albumin itself.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
803
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-70
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Endocytosis of formaldehyde-denatured serum albumin by nonparenchymal liver cells in vitro.
pubmed:publicationType
Journal Article