ENDOCYTOSIS OF FORMALDEHYDE-DENATURED SERUM-ALBUMIN BY NONPARENCHYMAL LIVER-CELLS INVITRO

Eskild, W; Berg, T

HERO ID

1578985

Reference Type

Journal Article

Year

1984

Language

English

PMID

6696954

HERO ID 1578985
In Press No
Year 1984
Title ENDOCYTOSIS OF FORMALDEHYDE-DENATURED SERUM-ALBUMIN BY NONPARENCHYMAL LIVER-CELLS INVITRO
Authors Eskild, W; Berg, T
Journal Biochimica et Biophysica Acta
Volume 803
Issue 1-2
Page Numbers 63-70
Abstract 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.
Doi 10.1016/0167-4889(84)90055-7
Pmid 6696954
Wosid WOS:A1984SH59700009
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:A1984SH59700009
Is Public Yes
Language Text English