Abstract:
:The fate of [125I] lactoferrin after binding on its specific receptor on HT29-D4 cells, a clone of HT29 cells, was studied and compared with that of [125I]transferrin. Time courses of protein binding in relation with temperature clearly show that different mechanisms of ligand-transportation for the two glycoproteins exist on these cells: whereas transferrin would enter into the cell probably by a relatively classic pathway of receptor-mediated endocytosis, lactoferrin and its specific receptor would not be internalized. Thus the mechanism by which lactoferrin promotes HT29 cell growth seems quite different from that of transferrin on the same cells.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Roiron-Lagroux D,Figarella Cdoi
10.1016/0006-291x(90)92167-xsubject
Has Abstractpub_date
1990-07-31 00:00:00pages
837-42issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(90)92167-Xjournal_volume
170pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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更新日期:1993-06-30 00:00:00
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journal_title:Biochemical and biophysical research communications
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更新日期:2005-04-01 00:00:00
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journal_title:Biochemical and biophysical research communications
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更新日期:1995-04-26 00:00:00
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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更新日期:1997-09-08 00:00:00
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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更新日期:2000-01-07 00:00:00
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journal_title:Biochemical and biophysical research communications
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更新日期:2018-05-05 00:00:00
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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