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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1996-9-18
|
| pubmed:abstractText |
Lactoferrin inhibits the hepatic uptake of lipoprotein remnants, and we showed earlier that arginine residues of lactoferrin are involved. In this study, lactoferrin was treated with aminopeptidase-M (APM), which resulted in removal of 14 N-terminal amino acids, including 4 clustered arginines at positions 2-5 (APM-lactoferrin). After i.v. injection into rats, 125I-APM-lactoferrin was cleared within 10 min by the liver parenchymal cells (74.7% of the dose). Binding of APM-lactoferrin to isolated parenchymal liver cells was saturable with a Kd of 186 nM (750.000 sites/cell). This is in striking contrast to the binding of lactoferrin (Kd 10 microM; 20 x 10(6) sites/cell). Preinjection of rats with 20 mg of APM-lactoferrin/kg body weight reduced the liver association of beta-VLDL by 50%, whereas lactoferrin had no effect at this dose. With isolated parenchymal liver cells, APM-lactoferrin was a more effective competitor for beta-VLDL binding than native lactoferrin (50% inhibition at 0.5 mg/ml vs. 8.0 mg/ml). We conclude that the 4-arginine cluster of lactoferrin at position 2-5 involved in the massive association of lactoferrin with the parenchymal liver cell, but is not essential for the inhibition of the lipoprotein remnant uptake. The Arg/Lys sequence at position 25-30, which resembles the binding site of apoE, may mediate the high affinity binding of lactoferrin and block the binding of beta-VLDL to the remnant receptor efficiently.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0044-2771
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
34 Suppl 3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
118-21
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:8767485-Aminopeptidases,
pubmed-meshheading:8767485-Animals,
pubmed-meshheading:8767485-Binding Sites,
pubmed-meshheading:8767485-Endocytosis,
pubmed-meshheading:8767485-Lactoferrin,
pubmed-meshheading:8767485-Lipoproteins, VLDL,
pubmed-meshheading:8767485-Liver,
pubmed-meshheading:8767485-Male,
pubmed-meshheading:8767485-Rats,
pubmed-meshheading:8767485-Rats, Wistar
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Recognition of lactoferrin and aminopeptidase M-modified lactoferrin by the liver: involvement of the remnant receptor.
|
| pubmed:affiliation |
Division of Biopharmaceutics, Leiden/Amsterdam Center for Drug Research, University of Leiden, Sylvius Laboratory, The Netherlands.
|
| pubmed:publicationType |
Journal Article
|