FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2169341489> ?p ?o ?g. }

• W2169341489 endingPage "295" @default.
• W2169341489 startingPage "289" @default.
• W2169341489 abstract "1. Lactoferrin and aminopeptidase M-modified lactoferrin (APM-lactoferrin; which lacks its 14 N-terminal amino acids) inhibit the liver uptake of lipoprotein remnants. In the present study, the role of proteoglycans in the initial interaction of β-migrating very-low-density lipoprotein (β-VLDL), native and APM-lactoferrin with isolated rat parenchymal liver cells was investigated. Treatment of the cells with chondroitinase lowered the Kd of lactoferrin binding (from 10 to 2.4 μM), and the number of sites/cell (from 20×106 to 7×106), while heparinase treatment did not affect the binding. The binding characteristics of APM-lactoferrin and β-VLDL were not altered by treatment of the cells with chondroitinase or heparinase. It is concluded that proteoglycans are not involved in the initial binding of APM-lactoferrin and β-VLDL to parenchymal cells, while chondroitin sulphate proteoglycans are mainly responsible for the massive, low-affinity binding of native lactoferrin. 2. The binding of lactoferrin, APM-lactoferrin and β-VLDL to parenchymal liver cells was not influenced by the glutathione S-transferase-receptor-associated protein (GST-RAP) (97.2±4.0%, 95.5±3.7% and 98.5% of the control binding), while the binding of α2-macroglobulin was fully blocked at 10 μg/ml GST-RAP (1.8±0.5% of the control binding). Since GST-RAP blocks the binding of all the known ligands to the low-density lipoprotein (LDL)-receptor-related protein (LRP), it is concluded that LRP is not the initial primary recognition site for lactoferrin, APM-lactoferrin and β-VLDL on parenchymal liver cells. 3. We showed earlier that APM-lactoferrin, as compared with lactoferrin, is a more effective inhibitor of the liver uptake of lipoprotein remnants (49.4±4.0% versus 80.8±4.8% of the control at 500 μg/ml respectively). We found in the present study that β-VLDL is able to inhibit the binding of APM-lactoferrin to parenchymal liver cells significantly (74.9±3.3% of the control; P &lt; 0.002), while the lactoferrin binding was unaffected. It is concluded that a still unidentified specific recognition site (the putative remnant receptor) is responsible for the initial binding of remnants to parenchymal cells and it is suggested that the partial cross-competition between APM-lactoferrin and β-VLDL may be of further help in the elucidation of the molecular nature of this recognition site." @default.
• W2169341489 created "2016-06-24" @default.
• W2169341489 creator A5000147978 @default.
• W2169341489 creator A5017175413 @default.
• W2169341489 creator A5073475622 @default.
• W2169341489 creator A5090088499 @default.
• W2169341489 date "1996-01-01" @default.
• W2169341489 modified "2023-10-17" @default.
• W2169341489 title "Recognition of lactoferrin and aminopeptidase M-modified lactoferrin by the liver: involvement of proteoglycans and the remnant receptor" @default.
• W2169341489 cites W1254605347 @default.
• W2169341489 cites W1490154674 @default.
• W2169341489 cites W1490629978 @default.
• W2169341489 cites W1515028535 @default.
• W2169341489 cites W152075184 @default.
• W2169341489 cites W1521056506 @default.
• W2169341489 cites W1555380614 @default.
• W2169341489 cites W1556453331 @default.
• W2169341489 cites W1578786377 @default.
• W2169341489 cites W1583563138 @default.
• W2169341489 cites W1586184394 @default.
• W2169341489 cites W1590765841 @default.
• W2169341489 cites W1600508667 @default.
• W2169341489 cites W1658991581 @default.
• W2169341489 cites W1725290148 @default.
• W2169341489 cites W1777833087 @default.
• W2169341489 cites W1778185206 @default.
• W2169341489 cites W1840979539 @default.
• W2169341489 cites W1870396813 @default.
• W2169341489 cites W1900087291 @default.
• W2169341489 cites W1986625588 @default.
• W2169341489 cites W1991236622 @default.
• W2169341489 cites W2001924222 @default.
• W2169341489 cites W2011069780 @default.
• W2169341489 cites W201928681 @default.
• W2169341489 cites W2024982245 @default.
• W2169341489 cites W2030058228 @default.
• W2169341489 cites W2034657155 @default.
• W2169341489 cites W2034968148 @default.
• W2169341489 cites W2040676625 @default.
• W2169341489 cites W2043983463 @default.
• W2169341489 cites W2048252705 @default.
• W2169341489 cites W2049370364 @default.
• W2169341489 cites W2054941870 @default.
• W2169341489 cites W2077576735 @default.
• W2169341489 cites W2078923563 @default.
• W2169341489 cites W2081860696 @default.
• W2169341489 cites W2085338361 @default.
• W2169341489 cites W2085649019 @default.
• W2169341489 cites W2087757733 @default.
• W2169341489 cites W2095029703 @default.
• W2169341489 cites W2130728604 @default.
• W2169341489 cites W2155759352 @default.
• W2169341489 cites W2163682706 @default.
• W2169341489 cites W2185289999 @default.
• W2169341489 cites W2260568133 @default.
• W2169341489 cites W2319573935 @default.
• W2169341489 cites W248108054 @default.
• W2169341489 cites W4248975799 @default.
• W2169341489 cites W2230565627 @default.
• W2169341489 doi "https://doi.org/10.1042/bj3130289" @default.
• W2169341489 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1216896" @default.
• W2169341489 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8546697" @default.
• W2169341489 hasPublicationYear "1996" @default.
• W2169341489 type Work @default.
• W2169341489 sameAs 2169341489 @default.
• W2169341489 citedByCount "29" @default.
• W2169341489 countsByYear W21693414892012 @default.
• W2169341489 countsByYear W21693414892016 @default.
• W2169341489 crossrefType "journal-article" @default.
• W2169341489 hasAuthorship W2169341489A5000147978 @default.
• W2169341489 hasAuthorship W2169341489A5017175413 @default.
• W2169341489 hasAuthorship W2169341489A5073475622 @default.
• W2169341489 hasAuthorship W2169341489A5090088499 @default.
• W2169341489 hasBestOaLocation W21693414892 @default.
• W2169341489 hasConcept C153911025 @default.
• W2169341489 hasConcept C170493617 @default.
• W2169341489 hasConcept C185592680 @default.
• W2169341489 hasConcept C2778163477 @default.
• W2169341489 hasConcept C2779170986 @default.
• W2169341489 hasConcept C2780072125 @default.
• W2169341489 hasConcept C43554185 @default.
• W2169341489 hasConcept C55493867 @default.
• W2169341489 hasConcept C8243546 @default.
• W2169341489 hasConcept C86803240 @default.
• W2169341489 hasConceptScore W2169341489C153911025 @default.
• W2169341489 hasConceptScore W2169341489C170493617 @default.
• W2169341489 hasConceptScore W2169341489C185592680 @default.
• W2169341489 hasConceptScore W2169341489C2778163477 @default.
• W2169341489 hasConceptScore W2169341489C2779170986 @default.
• W2169341489 hasConceptScore W2169341489C2780072125 @default.
• W2169341489 hasConceptScore W2169341489C43554185 @default.
• W2169341489 hasConceptScore W2169341489C55493867 @default.
• W2169341489 hasConceptScore W2169341489C8243546 @default.
• W2169341489 hasConceptScore W2169341489C86803240 @default.
• W2169341489 hasIssue "1" @default.
• W2169341489 hasLocation W21693414891 @default.
• W2169341489 hasLocation W21693414892 @default.
• W2169341489 hasLocation W21693414893 @default.

• next