Linked Life Data

1329984

Source:http://linkedlifedata.com/resource/pubmed/id/1329984

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-12-23
pubmed:abstractText
The binding of human intermediate density lipoproteins (IDL) to HepG2 cells was studied. We found that human 125I-IDL interact with a binding site of high-affinity (Kd 0.74 micrograms/ml, Bmax 0.049 micrograms/mg cell protein) and a binding site of lower affinity (Kd 86.8 micrograms/ml; Bmax 0.53 micrograms/mg cell protein). The high-affinity binding sites show characteristics of LDL-receptors since they interact with IDL and low-density lipoproteins (LDL) and are calcium dependent. The low-affinity binding sites are calcium-independent and interact with IDL, LDL, high density lipoproteins-3 (HDL3), apolipoprotein (apo) E-liposomes, apoCs-liposomes, apoA-I-liposomes but not with liposomes containing albumin or erythrocyte membrane proteins. Therefore, HepG2 cells have on their surface a binding site that resembles or is identical to the lipoprotein binding site (LBS) that we found on rat liver membranes (Brissette and Noël (1986) J. Biol. Chem. 261, 6847-6852). Internalization, degradation and cholesterol ester selective uptake were determined in the presence or in the absence of a sufficient amount of human HDL3 to abolish the interaction of IDL to the LBS in order to obtain information on the function of this site. Our results suggest that the LBS participates in the internalization of IDL but not in their degradation and that it is responsible for the selective uptake of cholesterol esters of IDL.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
1165
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Analysis of the binding and association of human intermediate density lipoproteins to HepG2 cells.
pubmed:affiliation
Laboratory of Lipoprotein Metabolism, Clinical Research Institute of Montreal, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't