Linked Life Data

221921

Source:http://linkedlifedata.com/resource/pubmed/id/221921

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1979-8-29
pubmed:abstractText
Competitive binding assays have demonstrated that a cholesterol-induced canine lipoprotein containing only the E apoprotein (apo-E HDL(c)) binds to the same cell surface receptors of human fibroblasts as human low density lipoproteins (LDL). However, the apo-E HDL(c) have a much greater binding activity than LDL. Equilibrium and kinetic binding studies were conducted at 4 degrees C to determine the mechanism for this enhanced receptor binding activity. Based on the data, the binding of both LDL and apo-E HDL(c) appears to be a simple bimolecular receptor interaction, and no heterogeneity of binding sites or cooperative effects among the receptor sites were observed. Equilibrium dissociation constants determined by Scatchard analysis of the equilibrium binding data for apo-E HDL(c) (K(d) = 0.12 x 10(-9) M) and LDL (K(d) = 2.8 x 10(-9) M) revealed a 23-fold greater affinity of HDL(c) for the receptors. Association and dissociation rate constants for the lipoprotein-receptor complex were determined from the time course of binding at various lipoprotein concentrations. The equilibrium dissociation constants calculated from these kinetic data confirmed that apo-E HDL(c) had a much higher affinity for the receptor than LDL. Furthermore, the kinetic studies indicated that apo-E HDL(c) bound more rapidly than LDL with rates of association of 18.0 x 10(4) and 5.5 x 10(4) M(-1) sec(-1), respectively. The rate of dissociation of the apo-E HDL(c)-receptor complex (1.7 x 10(-5) sec(-1)) was slower than that of the LDL receptor complex (6.3 x 10(-5) sec(-1)). An additional important difference between the binding of apo-E HDL(c) and LDL was that 4 times (3.6 +/- 0.4) as many LDL particles as HDL(c) particles were required for saturation of the receptors at maximal binding. These data indicate that each HDL(c) particle binds to multiple cell surface receptors at a ratio of 4:1 for LDL receptor binding.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-167808, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-177413, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-181140, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-189940, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-192082, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-193851, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-197883, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-198407, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-200368, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-206278, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-210175, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-214439, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-4138629, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-4334903, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-4335139, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-4362634, http://linkedlifedata.com/resource/pubmed/commentcorrection/221921-4733239
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2311-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Rate and equilibrium constants for binding of apo-E HDLc (a cholesterol-induced lipoprotein) and low density lipoproteins to human fibroblasts: evidence for multiple receptor binding of apo-E HDLc.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.