Linked Life Data

7592875

Source:http://linkedlifedata.com/resource/pubmed/id/7592875

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
1995-12-21
pubmed:abstractText
The very low density lipoprotein (VLDL) receptor binds apolipoprotein E-rich lipoproteins as well as the 39-kDa receptor-associated protein (RAP). Ligand blotting experiments using RAP and immunoblotting experiments using an anti-VLDL receptor IgG detected the VLDL receptor in detergent extracts of human aortic endothelial cells, human umbilical vein endothelial cells, and human aortic smooth muscle cells. To gain insight into the role of the VLDL receptor in the vascular endothelium, its ligand binding properties were further characterized. In vitro binding experiments documented that lipoprotein lipase (LpL), a key enzyme in lipoprotein catabolism, binds with high affinity to purified VLDL receptor. In addition, urokinase complexed with plasminogen activator-inhibitor type I (uPA.PAI-1) also bound to the purified VLDL receptor with high affinity. To assess the capacity of the VLDL receptor to mediate the cellular internalization of ligands, an adenoviral vector was used to introduce the VLDL receptor gene into a murine embryonic fibroblast cell line deficient in the VLDL receptor and the LDL receptor-related protein, another endocytic receptor known to bind LpL and uPA.PAI-1 complexes. Infected fibroblasts that express the VLDL receptor mediate the cellular internalization of 125I-labeled LpL and uPA.PAI-1 complexes, leading to their degradation. Non-infected fibroblasts or fibroblasts infected with the lacZ gene did not internalize these ligands. These studies confirm that the VLDL receptor binds to and mediates the catabolism of LpL and uPA.PAI-1 complexes. Thus, the VLDL receptor may play a unique role on the vascular endothelium in lipoprotein catabolism by regulating levels of LpL and in the regulation of fibrinolysis by facilitating the removal of urokinase complexed with its inhibitor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26550-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7592875-Adenoviruses, Human, pubmed-meshheading:7592875-Aorta, pubmed-meshheading:7592875-Apolipoproteins E, pubmed-meshheading:7592875-Carrier Proteins, pubmed-meshheading:7592875-Cell Line, pubmed-meshheading:7592875-Cell Transformation, Viral, pubmed-meshheading:7592875-Cells, Cultured, pubmed-meshheading:7592875-Endothelium, Vascular, pubmed-meshheading:7592875-Glycoproteins, pubmed-meshheading:7592875-Humans, pubmed-meshheading:7592875-Kinetics, pubmed-meshheading:7592875-LDL-Receptor Related Protein-Associated Protein, pubmed-meshheading:7592875-Lipoprotein Lipase, pubmed-meshheading:7592875-Muscle, Smooth, Vascular, pubmed-meshheading:7592875-Plasminogen Activator Inhibitor 1, pubmed-meshheading:7592875-Protein Binding, pubmed-meshheading:7592875-Receptors, LDL, pubmed-meshheading:7592875-Recombinant Proteins, pubmed-meshheading:7592875-Umbilical Veins, pubmed-meshheading:7592875-Urokinase-Type Plasminogen Activator
pubmed:year
1995
pubmed:articleTitle
The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes.
pubmed:affiliation
Holland Laboratory, Department of Biochemistry, American Red Cross, Rockville, Maryland 20855, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't