Linked Life Data

1318310

Source:http://linkedlifedata.com/resource/pubmed/id/1318310

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1992-7-16
pubmed:databankReference
pubmed:abstractText
Plasma membranes of cultured cells contain high affinity receptors for high density lipoprotein (HDL) that appear to mediate removal of excess intracellular cholesterol. Recent studies using ligand blot analysis have identified a 110-kDa membrane protein which has features predicted for an HDL receptor, in that it preferentially binds HDL apolipoproteins and undergoes up-regulation in response to cholesterol loading of cells. In this study, we isolated a cDNA clone from an expression library using an antibody raised against partially purified 110-kDa HDL-binding protein. This clone encodes a novel cell protein, designated HBP, comprised mostly of 14 imperfect tandem repeats of approximately 70 amino acids in length. Each repeat appears to contain two amphipathic helices. Expression of HBP in cultured cells was increased severalfold when cells were loaded with cholesterol, as evident by increases in both HBP mRNA and membrane-associated protein. Overexpression of HBP in mammalian cell transfectants was associated with higher HDL binding to isolated cell protein and with modest increases in HDL binding to the cell surface. Proteins identified by ligand blot analysis had lower apparent M(r) than the primary HBP gene product and varied in M(r) and in HDL binding activity between cell types, suggesting that HBP undergoes cell-specific processing. These results provide preliminary evidence that HBP is a component of a cellular pathway that facilitates removal of excess cholesterol from cells, perhaps through its interaction with HDL. However, the predicted structure of HBP does not conform to that of any known receptor, suggesting that it does not function as a classic plasma membrane receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
12131-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1318310-Amino Acid Sequence, pubmed-meshheading:1318310-Animals, pubmed-meshheading:1318310-Base Sequence, pubmed-meshheading:1318310-Blotting, Western, pubmed-meshheading:1318310-Carrier Proteins, pubmed-meshheading:1318310-Cattle, pubmed-meshheading:1318310-Cells, Cultured, pubmed-meshheading:1318310-Cholesterol, pubmed-meshheading:1318310-Cloning, Molecular, pubmed-meshheading:1318310-DNA, pubmed-meshheading:1318310-Gene Expression, pubmed-meshheading:1318310-Humans, pubmed-meshheading:1318310-Lipoproteins, HDL, pubmed-meshheading:1318310-Molecular Sequence Data, pubmed-meshheading:1318310-Polymerase Chain Reaction, pubmed-meshheading:1318310-RNA-Binding Proteins, pubmed-meshheading:1318310-Receptors, Cell Surface, pubmed-meshheading:1318310-Receptors, Lipoprotein, pubmed-meshheading:1318310-Sequence Alignment, pubmed-meshheading:1318310-Tumor Cells, Cultured, pubmed-meshheading:1318310-Up-Regulation
pubmed:year
1992
pubmed:articleTitle
Cloning and expression of a cellular high density lipoprotein-binding protein that is up-regulated by cholesterol loading of cells.
pubmed:affiliation
Zymogenetics Incorporated, Seattle, Washington 98105.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.