Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1984-11-26
pubmed:abstractText
A 10,000-11,000 molecular weight apoprotein was isolated from an ethanol-ether extract of rat lung surfactant and purified by silicic acid chromatography. The protein (Apo Et) significantly augmented the uptake of phospholipids in liposomal form by cultured rat granular pneumocytes by a time-dependent process that varied with protein concentration and liposome composition. The protein had no effect on cell viability and showed no phospholipase activity. The mechanism for this augmented phospholipid uptake is not known but could be due to an alteration of physical form of the phospholipids by the protein or to a receptor-mediated uptake of phospholipids. This protein may prove to be a physiologically important regulator of the recycling of lung surfactant phospholipids.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0190-2148
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
"Hydrophobic" surfactant apoproteins and augmentation of phospholipid recycling.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't