Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1997-8-18
pubmed:databankReference
pubmed:abstractText
The rapid movement of phospholipids (PL) between plasma membrane leaflets in response to increased intracellular Ca2+ is thought to play a key role in expression of platelet procoagulant activity and in clearance of injured or apoptotic cells. We recently reported isolation of a approximately 37-kDa protein in erythrocyte membrane that mediates Ca2+-dependent movement of PL between membrane leaflets, similar to that observed upon elevation of Ca2+ in the cytosol (Bassé, F., Stout, J. G., Sims, P. J., and Wiedmer, T. (1996) J. Biol. Chem. 271, 17205-17210). Based on internal peptide sequence obtained from this protein, a 1,445-base pair cDNA was cloned from a K-562 cDNA library. The deduced "PL scramblase" protein is a proline-rich, type II plasma membrane protein with a single transmembrane segment near the C terminus. Antibody against the deduced C-terminal peptide was found to precipitate the approximately 37-kDa red blood cell protein and absorb PL scramblase activity, confirming the identity of the cloned cDNA to erythrocyte PL scramblase. Ca2+-dependent PL scramblase activity was also demonstrated in recombinant protein expressed from plasmid containing the cDNA. Quantitative immunoblotting revealed an approximately 10-fold higher abundance of PL scramblase in platelet ( approximately 10(4) molecules/cell) than in erythrocyte ( approximately 10(3) molecules/cell), consistent with apparent increased PL scramblase activity of the platelet plasma membrane. PL scramblase mRNA was found in a variety of hematologic and nonhematologic cells and tissues, suggesting that this protein functions in all cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18240-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9218461-Amino Acid Sequence, pubmed-meshheading:9218461-Base Sequence, pubmed-meshheading:9218461-Carrier Proteins, pubmed-meshheading:9218461-Cloning, Molecular, pubmed-meshheading:9218461-DNA Primers, pubmed-meshheading:9218461-Erythrocyte Membrane, pubmed-meshheading:9218461-HL-60 Cells, pubmed-meshheading:9218461-HeLa Cells, pubmed-meshheading:9218461-Humans, pubmed-meshheading:9218461-Kinetics, pubmed-meshheading:9218461-Lipid Bilayers, pubmed-meshheading:9218461-Membrane Lipids, pubmed-meshheading:9218461-Membrane Proteins, pubmed-meshheading:9218461-Molecular Sequence Data, pubmed-meshheading:9218461-Phospholipid Transfer Proteins, pubmed-meshheading:9218461-Polymerase Chain Reaction, pubmed-meshheading:9218461-Recombinant Proteins, pubmed-meshheading:9218461-Tumor Cells, Cultured
pubmed:year
1997
pubmed:articleTitle
Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids.
pubmed:affiliation
Blood Research Institute, The Blood Center of Southeastern Wisconsin, Milwaukee, Wisconsin 53201-2178, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't