|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
24
|
|
pubmed:dateCreated |
1990-2-1
|
|
pubmed:abstractText |
Chinese hamster ovary (CHO-K1) cells were pulse labeled with [3H]serine, and the synthesis of phosphatidyl[3H]ethanolamine from phosphatidyl[3H]serine during the subsequent chase was used as a measure of lipid translocation to the mitochondria. When the CHO-K1 cells were pulse labeled and subsequently permeabilized with 50 micrograms of saponin per ml, there was no significant turnover of nascent phosphatidyl[3H]serine to form phosphatidyl[3H]ethanolamine during an ensuing chase. Saponin treatment rendered greater than 99% of the cells permeable as judged by trypan blue exclusion and depleted them of 85% of their complement of cytosolic proteins as determined by residual lactic acid dehydrogenase activity. Supplementation of the permeabilized cells with 2 mM ATP resulted in significant phosphatidyl[3H]ethanolamine synthesis (83% of that found in intact cells) from phosphatidyl[3H]serine during a subsequent 2-hr chase. Phosphatidyl[3H]ethanolamine synthesis essentially ceased after 2 hr in the permeabilized cells. The translocation-dependent synthesis of phosphatidyl[3H]ethanolamine was a saturable process with respect to ATP concentration in permeabilized cells. The conversion of phosphatidyl[3H]serine to phosphatidyl[3H]ethanolamine did not occur in saponin-treated cultures supplemented with 2 mM AMP, 2 mM 5'-adenylyl imidodiphosphate, or apyrase (2.5 units/ml) plus 2 mM ATP. ATP was the most effective nucleotide, but the addition of GTP, CTP, UTP, and ADP also supported the translocation-dependent synthesis of phosphatidyl[3H]ethanolamine albeit to a lesser extent. These data provide evidence that the interorganelle translocation of phosphatidylserine requires ATP and is largely independent of soluble cytosolic proteins.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-1256578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-13671378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-203454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-212440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-2542259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-2642391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-2833521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-2917149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-2997219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3003047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3081502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3084470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3090025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3304148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3768356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-3856869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-4040520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-4329152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-4425464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-4968799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-5016308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-5835014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-6243289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-6425837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-6746745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-6773570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-6838865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2602382-7437457
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
86
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
9921-5
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:2602382-Adenosine Triphosphate,
pubmed-meshheading:2602382-Adenylyl Imidodiphosphate,
pubmed-meshheading:2602382-Animals,
pubmed-meshheading:2602382-Biological Transport,
pubmed-meshheading:2602382-Carboxy-Lyases,
pubmed-meshheading:2602382-Cell Line,
pubmed-meshheading:2602382-Cell Membrane Permeability,
pubmed-meshheading:2602382-Kinetics,
pubmed-meshheading:2602382-Mitochondria,
pubmed-meshheading:2602382-Phosphatidylethanolamines,
pubmed-meshheading:2602382-Phosphatidylserines,
pubmed-meshheading:2602382-Ribonucleotides,
pubmed-meshheading:2602382-Saponins
|
|
pubmed:year |
1989
|
|
pubmed:articleTitle |
Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells.
|
|
pubmed:affiliation |
Lord and Taylor Laboratory for Lung Biochemistry, Department of Medicine, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
