Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1997-10-15
|
pubmed:abstractText |
This study evaluated whether annexins I, II and VI possess Ca2+ transport activity in phospholipid membranes by the burst method, and the activity of each was compared with that of annexin V. Briefly, in the presence of 400 microM Ca2+, each annexin at 50 nM was added to large unilamellar vesicles (LUV) which were then burst in fura-2 solution with 0.2% Triton X-100, followed by examination of Ca2+ signals. Annexins I, II, V and VI were all shown to express, each to a different degree, Ca2+ activity toward phosphatidylserine/phosphatidyl- ethanolamine-LUV. Ca2+ signal intensity increased dependent on annexin concentration, and the Ca2+ transport activity of annexin V and VI was higher than that of annexin I and II. However, none of annexin I, II, V and VI expressed Ca2+ transport activity in LUV produced using phosphatidylcholine. Ca(2+)-incorporated LUV with no annexin showed signals whose intensity was proportional to Ca2+ concentration. The Ca2+ transport activity of the annexins could be effectively measured by the burst method. Ca2+ signal intensity would thus appear to be unique for each of the annexins and to be determined by the particular function and specificity of each of those considered in this study.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A1,
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A2,
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A5,
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A6,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylethanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
28
|
pubmed:volume |
237
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
499-503
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9299392-Animals,
pubmed-meshheading:9299392-Annexin A1,
pubmed-meshheading:9299392-Annexin A2,
pubmed-meshheading:9299392-Annexin A5,
pubmed-meshheading:9299392-Annexin A6,
pubmed-meshheading:9299392-Calcium,
pubmed-meshheading:9299392-Cattle,
pubmed-meshheading:9299392-Kinetics,
pubmed-meshheading:9299392-Liposomes,
pubmed-meshheading:9299392-Liver,
pubmed-meshheading:9299392-Lung,
pubmed-meshheading:9299392-Myocardium,
pubmed-meshheading:9299392-Phosphatidylethanolamines,
pubmed-meshheading:9299392-Phosphatidylserines,
pubmed-meshheading:9299392-Rats,
pubmed-meshheading:9299392-Serum Albumin, Bovine
|
pubmed:year |
1997
|
pubmed:articleTitle |
Presence and comparison of Ca2+ transport activity of annexins I, II, V, and VI in large unilamellar vesicles.
|
pubmed:affiliation |
Department of Anatomy, Tokyo Women's Medical College, Japan. matsudar@research.twmc.ac.jp
|
pubmed:publicationType |
Journal Article,
Comparative Study
|