Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1994-6-29
|
pubmed:abstractText |
We investigated the use of annexin V (placental anticoagulant protein I), a calcium-dependent protein that binds tightly to phosphatidylserine-containing membranes, as a means to measure membrane phospholipid asymmetry in human erythrocytes. Iodine 125-labeled annexin V bound to erythrocytes in a specific, reversible, calcium-dependent reaction (dissociation constant = 25 +/- 4 nmol/L at 37 degrees C and 2.5 mmol/L calcium). Lysed erythrocytes contained 1.2 x 10(6) binding sites for annexin V. Treatment of erythrocytes with 1 mumol/L A23187 in the presence of 2.5 mmol/L calcium at 37 degrees C caused a gradual but marked increase in annexin V binding sites, reaching a level of approximately 300,000 sites per cell after 8 hours of incubation. We also noted a very gradual spontaneous exposure of annexin V binding sites during storage of purified erythrocytes, reaching a level of approximately 20,000 sites per cell after 30 days. Measurements could also be made directly on diluted whole blood specimens. In samples freshly drawn from 35 normal donors, a mean number of 276 sites per cell were present; this increased to 858 sites per cell after storage of specimens at 4 degrees C for 24 hours. Measurement of annexin V binding to samples from patients with sickle-cell anemia revealed a marked increase in binding (mean of 12,430 sites per cell for all samples); serial measurements in a patient hospitalized with sickle-cell crisis showed a progressive decline in annexin V binding over a period of 6 days.(ABSTRACT TRUNCATED AT 250 WORDS)
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A5,
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0022-2143
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
123
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
741-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8195679-Annexin A5,
pubmed-meshheading:8195679-Binding Sites,
pubmed-meshheading:8195679-Calcimycin,
pubmed-meshheading:8195679-Calcium,
pubmed-meshheading:8195679-Erythrocytes,
pubmed-meshheading:8195679-Female,
pubmed-meshheading:8195679-Humans,
pubmed-meshheading:8195679-Male,
pubmed-meshheading:8195679-Membrane Lipids,
pubmed-meshheading:8195679-Phosphatidylserines,
pubmed-meshheading:8195679-Phospholipids,
pubmed-meshheading:8195679-Reference Values,
pubmed-meshheading:8195679-Sickle Cell Trait
|
pubmed:year |
1994
|
pubmed:articleTitle |
Measurement of membrane phospholipid asymmetry in normal and sickle-cell erythrocytes by means of annexin V binding.
|
pubmed:affiliation |
Department of Laboratory Medicine, University of Washington, Seattle 98195.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|