Linked Life Data

8155663

Source:http://linkedlifedata.com/resource/pubmed/id/8155663

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-5-19
pubmed:abstractText
The mechanism of vesicle formation as well as the precise reasons for their stability are not known. Thus, it is necessary to simulate the process in vitro for studying its mechanism. If phospholipids are suspended in physiological solution by means of cholate and the detergent is then removed by dialysis, the phospholipids self-assemble to form unilamellar vesicles. We report here that the addition of Na,K-ATPase (an integral membrane protein) to the phospholipids changes the vesicle structure, they become larger and a multilamellar population appears. By contrast, carboxyfluorescein, a compound commonly used for labelling the aqueous vesicle compartment, produces an unexpected effect on vesicle structure by inducing complex, tore-like intravesicular multilayer formations associated with a 5-fold increase in diameter. Thus, the presence of a protein in the membrane phase or of a compound in the water phase can influence and direct vesicle formation in vitro; these model systems might give some clues to possible physicochemical or biological factors governing the formation of natural membrane structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
1191
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Na,K-ATPase and carboxyfluorescein distinctly alter vesicle formation in vitro.
pubmed:affiliation
Laboratory of Experimental Cell Therapeutics, University of Geneva Medical School, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't