Linked Life Data

9408179

Source:http://linkedlifedata.com/resource/pubmed/id/9408179

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-1-16
pubmed:abstractText
Annexin V, VI and VII-core (delta1-107) are members of the annexin protein family and bind to acidic phospholipid membranes in a calcium dependent manner. They also show ion channel activity under certain conditions. As annexins bind peripherally to lipid membranes, ion channel formation must consist of at least two steps: An adsorption reaction regulating the binding of annexin to the membrane surface and the opening and closing of the active species controlling the channel activity. By using the baseline current through the patch clamp seal as a probe for unoccupied binding sites at the membrane, we show that the adsorption of annexins to membranes is not only calcium dependent but also strongly voltage dependent. Whereas the free transfer energies at low calcium concentrations are similar for all three annexins, the binding of annexin V becomes much tighter with higher calcium levels, compared to annexin VI and VII-core. This correlates with the finding that annexin VI and VII-core display channel activity much more often than annexin V if one assumes that a high coverage of the membrane surface with annexins stabilizes the bilayer. At higher protein concentrations weaker binding is observed in agreement with the previously reported anti-cooperativity of membrane binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
1330
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
254-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Voltage dependent binding of annexin V, annexin VI and annexin VII-core to acidic phospholipid membranes.
pubmed:affiliation
Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Martinsried, Germany. ahofmann@biochem.mpg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't