Linked Life Data

11129983

Source:http://linkedlifedata.com/resource/pubmed/id/11129983

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-12-20
pubmed:abstractText
P-glycoprotein (P-gp) acts as an active efflux mechanism for a large number of cytostatics and seems to be involved in the frequent failure of cancer chemotherapy. The molecular events of substrate recognition and transport still are not understood completely. We show here that the percentage of P-gp epitopes available for labeling with UIC2 monoclonal antibody is increased significantly after methanol permeabilization/fixation of cells. At the same time, binding of the MRK16 and 4E3 anti-P-gp antibodies is changed only moderately. Confocal microscopical images of UIC2-PE-labeled cells show that the epitopes becoming available after fixation are situated mainly in the plasma membrane. Thus, only a minority of P-gp molecules are accessible for UIC2 in the cell membrane of live cells, and methanol treatment can expose a large pool of previously plasma membrane-embedded, cryptic UIC2 epitopes. The UIC2-reactive P-gp molecules do not appear to be sequestered spatially, as suggested by the high fluorescence resonance energy transfer efficiency measured between the fluorescently labeled competing UIC2 and MRK16 antibodies, suggestive of P-gp dimerization and oligomerization on live cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0361-090X
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
415-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Conformational heterogeneity of P-glycoprotein.
pubmed:affiliation
Department of Biophysics and Cell Biology, University Medical School of Debrecen, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't