Linked Life Data

11512023

Source:http://linkedlifedata.com/resource/pubmed/id/11512023

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-8-20
pubmed:abstractText
Clostridium botulinum C2 toxin (C2 toxin) and purified ADP-ribosylated-alpha-actin (ADP-r-alpha-actin) cause specific actin depolymerisation in living cells. This effect was used to investigate the actin microfilament system with particular emphasis on cell-cell adhesion and plasma membrane integrity in endothelial cells. C2 toxin caused time- and dose-dependent (15-100 ng/ml) changes in endothelial surface morphology (investigated by atomic force microscopy), intercellular gap formation and cell detachment under shear stress. Low concentrations of C2 toxin (1.5 ng/ml), however, did not induce cell detachment but inhibited shear stress-dependent cell alignment. Gap formation as well as cell loss under shear stress was also observed in cells microinjected with purified ADP-r-alpha-actin. Intercellular gap formation was mediated by increased alpha-catenin solubility (40%) due to actin filament depolymerisation. Disintegration of plasma membranes (measured by LDH release) and cell fragmentation during simultaneous exposure to shear stress and C2 toxin were due to a loss of more than 50% of membrane-associated actin. These data show that small disturbances in actin dynamics inhibit shear stress-dependent cell alignment; that depolymerisation of actin filaments increases the solubility of alpha-catenin, thus resulting in cell dissociation and that actin filaments of the membrane cytoskeleton are required to protect the cells from haemodynamic injury such as shear stress. Together, the study shows a heterogeneous regulation of actin filament dynamics at subcellular locations. Junction-associated actin filaments displayed the highest sensitivity whereas stress fibres were far more stable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0031-6768
pubmed:author
pubmed:issnType
Print
pubmed:volume
442
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
675-87
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11512023-Actin Cytoskeleton, pubmed-meshheading:11512023-Actins, pubmed-meshheading:11512023-Animals, pubmed-meshheading:11512023-Botulinum Toxins, pubmed-meshheading:11512023-Cadherins, pubmed-meshheading:11512023-Cell Adhesion, pubmed-meshheading:11512023-Cell Fractionation, pubmed-meshheading:11512023-Cell Membrane, pubmed-meshheading:11512023-Cell Surface Extensions, pubmed-meshheading:11512023-Cells, Cultured, pubmed-meshheading:11512023-Cytoskeletal Proteins, pubmed-meshheading:11512023-Endothelium, Vascular, pubmed-meshheading:11512023-Immunoblotting, pubmed-meshheading:11512023-Intercellular Junctions, pubmed-meshheading:11512023-Microinjections, pubmed-meshheading:11512023-Microscopy, Atomic Force, pubmed-meshheading:11512023-Poly(ADP-ribose) Polymerases, pubmed-meshheading:11512023-Polymers, pubmed-meshheading:11512023-Stress, Mechanical, pubmed-meshheading:11512023-Swine, pubmed-meshheading:11512023-alpha Catenin
pubmed:year
2001
pubmed:articleTitle
Role of actin filaments in endothelial cell-cell adhesion and membrane stability under fluid shear stress.
pubmed:affiliation
Institut für Physiologie, TU-Dresden, Fiedlerstrasse 42, 01307 Dresden, Germany. Hans.Schnittler@mailbox.TU-Dresden.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't