Document Detail


Protein kinase C affects reformation of endothelial junctions in xenopus XTH-2 cells.
MedLine Citation:
PMID:  10527549     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Endothelial cells can reversibly be forced to suppress the formation of endothelial junctions (EJ) by cultivation in a low calcium medium. The authors localized vinculin and cadherin as marker proteins of EJ and actin as a cytoskeletal component by fluorescence microscopy, and used this cell model to study the reformation of endothelial junctions under conditions of activation and inhibition of protein kinase C (PKC). Inhibition of PKC by H-7 leads to an acceleration of EJ reformation, while constitutive activation by TPA inhibits the reformation process.
Authors:
N S Werner; R Meyer; F Achenbach
Related Documents :
23467079 - An in vitro model for the evaluation of the adhesion of solid oral dosage forms to the ...
14598099 - A novel diaphragm-to-housing junction adhesive method: alumina ball milling.
16783819 - Junctional adhesion molecule-a regulates cell migration and resistance to shear stress.
19258599 - Regulated release and functional modulation of junctional adhesion molecule a by disint...
12901789 - Nectins and nectin-like molecules: roles in cell adhesion, migration, and polarization.
11053409 - Jam-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lympha...
21698469 - Vegf-c differentially regulates vegf-a expression in ocular and cancer cells; promotes ...
12415009 - Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the...
22988499 - Rgd-dependent epithelial cell-matrix interactions in the human intestinal crypt.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Cell biology international     Volume:  23     ISSN:  1065-6995     ISO Abbreviation:  Cell Biol. Int.     Publication Date:  1999  
Date Detail:
Created Date:  2000-04-04     Completed Date:  2000-04-04     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  9307129     Medline TA:  Cell Biol Int     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  73-80     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Affiliation:
Innere Klinik und Poliklinik (Tumorforschung), Universitätsklinikum Essen, Hufelandstr. 55, Essen, D-45122, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine / pharmacology
Animals
Cadherins / physiology
Cell Line
Endothelium, Vascular / cytology*,  physiology*
Enzyme Activation / physiology
Enzyme Inhibitors / pharmacology
Intercellular Junctions / physiology*
Phorbol Esters / pharmacology
Protein Kinase C / physiology*
Signal Transduction
Vinculin / physiology
Xenopus
Chemical
Reg. No./Substance:
0/Cadherins; 0/Enzyme Inhibitors; 0/Phorbol Esters; 125361-02-6/Vinculin; 84477-87-2/1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; EC 2.7.11.13/Protein Kinase C

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Lovastatin induces mitotic abnormalities in various cell lines.
Next Document:  Protein domains involved in nuclear transport of Fos.