Linked Life Data

9268696

Source:http://linkedlifedata.com/resource/pubmed/id/9268696

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-9-15
pubmed:abstractText
In HaCaT keratinocytes bradykinin-triggered actin reorganization was inhibited by quinacrine, a phospholipase A2 inhibitor, and restored by addition of arachidonic acid. Bradykinin-induced actin breakdown and cortical actin formation were respectively prevented by indomethacin, a cyclooxygenase inhibitor, and nordihydroguaiaretic acid, a lipoxygenase inhibitor. Addition of prostaglandins or leukotrienes, respectively, reversed the effects of inhibitors. This suggested a crucial role for a cyclooxygenase product in actin depolymerization and for a lipoxygenase product in cortical actin formation. Furthermore, we found that bradykinin stimulated HaCaT keratinocyte migration. This event was blocked by quinacrine, indomethacin or nordihydroguaiaretic acid, and restored by addition of prostaglandins or leukotrienes, respectively. We also showed that genistein, a tyrosine kinase inhibitor, inhibited HaCaT cell locomotion. In conclusion, bradykinin modulated actin reorganization and cell motility in keratinocytes, probably by a mechanism involving arachidonic acid metabolites and a tyrosine kinase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
237
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
257-61
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Bradykinin induces actin reorganization and enhances cell motility in HaCaT keratinocytes.
pubmed:affiliation
Department of General Dermatology, NOVARTIS Research Institute, Brunner Strasse 59, Vienna, A-1235, Austria.
pubmed:publicationType
Journal Article