Document Detail


L-selectin regulates actin polymerisation via activation of the small G-protein Rac2.
MedLine Citation:
PMID:  9070897     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
L-selectin mediated adhesion to endothelial cells is a crucial step in the immune response to pathogens (1, 2) and in lymphocyte homing (3, 4). Selectin molecules mediate leukocyte rolling on endothelial cells, the initial step of adhesion (5, 6). We have previously shown that stimulation of Jurkat T-lymphocytes via L-selectin results in activation of the p21Ras pathway and synthesis of reactive oxygen intermediates (7). Here, we show that cellular stimulation via L-selectin induces a change of cytoskeleton organisation demonstrated by a tenfold increase of actin filament polymerisation. This actin polymerisation is mediated by a Ras and Rac2 regulated pathway, since inhibition of Ras by transient transfection of transdominant inhibitory N17Ras or suppression of Rac2 protein expression by antisense oligonucleotides prevents L-selectin triggered actin polymerisation. Our results point to a signaling cascade from L-selectin via Ras and Rac2 to actin filaments, which might be important for leukocyte adhesion.
Authors:
B Brenner; E Gulbins; G L Busch; U Koppenhoefer; F Lang; O Linderkamp
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  231     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1997 Feb 
Date Detail:
Created Date:  1997-04-16     Completed Date:  1997-04-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  802-7     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, University of Heidelberg, Germany.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Enzyme Activation
GTP-Binding Proteins / metabolism*
Guanosine Triphosphate / metabolism
Humans
L-Selectin / metabolism*
Microfilaments / ultrastructure*
Polymers
Protein Binding
Proto-Oncogene Proteins p21(ras) / metabolism*
Tumor Cells, Cultured
rac GTP-Binding Proteins
Chemical
Reg. No./Substance:
0/Actins; 0/Polymers; 126880-86-2/L-Selectin; 86-01-1/Guanosine Triphosphate; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.5.2/HRAS protein, human; EC 3.6.5.2/Proto-Oncogene Proteins p21(ras); EC 3.6.5.2/rac GTP-Binding Proteins

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


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