Document Detail


Lysophosphatidylcholine-mediated functional inactivation of syndecan-4 results in decreased adhesion and motility of dendritic cells.
MedLine Citation:
PMID:  20607801     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Following antigen contact, maturation and migration of DCs into lymphatic tissues are crucial to the developing immune response or maintenance of tolerance. Lysophosphatidylcholine (LysoPC) is generated during apoptosis of cells and acts as a "find-and-eat-me" signal thought to prevent autoimmunity. Moreover, LysoPC can activate PKCδ and initiates a signaling cascade that leads to phosphorylation and inactivation of syndecan-4 (SDC4), a heparansulfate proteoglycan integrin co-receptor. In human monocyte-derived DCs, we recently demonstrated that SDC4 is upregulated during maturation thereby stimulating DC motility. Here, we investigate the effects of LysoPC on DC motility as well as on the involvement of PKCδ phosphorylation-dependent regulation of DC motility by SDC4 and PKCα. Employing a static adhesion assay and videomicroscopy, we show that LysoPC inhibits adhesion of DCs to fibronectin and motility of DCs by decreasing podosome formation. Moreover, DC podosome formation and motility, which both are regulated by SDC4 and subject to control by PKCδ-dependent phosphorylation of SDC4, were inhibited in LysoPC-matured DCs. Thus, these DC are defective in adhesion and migration. Based on our results, we hypothesize that LysoPC released during apoptosis might delay DC migration to lymphoid organs and thus prevent autoimmunity.
Authors:
Johannes Bühligen; Mirko Himmel; Carl Gebhardt; Jan C Simon; Wolfgang Ziegler; Marco Averbeck
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cellular physiology     Volume:  225     ISSN:  1097-4652     ISO Abbreviation:  J. Cell. Physiol.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-09-15     Completed Date:  2010-10-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0050222     Medline TA:  J Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  905-14     Citation Subset:  IM    
Copyright Information:
© 2010 Wiley-Liss, Inc.
Affiliation:
Department of Dermatology, Venerology and Allergology, Universitätsklinikum Leipzig, Leipzig, Germany.
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MeSH Terms
Descriptor/Qualifier:
Antigens, CD86 / metabolism
Apoptosis
Autoimmunity
Cell Adhesion*
Cell Movement*
Cell Surface Extensions / metabolism
Cells, Cultured
Dendritic Cells / immunology,  metabolism*
Fibronectins / metabolism
HLA-DR Antigens / metabolism
Humans
Intracellular Signaling Peptides and Proteins / metabolism
Lysophosphatidylcholines / metabolism*
Membrane Proteins / metabolism
Microscopy, Video
Phosphorylation
Protein Kinase C-alpha / metabolism
Protein Kinase C-delta / metabolism
Syndecan-4 / metabolism*
Chemical
Reg. No./Substance:
0/Antigens, CD86; 0/CD86 protein, human; 0/Fibronectins; 0/HLA-DR Antigens; 0/Intracellular Signaling Peptides and Proteins; 0/Lysophosphatidylcholines; 0/Membrane Proteins; 0/SDC4 protein, human; 0/Syndecan-4; 125267-21-2/myristoylated alanine-rich C kinase substrate; EC 2.7.1.37/PRKCA protein, human; EC 2.7.1.37/PRKCD protein, human; EC 2.7.11.13/Protein Kinase C-alpha; EC 2.7.11.13/Protein Kinase C-delta

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