Document Detail

Activation of formyl peptide receptor-1 enhances restitution of human retinal pigment epithelial cell monolayer under electric fields.
MedLine Citation:
PMID:  21228377     Owner:  NLM     Status:  MEDLINE    
PURPOSE: This study aimed at identifying the expression of functional formyl peptide receptor (FPR)-1 in human retinal pigment epithelium (hRPE) cells and to evaluate the role of FPR in regulation of wound closure of the hRPE monolayer under electric fields (EFs).
METHODS: The expression of FPR in hRPE cells was analyzed with an immunofluoresence labeling assay and RT-PCR. Cultured wounded hRPE monolayers were exposed to EFs with free serum, 20%, serum, and a classical FPR agonist, N-formyl-Met-Leu-Phe (fMLF), respectively, for 3 hours. Cell monolayer migrations were traced using an image analyzer. Expressions of cell junction molecules were measured by RT-PCR, and the ultrastructure of cell junctions was observed with transmission electron microscopy (TEM).
RESULTS: The expression of functional FPR was observed and localized along actin filaments in cellular lamellipodia and filopodia. EFs and fMLF significantly increased the migration rates of the wounded RPE monolayer. The migrating distances of monolayers were 24.262 ± 6.82 μm, 40.243 ± 5.069 μm, and 56.926 ± 7.821 μm in cells with free serum, 20% serum, and fMLF under EFs at 3 hours, respectively (P < 0.01). The mRNA expressions of connexin 43(Cx43) and zonula occludens (ZO)-1 were detected in hRPE cells. TEM revealed that cell junctions formed between hRPE cells in the monolayer.
CONCLUSIONS: These results showed for the first time that functional FPR expresses in hRPE cells and that activation of FPR enhances migration of the wounded hRPE monolayer. The mRNA expressions and ultrastructures of cell junctions further demonstrated the RPE sheet as a monolayer migrating under EFs.
Xiao-Guang Zhang; Yan-Nian Hui; Xiao-Feng Huang; Hong-Jun Du; Jian Zhou; Ji-Xian Ma
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-05-16
Journal Detail:
Title:  Investigative ophthalmology & visual science     Volume:  52     ISSN:  1552-5783     ISO Abbreviation:  Invest. Ophthalmol. Vis. Sci.     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-05-17     Completed Date:  2011-07-26     Revised Date:  2013-01-09    
Medline Journal Info:
Nlm Unique ID:  7703701     Medline TA:  Invest Ophthalmol Vis Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3160-5     Citation Subset:  IM    
Department of Ophthalmology, Xijing Hospital, Fourth Military Medical University, Xi'an, China
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MeSH Terms
Actins / metabolism
Cadherins / genetics
Cell Movement / physiology*
Cells, Cultured
Connexin 43 / genetics
Electromagnetic Fields
Fluorescent Antibody Technique, Indirect
Gene Expression Regulation / physiology
Membrane Proteins / genetics
Microscopy, Electron, Transmission
Phosphoproteins / genetics
RNA, Messenger / metabolism
Receptors, Formyl Peptide / genetics,  metabolism*
Retinal Pigment Epithelium / metabolism*
Reverse Transcriptase Polymerase Chain Reaction
Tissue Donors
Wound Healing / physiology*
Zonula Occludens-1 Protein
Reg. No./Substance:
0/Actins; 0/Cadherins; 0/Connexin 43; 0/FPR1 protein, human; 0/GJA1 protein, human; 0/Membrane Proteins; 0/Phosphoproteins; 0/RNA, Messenger; 0/Receptors, Formyl Peptide; 0/TJP1 protein, human; 0/Zonula Occludens-1 Protein

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

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