Document Detail

Promigratory and procontractile growth factor environments differentially regulate cell morphogenesis.
MedLine Citation:
PMID:  19796636     Owner:  NLM     Status:  MEDLINE    
Three-dimensional (3D) cell-matrix cultures provide a useful model to analyze and dissect the structural, functional, and mechanical aspects of cell-matrix interactions and motile behavior important for cell and tissue morphogenesis. In the current studies we tested the effects of serum and physiological growth factors on the morphogenetic behavior of human fibroblasts cultured on the surfaces of 3D collagen matrices. Fibroblasts in medium containing serum contracted into clusters, whereas cells in medium containing platelet-derived growth factor (PDGF) were observed to migrate as individuals. The clustering activity of serum appeared to depend on lysophosphatidic acid, required cell contraction based on inhibition by blocking Rho kinase or myosin II, and was reversed upon switching to PDGF. Oncogenic Ras transformed human fibroblasts did not exhibit serum-stimulated cell clustering. Our findings emphasize the importance of cell-specific promigratory and procontractile growth factor environments in the differential regulation of cell motile function and cell morphogenesis.
Sangmyung Rhee; Chin-Han Ho; Frederick Grinnell
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2009-09-29
Journal Detail:
Title:  Experimental cell research     Volume:  316     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2010 Jan 
Date Detail:
Created Date:  2009-11-30     Completed Date:  2010-01-14     Revised Date:  2014-09-22    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  232-44     Citation Subset:  IM    
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MeSH Terms
Actins / metabolism
Amides / pharmacology
Cell Aggregation / drug effects,  physiology*
Cell Culture Techniques
Cell Line, Transformed
Cell Movement / drug effects,  physiology*
Cell Shape / drug effects,  physiology*
Collagen / physiology
Enzyme Inhibitors / pharmacology
Fibroblasts / cytology*,  drug effects,  metabolism
Heterocyclic Compounds with 4 or More Rings / pharmacology
Intercellular Signaling Peptides and Proteins / pharmacology,  physiology*
Lysophospholipids / deficiency,  pharmacology
Myosin Type II / antagonists & inhibitors,  metabolism
Oncogene Protein p21(ras) / genetics
Platelet-Derived Growth Factor / pharmacology
Pyridines / pharmacology
Serum / physiology
Sphingosine / analogs & derivatives,  pharmacology
Vinculin / metabolism
rho-Associated Kinases / antagonists & inhibitors,  metabolism
Grant Support
Reg. No./Substance:
0/Actins; 0/Amides; 0/Enzyme Inhibitors; 0/Heterocyclic Compounds with 4 or More Rings; 0/Intercellular Signaling Peptides and Proteins; 0/Lysophospholipids; 0/Platelet-Derived Growth Factor; 0/Pyridines; 0/blebbistatin; 125361-02-6/Vinculin; 138381-45-0/Y 27632; 22002-87-5/lysophosphatidic acid; 26993-30-6/sphingosine 1-phosphate; 9007-34-5/Collagen; EC Kinases; EC 3.6.1.-/Myosin Type II; EC Protein p21(ras); NGZ37HRE42/Sphingosine

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

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