Document Detail


Regulation of cell adhesion signaling by synthetic glycopolymer matrix in primary cultured hepatocyte.
MedLine Citation:
PMID:  14572665     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Control of cell-matrix interactions is a central principle for the design of biomaterial in tissue engineering. In this study, we evaluated a synthetic glycopolymer, which is recognized by the asialoglycoprotein receptor (ASGPR) expressed on the surface of hepatocytes, as an artificial matrix to regulate integrin-mediated signaling. The phosphorylation of focal adhesion kinase was restricted in hepatocytes cultured on the glycopolymer compared with fibronectin. In addition, there was no reorganization of cytoskeleton-related proteins such as actin filaments, microtubules, and vinculin in hepatocytes cultured on the glycopolymer. DNA synthesis and cyclin D1 expression were suppressed in hepatocytes grown on the glycopolymer as compared with those grown on fibronectin and collagen. The data suggest that the glycopolymer will be a good artificial matrix to regulate integrin-mediated signaling and cell growth through the unique ASGPR-carbohydrate interaction.
Authors:
Sang-Heon Kim; Jong-Hun Kim; Toshihiro Akaike
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  553     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2003 Oct 
Date Detail:
Created Date:  2003-10-23     Completed Date:  2003-12-09     Revised Date:  2012-06-05    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  433-9     Citation Subset:  IM    
Affiliation:
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, 226-8501 Yokohama, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Asialoglycoprotein Receptor / metabolism
Cell Adhesion / drug effects,  physiology*
Cell Cycle / drug effects,  physiology
Collagen / pharmacology
Cyclin D1 / biosynthesis,  drug effects
Cytoskeletal Proteins / analysis,  metabolism
DNA / biosynthesis,  drug effects
Extracellular Matrix / metabolism
Fibronectins / pharmacology
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
Focal Adhesions / drug effects,  metabolism
Hepatocytes / cytology,  drug effects,  metabolism,  physiology*
Integrins / antagonists & inhibitors,  metabolism
Male
Mice
Mice, Inbred ICR
Phosphorylation
Polystyrenes / chemistry,  pharmacology*
Protein-Tyrosine Kinases / metabolism
Signal Transduction / physiology
Chemical
Reg. No./Substance:
0/Asialoglycoprotein Receptor; 0/Cytoskeletal Proteins; 0/Fibronectins; 0/Integrins; 0/Polystyrenes; 136601-57-5/Cyclin D1; 9007-34-5/Collagen; 9007-49-2/DNA; EC 2.7.10.1/Focal Adhesion Kinase 1; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.2/Focal Adhesion Protein-Tyrosine Kinases; EC 2.7.10.2/Ptk2 protein, mouse

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


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