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Mussel adhesive protein fused with cell adhesion recognition motif triggers integrin-mediated adhesion and signaling for enhanced cell spreading, proliferation, and survival SCIE SCOPUS

Title
Mussel adhesive protein fused with cell adhesion recognition motif triggers integrin-mediated adhesion and signaling for enhanced cell spreading, proliferation, and survival
Authors
Kim, BJChoi, YSChoi, BHLim, SSong, YHCha, HJ
Date Issued
2010-09-01
Publisher
WILEY-LISS
Abstract
Adhesion of cells to a surface is a basic and important requirement in the fields of cell culture and tissue engineering. Previously, we constructed the cell adhesive, fp-151-RGD, by fusion of the hybrid mussel adhesive protein, fp-151, and GRGDSP peptide, one of the major cell adhesion recognition motifs; fp-151-RGD efficiently immobilized cells on coated culture surfaces with no protein and surface modifications, and apparently enhanced cell adhesion, proliferation, and spreading abilities. In the present study, we investigated the potential use of fp-151-RGD as a biomimetic extracellular matrix material at the molecular level by elucidating its substantial effects on integrin-mediated adhesion and signaling. Apoptosis derived from serum deprivation was significantly suppressed on the fp-151-RGD-coated surface, indicating that RGD-induced activation of integrin-mediated signaling triggers the pathway for cell survival. Analysis of the phosphorylation of focal adhesion kinase clearly demonstrated activation of focal adhesion kinase, a well-established indicator of integrin-mediated signaling, on the fp-151-RGD-coated surface, leading to significantly enhanced cell behaviors, including proliferation, spreading and survival, and consequently, more efficient cell culture. (C) 2010 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 94A: 886-892, 2010.
Keywords
mussel adhesive protein; cell adhesion recognition motif; fp-151-RGD; integrin-mediated signaling; cell adhesion material; RGD PEPTIDE; 3T3 FIBROBLASTS; MATRIX; DEATH; BIOMATERIALS; APOPTOSIS; BYSSUS; PHOSPHORYLATION; TRANSDUCTION; FIBRONECTIN
URI
https://oasis.postech.ac.kr/handle/2014.oak/25351
DOI
10.1002/JBM.A.32768
ISSN
1549-3296
Article Type
Article
Citation
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, vol. 94A, no. 3, page. 886 - 892, 2010-09-01
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차형준CHA, HYUNG JOON
Dept. of Chemical Enginrg
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