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      bFGF Regulates PI3-Kinase-Rac1-JNK Pathway and Promotes Fibroblast Migration in Wound Healing

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          Abstract

          Fibroblast proliferation and migration play important roles in wound healing. bFGF is known to promote both fibroblast proliferation and migration during the process of wound healing. However, the signal transduction of bFGF-induced fibroblast migration is still unclear, because bFGF can affect both proliferation and migration. Herein, we investigated the effect of bFGF on fibroblast migration regardless of its effect on fibroblast proliferation. We noticed involvement of the small GTPases of the Rho family, PI3-kinase, and JNK. bFGF activated RhoA, Rac1, PI3-kinase, and JNK in cultured fibroblasts. Inhibition of RhoA did not block bFGF-induced fibroblast migration, whereas inhibition of Rac1, PI3-kinase, or JNK blocked the fibroblast migration significantly. PI3-kinase-inhibited cells down-regulated the activities of Rac1 and JNK, and Rac1-inhibited cells down-regulated JNK activity, suggesting that PI3-kinase is upstream of Rac1 and that JNK is downstream of Rac1. Thus, we concluded that PI3-kinase, Rac1, and JNK were essential for bFGF-induced fibroblast migration, which is a novel pathway of bFGF-induced cell migration.

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          Integrin signaling.

          E Ruoslahti, F R Giancotti, ZHANG YUEGANG (1999)
          Cells reside in a protein network, the extracellular matrix (ECM), which they secrete and mold into the intercellular space. The ECM exerts profound control over cells. The effects of the matrix are primarily mediated by integrins, a family of cell surface receptors that attach cells to the matrix and mediate mechanical and chemical signals from it. These signals regulate the activities of cytoplasmic kinases, growth factor receptors, and ion channels and control the organization of the intracellular actin cytoskeleton. Many integrin signals converge on cell cycle regulation, directing cells to live or die, to proliferate, or to exit the cell cycle and differentiate.
          Article 0 comments Cited 337 times – based on 0 reviews     Review now
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            Rho GTPases Control Polarity, Protrusion, and Adhesion during Cell Movement

            Catherine Nobes, Alan Hall (1999)
            Cell movement is essential during embryogenesis to establish tissue patterns and to drive morphogenetic pathways and in the adult for tissue repair and to direct cells to sites of infection. Animal cells move by crawling and the driving force is derived primarily from the coordinated assembly and disassembly of actin filaments. The small GTPases, Rho, Rac, and Cdc42, regulate the organization of actin filaments and we have analyzed their contributions to the movement of primary embryo fibroblasts in an in vitro wound healing assay. Rac is essential for the protrusion of lamellipodia and for forward movement. Cdc42 is required to maintain cell polarity, which includes the localization of lamellipodial activity to the leading edge and the reorientation of the Golgi apparatus in the direction of movement. Rho is required to maintain cell adhesion during movement, but stress fibers and focal adhesions are not required. Finally, Ras regulates focal adhesion and stress fiber turnover and this is essential for cell movement. We conclude that the signal transduction pathways controlled by the four small GTPases, Rho, Rac, Cdc42, and Ras, cooperate to promote cell movement.
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              The lamellipodium: where motility begins

              J.Victor Small, Theresia Stradal, Emmanuel Vignal … (2002)
              Lamellipodia, filopodia and membrane ruffles are essential for cell motility, the organization of membrane domains, phagocytosis and the development of substrate adhesions. Their formation relies on the regulated recruitment of molecular scaffolds to their tips (to harness and localize actin polymerization), coupled to the coordinated organization of actin filaments into lamella networks and bundled arrays. Their turnover requires further molecular complexes for the disassembly and recycling of lamellipodium components. Here, we give a spatial inventory of the many molecular players in this dynamic domain of the actin cytoskeleton in order to highlight the open questions and the challenges ahead.
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                Author and article information

                Contributors
                : Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2010
                Publication date (Electronic): 17 August 2010
                Volume: 5
                Issue: 8
                Electronic Location Identifier: e12228
                Affiliations
                [1 ]Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan
                [2 ]Department of Anatomy and Neuroscience, Osaka University Graduate School of Medicine, Osaka, Japan
                University of Birmingham, United Kingdom
                Author notes

                Conceived and designed the experiments: SK TK. Performed the experiments: SK TF TK. Analyzed the data: SK TF SM KS MT SM TK. Contributed reagents/materials/analysis tools: SK TF SM KS MT SM MT YS KY KH TK. Wrote the paper: SK TK.

                Article
                Publisher ID: 10-PONE-RA-17130R2
                DOI: 10.1371/journal.pone.0012228
                PMC ID: 2923192
                PubMed ID: 20808927
                SO-VID: 565d2a8a-87a4-4df1-864b-4489a9a1de54
                Copyright © Kanazawa et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                Date received : 15 March 2010
                Date accepted : 25 July 2010
                Page count
                Pages: 12
                Categories
                Subject: Research Article
                Subject: Dermatology
                Subject: Cell Biology/Cell Signaling
                Subject: Cell Biology/Cytoskeleton

                ScienceOpen disciplines: Uncategorized
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                ScienceOpen disciplines: Uncategorized

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