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First published online 31 July 2007
doi: 10.1242/jcs.03480


Journal of Cell Science 120, 2851-2863 (2007)
Published by The Company of Biologists 2007
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Research Article

Reduced migration, altered matrix and enhanced TGFbeta1 signaling are signatures of mouse keratinocytes lacking Sdc1

Mary Ann Stepp1,2,*, Yueyuan Liu1, Sonali Pal-Ghosh1, Rosalyn A. Jurjus1, Gauri Tadvalkar1, Adith Sekaran1, Kristen LoSicco1, Li Jiang3, Melinda Larsen4,{ddagger}, Luowei Li5 and Stuart H. Yuspa5

1 Department of Anatomy and Cell Biology, George Washington University Medical School, Washington, DC 20037, USA
2 Department of Ophthalmology, George Washington University Medical School, Washington, DC 20037, USA
3 Institute for Biomedical Engineering, School of Engineering and Applied Science, George Washington University, Washington, DC 20037, USA
4 National Institute of Dental and Craniofacial Research/Laboratory of Cellular and Developmental Biology, National Institutes of Health, Bethesda, MD 20892, USA
5 National Cancer Institute/Laboratory of Cancer Biology and Genetics, National Institutes of Health, Bethesda, MD 20892, USA

* Author for correspondence (e-mail: mastepp{at}gwu.edu)

Accepted 12 June 2007

We have reported previously that syndecan-1 (Sdc1)-null mice show delayed re-epithelialization after skin and corneal wounding. Here, we show that primary keratinocytes obtained from Sdc1-null mice and grown for 3-5 days in culture are more proliferative, more adherent and migrate more slowly than wt keratinocytes. However, the migration rates of Sdc1-null keratinocytes can be restored to wild-type levels by replating Sdc1-null keratinocytes onto tissue culture plates coated with fibronectin and collagen I, laminin (LN)-332 or onto the matrices produced by wild-type cells. Migration rates can also be restored by treating Sdc1-null keratinocytes with antibodies that block {alpha}6 or {alpha}v integrin function, or with TGFbeta1. Antagonizing either beta1 integrin function using a function-blocking antibody or TGFbeta1 using a neutralizing antibody reduced wild-type keratinocyte migration more than Sdc1-null keratinocyte migration. Cultures of Sdc1-null keratinocytes accumulated less collagen than wild-type cultures but their matrices contained the same amount of LN-332. The Sdc1-null keratinocytes expressed similar total amounts of eight different integrin subunits but showed increased surface expression of {alpha}vbeta6, {alpha}vbeta8, and {alpha}6beta4 integrins compared with wild-type keratinocytes. Whereas wild-type keratinocytes increased their surface expression of {alpha}2beta1, {alpha}vbeta6, {alpha}vbeta8, and {alpha}6beta4 after treatment with TGFbeta1, Sdc1-null keratinocytes did not. Additional data from a dual-reporter assay and quantification of phosphorylated Smad2 show that TGFbeta1 signaling is constitutively elevated in Sdc1-null keratinocytes. Thus, our results identify TGFbeta1 signaling and Sdc1 expression as important factors regulating integrin surface expression, activity and migration in keratinocyte and provide new insight into the functions regulated by Sdc1.

Key words: Syndecan-1, Keratinocytes, Integrins


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