HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mukoyama, Y. Articles by Matsuyoshi, N. Search for Related Content PubMed Articles by Mukoyama, Y. Articles by Matsuyoshi, N.

¹ Department of Dermatology, Graduate School of Medicine, Kyoto University, 54 kawahara-cho, Shogo-in, Sakyo-ku, Kyoto 606-8317, Japan
² Drug Discovery Research, Research Laboratories, Kyoto R&D Center, Maruho Co., Ltd., 92 Awata-cho, Chudoji, Shimogyo-ku, Kyoto 600-8815, Japan
³ Life Sciences, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

T-cadherin is a glycosyl-phosphatidylinositol (GPI) anchored cadherin molecule. We previously reported that T-cadherin is normally expressed on the basal keratinocytes of the epidermis and is down-regulated in cutaneous squamous cell carcinoma (SCC). We found that expression of T-cadherin in cutaneous squamous carcinoma cells regulated level of surface ß1 integrin, which functioned as extracellular matrix (ECM) receptor. Involvement of T-cadherin in ß1 integrin trafficking was studied using three different stable cell lines with cytomegalovirus (CMV)-driven over-expression, tetracycline (Tet)-inducible expression and RNAi-mediated suppressed expression of T-cadherin. Pulse–chase analysis using a cholesterol-depleting reagent and a tyrosine kinase inhibitor showed that ß1 integrin mainly internalized via caveolae. Over-expression of T-cadherin suppressed the internalization of both ß1 integrin and cholera toxin (CTX), a marker of caveolae-mediated endocytosis. By Western blot analysis of tyrosine-kinase target molecules, we demonstrated a reduced level of EGF receptor (EGFR)-phosphorylation in T-cadherin over-expressing cells. In addition, studies using EGF and EGFR specific inhibitors revealed that EGFR activation stimulated ß1 integrin internalization. Taking these results together, T-cadherin may modulate cell–matrix adhesion in basal keratinocytes as well as invasive potency in SCC by regulating surface level of ß1 integrin.

^* Correspondence: E-mail: mukoyama_bux{at}mii.maruho.co.jp

This article has been cited by other articles:

				E. V. Vassilieva, K. Gerner-Smidt, A. I. Ivanov, and A. Nusrat Lipid rafts mediate internalization of {beta}1-integrin in migrating intestinal epithelial cells Am J Physiol Gastrointest Liver Physiol, November 1, 2008; 295(5): G965 - G976. [Abstract] [Full Text] [PDF]

				M. Philippova, D. Ivanov, M. B. Joshi, E. Kyriakakis, K. Rupp, T. Afonyushkin, V. Bochkov, P. Erne, and T. J. Resink Identification of Proteins Associating with Glycosylphosphatidylinositol- Anchored T-Cadherin on the Surface of Vascular Endothelial Cells: Role for Grp78/BiP in T-Cadherin-Dependent Cell Survival Mol. Cell. Biol., June 15, 2008; 28(12): 4004 - 4017. [Abstract] [Full Text] [PDF]